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Conserved domains on  [gi|392926054|ref|NP_508923|]
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oleoyl-[acyl-carrier-protein] hydrolase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
6987-7412 4.74e-160

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


:

Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 504.70  E-value: 4.74e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6987 FTEPALLL----STNTVSYSDLAEKIENISKDIQKQLQIakatsvrEDELVGLDC---KNSYFALLACVFLGLPYAPIDP 7059
Cdd:cd17654     1 PDRPALIIdqttSDTTVSYADLAEKISNLSNFLRKKFQT-------EERAIGLRCdrgTESPVAILAILFLGAAYAPIDP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7060 TWPEPRQLFVKSK--VSFTLENCFSCNLKL------RNFNSRTQFGSIYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQ 7131
Cdd:cd17654    74 ASPEQRSLTVMKKchVSYLLQNKELDNAPLsftpehRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7132 CM-FRSNIRVLDSVKqVFDVSVSNIIGSVLNGGVLISSEHS--------TTITDQLQKCQYAFLPAAVFNGFTDK----- 7197
Cdd:cd17654   154 FNiTSEDILFLTSPL-TFDPSVVEIFLSLSSGATLLIVPTSvkvlpsklADILFKRHRITVLQATPTLFRRFGSQsikst 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7198 TMSRLESIETLTIGGE-TVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKCKV--STLNIGSALGDsLSNETCTICN 7274
Cdd:cd17654   233 VLSATSSLRVLALGGEpFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEedSPVQLGSPLLG-TVIEVRDQNG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7275 NSVRGNVQVKGISlaRGYITSAPHGTPFSDIYSTGDIVDSKLNSLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQI 7354
Cdd:cd17654   312 SEGTGQVFLGGLN--RVCILDDEVTVPKGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESC 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7355 VVLYSN-QMLIAFIVDQ-KSKLLHDSLVKTLKNRTQIPDYFVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17654   390 AVTLSDqQRLIAFIVGEsSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
5256-6071 1.56e-153

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 519.04  E-value: 1.56e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5256 DDTRVAVIGWSAEFSGSSNIHEYWENLMDGICSTG--------NNKYL-----------------LKNPFGFDNKFFNLT 5310
Cdd:COG3321     2 ADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITevpadrwdADAYYdpdpdapgktyvrwggfLDDVDEFDALFFGIS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5311 DEDARVLDPQVRKFIQHAYLALENSGYVKQK-HELRCGVFAGAEPSDYGR--ADDHDDAMRKLFVMNMNSYLASYASYCL 5387
Cdd:COG3321    82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESlAGSRTGVFVGASSNDYALllLADPEAIDAYALTGNAKSVLAGRISYKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5388 DLKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGFDDQKktMFSKSGVCRPFDKDSEGIVRGS 5467
Cdd:COG3321   162 DLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGG--MLSPDGRCRAFDADADGYVRGE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5468 GVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRaSFMAPNPAGQLKCMTDVLARFtNKEKERISFVECHATGTTLGD 5547
Cdd:COG3321   240 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADA-GVDPATVDYVEAHGTGTPLGD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5548 TIEMNSLRTAY----SFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSE------FrDGMGqfFTVN 5617
Cdd:COG3321   318 PIEAAALTAAFgqgrPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETpnphidF-ENSP--FYVN 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5618 GKKSTISQNS---LISIDSFGIGGTNVHMVIE-FPARSQEVVKISSENLILydmiPISAKTEYSLDHTSEAISKYLQTDT 5693
Cdd:COG3321   395 TELRPWPAGGgprRAGVSSFGFGGTNAHVVLEeAPAAAPAAAAAARPPQLL----VLSAKTEEALRALAARLAAFLEAHP 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5694 NK-IAQCSSTFIHSRVPMDSRTYLSVNNNNELL---------KIRTNKKTWFNGKSPKIALFFAPQGIQFTNILPNEYLK 5763
Cdd:COG3321   471 DLdLADVAYTLATGRAHFEHRLAVVASSREELAaklralaagEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYET 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5764 NSAYRREVEYLCELASSFGIPSLEGILYPTKNfDHLIHATQFAQIAIFVQCMAIFKAIKNV-FNPTCLIGHSVGEYAAAV 5842
Cdd:COG3321   551 EPVFRAALDECDALLRPHLGWSLREVLFPDEE-ESRLDRTEVAQPALFAVEYALARLWRSWgVRPDAVIGHSVGEYAAAC 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5843 ISGALKTEEALKLLIKRSELIGKTEKA-RMLMVWNYEKQ----LPSHVHVS-AIIDANTKCVV-GPVETIDNLEKYFINN 5915
Cdd:COG3321   630 VAGVLSLEDALRLVAARGRLMQALPGGgAMLAVGLSEEEvealLAGYDGVSiAAVNGPRSTVVsGPAEAVEALAARLEAR 709
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5916 HIKYRNIETKHGFHSKMFHCISKEFEFFCESFATKVPLIPMISSITGSEIK--IFDSKYCTMHLTNPVNLELVVDHIMKL 5993
Cdd:COG3321   710 GIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTgeALDADYWVRHLRQPVRFADAVEALLAD 789
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5994 DIDIIVEVGPTGVLSNLL---AKRNSKIVVVPTCGTKKHPKISLGECIGQLWSNGVDI--RKLTPKLA---VDgqVPGYC 6065
Cdd:COG3321   790 GVRVFLEVGPGPVLTGLVrqcLAAAGDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVdwSALYPGRGrrrVP--LPTYP 867

                  ....*.
gi 392926054 6066 FdERQF 6071
Cdd:COG3321   868 F-QRED 872
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
1889-2282 5.41e-122

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


:

Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 394.23  E-value: 5.41e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1889 NPIGVMAAACRLPGGVSsPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYG-NPVEGGNFItQDVTQFDPSFFKISK 1967
Cdd:cd00833     1 EPIAIVGMACRFPGAAD-PDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGkTYTRRGGFL-DDVDAFDAAFFGISP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1968 SEAELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYQDMMESSSIL----AMLGSMAAVIAGRVNYIFG 2039
Cdd:cd00833    79 REAEAMDPQQRLLLEVAWEALEDAGYspesLAGSRTGVFVGASSSDYLELLARDPDEidayAATGTSRAFLANRISYFFD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2040 CYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDGCV 2119
Cdd:cd00833   159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2120 VLMLelaKP-------NFHYMSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS---PSlAIDYWEAHGTGTPLGDP 2189
Cdd:cd00833   239 VVVL---KRlsdalrdGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAgvdPS-DIDYVEAHGTGTPLGDP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2190 IEFNTLSSIL-------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDINAGSIRLPIIGEDS 2262
Cdd:cd00833   315 IEVEALAKVFggsrsadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEAR 394
                         410       420
                  ....*....|....*....|....*.
gi 392926054 2263 ELVS------AGISSFGVSGTNAAAI 2282
Cdd:cd00833   395 PWPApagprrAGVSSFGFGGTNAHVI 420
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
13-394 9.44e-106

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


:

Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 347.24  E-value: 9.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   13 PNGEDGHEMAENIFLNRNNIALLPVEKNYLSDFREKHPE------VKAALVDGIEYFDDQYFGTGESEAICMDPQQRMLM 86
Cdd:cd00833    13 PGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytRRGGFLDDVDAFDAAFFGISPREAEAMDPQQRLLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   87 QGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLL-----PPDQYMATGNSASVMCGRITYFLNSRGAAVGIETACSS 161
Cdd:cd00833    93 EVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLardpdEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSS 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  162 SLVAFHLARQAIQSGETKLALVCGANHVGS-RSFHSLYNSHMVSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENN 240
Cdd:cd00833   173 SLVALHLACQSLRSGECDLALVGGVNLILSpDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  241 LLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSDIRVMS 318
Cdd:cd00833   253 DRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARagVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQ 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  319 P------KSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEME-------LNRVAISSYGF 385
Cdd:cd00833   333 PlligsvKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARpwpapagPRRAGVSSFGF 412

                  ....*....
gi 392926054  386 GGTNACAII 394
Cdd:cd00833   413 GGTNAHVIL 421
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
4290-4628 2.55e-93

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


:

Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 311.41  E-value: 2.55e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4290 ALLDSDARyWDPEYFGIRPSEAKFIDPQQRLLL-CSVAKLLDS-LLITSLT-SNTGVFIGCSANEFSHIVyAYGYKDPRA 4366
Cdd:cd00833    61 GFLDDVDA-FDAAFFGISPREAEAMDPQQRLLLeVAWEALEDAgYSPESLAgSRTGVFVGASSSDYLELL-ARDPDEIDA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4367 EWSGGTSNSALAGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKM-TVD 4445
Cdd:cd00833   139 YAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMlSPD 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4446 DFCKAFDVDANGYKRSEAVCSMLLTKSP----NIDSV-ATITNYATGHNGTSSSLFTPNGLSQLEVMQRATN----PLEK 4516
Cdd:cd00833   219 GRCRPFDADADGYVRGEGVGVVVLKRLSdalrDGDRIyAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYAragvDPSD 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4517 ILEIQTHCTGTKLGDPIEINAISKLVSSA------CKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLKCPTN 4590
Cdd:cd00833   299 IDYVEAHGTGTPLGDPIEVEALAKVFGGSrsadqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNP 378
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 392926054 4591 SIKTNKMICRFIGE-----DADENNSILINNFGFTGSNCSVVL 4628
Cdd:cd00833   379 KIDFEESPLRVPTEarpwpAPAGPRRAGVSSFGFGGTNAHVIL 421
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
3649-3927 1.06e-78

Acyl transferase domain in polyketide synthase (PKS) enzymes;


:

Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 264.26  E-value: 1.06e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3649 MLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLqgDVSLWEILFNTDHYKLLQLTKHMQPIMFCFGYATAQLWLS 3728
Cdd:smart00827    1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLL--GWSLLDVLLGEDGAASLLDTEVAQPALFAVQVALARLLRS 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3729 LGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIAGLGALLAVQREiADEVL-----RKFKVSVATINSP 3803
Cdd:smart00827   79 WGVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLS-EEEVEpllagVPDRVSVAAVNSP 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3804 KQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQEThLVSLRQCLADIKFSAGRTPLVSNVTGQIINT---FS 3880
Cdd:smart00827  158 SSVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPI-LDEFRAALAGLTPRPPRIPFVSTVTGTLIDGaelDD 236
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 392926054   3881 EAYIVKHTVSAVKFVDCVETLQA-KGVTVWIDAGSAAVLATFVKRIIQ 3927
Cdd:smart00827  237 ADYWVRNLREPVRFADAVRALLAeGGVTVFLEVGPHPVLTGPIKQTLA 284
PRK12316 super family cl36106
peptide synthase; Provisional
6457-7495 1.11e-65

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12316:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 251.80  E-value: 1.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6457 EVKAVESLKLPKSTSCEFVIAEIWKETLGISILNdANPNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEFT 6536
Cdd:PRK12316 2502 DVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVG-LDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFA 2580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6537 KFVKNLTTEKfAGNTNDKISYDAIPLTNSQTQMFMLRQIDTTSK-YNLifKITISYETKFVWEFLKYSLHSLIAYQPSYR 6615
Cdd:PRK12316 2581 ASLESGQTSR-APVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAaYHL--PSALHLRGVLDQAALEQAFDALVLRHETLR 2657
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6616 TVFKSGNSPYQYICSLTESFHDFDKRC------NLNNAISHEPNHLFEIGKSTPLRVRVAEDCDNSRIhIVFNQHHILTD 6689
Cdd:PRK12316 2658 TRFVEVGEQTRQVILPNMSLRIVLEDCagvadaAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHV-LVITQHHIVSD 2736
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6690 GWSMTVLSDTVSSLYAAYRG--ETSFPSKTKQTI--SQVAMGTKSSGDIKEALEYYQNTYHTIIPY------DSETGNTS 6759
Cdd:PRK12316 2737 GWSMQVMVDELVQAYAGARRgeQPTLPPLPLQYAdyAAWQRAWMDSGEGARQLDYWRERLGGEQPVlelpldRPRPALQS 2816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6760 PSYVRISKLIPSKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LIGYFMNNALFKTS 6838
Cdd:PRK12316 2817 HRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETErLIGFFVNTQVLRAQ 2896
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6839 LPFEiLRLEEILNIVLNSLEKSRSFATIPFYQMVEQ---NRKLNEISLFFNFRQKLDYPTVSMFGAKCEIEHLSLNNA-- 6913
Cdd:PRK12316 2897 VDAQ-LAFRDLLGQVKEQALGAQAHQDLPFEQLVEAlqpERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAat 2975
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6914 -FDFSFTIDETPTGSLITVDFDKSKYLDTTVHMFAniflKKLNNLRNMNTTIPIRRTD---------------------- 6970
Cdd:PRK12316 2976 qFDLALDTWESAEGLGASLTYATDLFDARTVERLA----RHWQNLLRGMVENPQRSVDelamldaeergqlleawnataa 3051
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6971 -FPSTLFQKGLFTSW--RLFTEPALLLSTNTVSYSDLAEKIENISKDIqkqlqiaKATSVREDELVGLDCKNSY---FAL 7044
Cdd:PRK12316 3052 eYPLERGVHRLFEEQveRTPDAVALAFGEQRLSYAELNRRANRLAHRL-------IERGVGPDVLVGVAVERSLemvVGL 3124
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7045 LACVFLGLPYAPIDPTWPEPRQLFV-------------------KSKVSFTLENCFSCNLKLRNFNSRTQFGSI-YSIFT 7104
Cdd:PRK12316 3125 LAILKAGGAYVPLDPEYPEERLAYMledsgaqlllsqshlrlplAQGVQVLDLDRGDENYAEANPAIRTMPENLaYVIYT 3204
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7105 SGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSE----HSTTITDQLQK 7180
Cdd:PRK12316 3205 SGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGpedwRDPALLVELIN 3284
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7181 CQYAFLPAAVFN----GFTDKTMSRLESIETLTIGGETVSDvviETAMKKFPRLRTIQIYGPTETCIWSLTNKCK---VS 7253
Cdd:PRK12316 3285 SEGVDVLHAYPSmlqaFLEEEDAHRCTSLKRIVCGGEALPA---DLQQQVFAGLPLYNLYGPTEATITVTHWQCVeegKD 3361
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7254 TLNIGSALGDS---LSNETCTICNNSVRGNVQVKGISLARGYItSAPHGT-------PFSD---IYSTGDIVDSKLNS-L 7319
Cdd:PRK12316 3362 AVPIGRPIANRacyILDGSLEPVPVGALGELYLGGEGLARGYH-NRPGLTaerfvpdPFVPgerLYRTGDLARYRADGvI 3440
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7320 QYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVLYSN-QMLIAFIV-DQKSKLLHDSLVKTLKNRtqIPDYFVQ-- 7395
Cdd:PRK12316 3441 EYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDgRQLVAYVVpEDEAGDLREALKAHLKAS--LPEYMVPah 3518
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7396 ---INKMPLNSSGKVD-KSLLLQAFENIRKSYkreiVVMKNSLEEKVINVFSKILG-RNVAPTDKFESIGGNSLNAIQIA 7470
Cdd:PRK12316 3519 llfLERMPLTPNGKLDrKALPRPDAALLQQDY----VAPVNELERRLAAIWADVLKlEQVGLTDNFFELGGDSIISLQVV 3594
                        1130      1140
                  ....*....|....*....|....*
gi 392926054 7471 HRlAEELKIEIKAHEILQSNSLKTF 7495
Cdd:PRK12316 3595 SR-ARQAGIRFTPKDLFQHQTIQGL 3618
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
830-1197 1.30e-64

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


:

Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 228.60  E-value: 1.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  830 IACdyQFAGVEGEKELWDTLLTSRLTTGKISDIRKKQCEGDAGLEV---------GLLKqDISMFDNSFFAIAKDEAEFL 900
Cdd:cd00833     8 MAC--RFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytrrgGFLD-DVDAFDAAFFGISPREAEAM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  901 DPQHRLLLNAAYNALEKSGLT--SIPDAD--LFLAISaHSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGIRGRA 976
Cdd:cd00833    85 DPQQRLLLEVAWEALEDAGYSpeSLAGSRtgVFVGAS-SSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  977 MIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL---KTLLDHHSTNSFSVDGSGFCRSDGVGVIILK 1052
Cdd:cd00833   164 LTVDTACSSSLVALHLACQSLRSGEcDLALVGGVNLILSPDMFVGFskaGMLSPDGRCRPFDADADGYVRGEGVGVVVLK 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1053 ---TAEK-GDS--AVIKiSSAKSH--HCGAVMTPVVSS----ISQLLEEAG----SFSYVEGHGTATSAGDSAE----SM 1112
Cdd:cd00833   244 rlsDALRdGDRiyAVIR-GSAVNQdgRTKGITAPSGEAqaalIRRAYARAGvdpsDIDYVEAHGTGTPLGDPIEvealAK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1113 AYQKLGSE---LIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVHNILPSEHIRNNE-NIRLPFVAEE----KQI 1184
Cdd:cd00833   323 VFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEEsPLRVPTEARPwpapAGP 402
                         410
                  ....*....|...
gi 392926054 1185 DRSAIVSFGITGT 1197
Cdd:cd00833   403 RRAGVSSFGFGGT 415
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
3203-3377 8.26e-43

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


:

Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 156.49  E-value: 8.26e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTA----KALREFEHWKSKVHTIAADINDKE---KLIRELTKLNV 3275
Cdd:smart00822    1 GTYLITGGLGGLGRALARWLAERGARRLVLLSRSGPDApgaaALLAELEAAGARVTVVACDVADRDalaAVLAAIPAVEG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3276 GITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHfnYKIENFIMMSSFTAACGNEGQLNYGVSNAYLEY 3355
Cdd:smart00822   81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTAD--LPLDFFVLFSSIAGVLGSPGQANYAAANAFLDA 158
                           170       180
                    ....*....|....*....|..
gi 392926054   3356 QVQRRRRQGKSGCAIQWGNWID 3377
Cdd:smart00822  159 LAEYRRARGLPALSIAWGAWAE 180
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
7527-7737 2.05e-17

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 91.30  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7527 IYLVHAIGGTIYPYYSFLQIFPKDISLYGIEF----DLKYPSNDLRELAHFYAEEIAAHAGNKRIFVMGHSMGGIMSREI 7602
Cdd:COG3319   604 LFCVHPAGGNVLCYRPLARALGPDRPVYGLQApgldGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEM 683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7603 VAELKIWGYDIPFVMLFDSWV--LRTNELDIENIKQFITYVFSGLP-----------DSEHRINRAIKLA---------- 7659
Cdd:COG3319   684 ARQLEAQGEEVALLVLLDSYApgALARLDEAELLAALLRDLARGVDlpldaeelralDPEERLARLLERLreaglpagld 763
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7660 ---------------QLLREYKTSVSDTKLYLFkskqlgdaafkkavRSDLNEELSRSMTCNGFDELSLQPVETYLIDGD 7724
Cdd:COG3319   764 aerlrrllrvfranlRALRRYRPRPYDGPVLLF--------------RAEEDPPGRADDPALGWRPLVAGGLEVHDVPGD 829
                         250
                  ....*....|...
gi 392926054 7725 HESCLKAENLKKV 7737
Cdd:COG3319   830 HFSMLREPHVAEL 842
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
4991-5131 7.38e-16

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05274:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 375  Bit Score: 83.59  E-value: 7.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4991 VFHLAGIVNNSLHENVKRDSLDEMVSIKLQGAKNLmkcCDET-----SHFVFSSSIANVLGSYGQSNYAFSNGLVTSFLE 5065
Cdd:cd05274   233 VIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNL---HELTpdlplDFFVLFSSVAALLGGAGQAAYAAANAFLDALAA 309
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 5066 TSST---KSTIIHWGPWKDVGMLAqpeRREIVKQIESNGWKLLPNQDAISVFYTQFMETHEQIIVFDGD 5131
Cdd:cd05274   310 QRRRrglPATSVQWGAWAGGGMAA---AAALRARLARSGLGPLAPAEALEALEALLASDAPQAVVASVD 375
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
1544-1759 3.71e-11

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


The actual alignment was detected with superfamily member pfam14765:

Pssm-ID: 469797  Cd Length: 296  Bit Score: 68.17  E-value: 3.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1544 HVVDSKIVLPGATSIRL----VHQLNGKPT-VELSNIDFLN--KITPSEAPSV---VKIEEQDGLEKLVF---------- 1603
Cdd:pfam14765   33 HRVGGTVVLPGAGYLEMaleaARQLFGGSGaVALRDVSILKalVLPEDDPVEVqtsLTPEEDGADSWWEFeifsragggw 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1604 -------------GETDAISFKLTELQNFNPIPNERLNAEVHHtdnIYERFANSHLTYRNEFQMVDSLKY--TMGKGEVR 1668
Cdd:pfam14765  113 ewtlhatgtvrlaPGEPAAPVDLESLPARCAQPADPRSVSSAE---FYERLAARGLFYGPAFQGLRRIWRgdGEALAEAR 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1669 FVSMKDLD--------ILIDGTLQAIVGCYFFENTNDNSPFVPFTIDQLSILNGDISQKQLHAVLKYDSSGN-FINGDAT 1739
Cdd:pfam14765  190 LPEAAAGGespyllhpALLDAALQLLGAALPAEAEHADQAYLPVGIERLRIYRSLPPGEPLWVHARLERRGGrTIVGDLT 269
                          250       260
                   ....*....|....*....|
gi 392926054  1740 VYDALGNIILHISNVTFKRL 1759
Cdd:pfam14765  270 LVDEDGRVVARIEGLRLRRV 289
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2943-3024 1.00e-10

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


:

Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 61.50  E-value: 1.00e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   2943 ATVDRTEIRRKVSLAVFDLATETL---SAEDLQ-SKGFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDELS 3018
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLghaAAEAIDpDRPFRDLGLDSLMAVELRNRLEAAT--GLRLPATLVFDHPTPAALA 79

                    ....*.
gi 392926054   3019 DHIVRK 3024
Cdd:smart00823   80 EHLAAE 85
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
6237-6393 4.46e-10

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd08953:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 436  Bit Score: 66.24  E-value: 4.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6237 LVFGANGFIGSIVFR-LLQEMGMNVIPISRASIP-----------------------SCDITNIKDVQNVFKSLG--FKK 6290
Cdd:cd08953   209 LVTGGAGGIGRALARaLARRYGARLVLLGRSPLPpeeewkaqtlaalealgarvlyiSADVTDAAAVRRLLEKVRerYGA 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6291 FSVVINCVGVETSA---KMNKTSLEQeiVLSPKTFGSVNILKCLEEFsiEVDKLVNFSSLSSVVPLLGNFDYASANCF-- 6365
Cdd:cd08953   289 IDGVIHAAGVLRDAllaQKTAEDFEA--VLAPKVDGLLNLAQALADE--PLDFFVLFSSVSAFFGGAGQADYAAANAFld 364
                         170       180       190
                  ....*....|....*....|....*....|
gi 392926054 6366 --VEALTKQGskYIKQFLTLSLPPLEGSRM 6393
Cdd:cd08953   365 afAAYLRQRG--PQGRVLSINWPAWREGGM 392
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
3994-4216 4.11e-09

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


The actual alignment was detected with superfamily member pfam14765:

Pssm-ID: 469797  Cd Length: 296  Bit Score: 62.00  E-value: 4.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3994 DEFELLEGHQLNGKIVVAGA-Y---------QLFKIDQLVKLKaagmelmlkNVKFLKPWYIEDNREYQIQ--------- 4054
Cdd:pfam14765   25 ADLPWLRDHRVGGTVVLPGAgYlemaleaarQLFGGSGAVALR---------DVSILKALVLPEDDPVEVQtsltpeedg 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4055 -----------WNSDMTiELIVNSVIVCSLEVEPQNSVLKLETI------SENEKPFEVHDFYETLFRNGLQYDSGFRRI 4117
Cdd:pfam14765   96 adswwefeifsRAGGGW-EWTLHATGTVRLAPGEPAAPVDLESLparcaqPADPRSVSSAEFYERLAARGLFYGPAFQGL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4118 ESARRSDKRCFSQIKSS----PFAWP------LIDSAMHSITASVVP--RRPDCYFLPVAMGSVTMKDTNSFTLPnLHAQ 4185
Cdd:pfam14765  175 RRIWRGDGEALAEARLPeaaaGGESPyllhpaLLDAALQLLGAALPAeaEHADQAYLPVGIERLRIYRSLPPGEP-LWVH 253
                          250       260       270
                   ....*....|....*....|....*....|..
gi 392926054  4186 TVITSETDKFIQVNVALLAGD-TPICEVRNMT 4216
Cdd:pfam14765  254 ARLERRGGRTIVGDLTLVDEDgRVVARIEGLR 285
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2790-2867 9.93e-09

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


:

Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 55.72  E-value: 9.93e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054   2790 AAKTLQMAVRHKVCLAVGDVIESGLDIDESqlstgFSELGIDSLATVDLLNRLNQKYfpEIELTTSDLFDNPSIIDLS 2867
Cdd:smart00823    9 RRRLLLDLVREQVAAVLGHAAAEAIDPDRP-----FRDLGLDSLMAVELRNRLEAAT--GLRLPATLVFDHPTPAALA 79
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1806-1857 5.17e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


:

Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 53.79  E-value: 5.17e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 392926054   1806 DIDNTTGFFDLGLTSIQAVKLRNAIKSNYP-NASSTCVFDYPSIDLLSGYLST 1857
Cdd:smart00823   32 AIDPDRPFRDLGLDSLMAVELRNRLEAATGlRLPATLVFDHPTPAALAEHLAA 84
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
3485-3549 1.00e-07

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 52.55  E-value: 1.00e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054 3485 IKEKVSSILMCSPTKLKNNKNIM-DMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLEKLAAHI 3549
Cdd:COG0236    10 LAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
730-803 4.71e-06

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 47.93  E-value: 4.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054  730 SDAEIESTVRTIVKQFLDIEEDDI----NLLETGAVDSLTSIEMVEAFGTAVNQTMPFDLLEAYPTILNIVDFLKTLV 803
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDPEEItpddSFFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
KAsynt_C_assoc super family cl24694
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
376-431 6.77e-06

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


The actual alignment was detected with superfamily member pfam16197:

Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 48.70  E-value: 6.77e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054   376 NRVAISSYGFGGTNACAIIEKPEKPSLVQKESYAESNVLFLSAKSHESLKLQIEEY 431
Cdd:pfam16197   25 GIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKALLEKL 80
KAsynt_C_assoc super family cl24694
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
4614-4695 1.03e-05

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


The actual alignment was detected with superfamily member pfam16197:

Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 47.92  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4614 INNFGFTGSNCSVVLK--PKNAISEhFVSSEVFYPILLSSHSAKSLQKYVQVL------CEFISnsakSLHDImmslFQK 4685
Cdd:pfam16197   29 VNSFGFGGANAHVILKsnPKPKIPP-ESPDNLPRLVLLSGRTEEAVKALLEKLenhlddAEFLS----LLNDI----HSL 99
                           90
                   ....*....|..
gi 392926054  4686 KI--HVHRQFII 4695
Cdd:pfam16197  100 PIsgHPYRGYAI 111
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
5167-5235 1.12e-04

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 44.07  E-value: 1.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 5167 EEIFFEIVGItdISSKLNIP----------FMDLGIDSLCMENLRYSLNKNFDLELTVSEMFENATYQKLQTYVETLRK 5235
Cdd:COG0236     4 EELEERLAEI--IAEVLGVDpeeitpddsfFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
 
Name Accession Description Interval E-value
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
6987-7412 4.74e-160

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 504.70  E-value: 4.74e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6987 FTEPALLL----STNTVSYSDLAEKIENISKDIQKQLQIakatsvrEDELVGLDC---KNSYFALLACVFLGLPYAPIDP 7059
Cdd:cd17654     1 PDRPALIIdqttSDTTVSYADLAEKISNLSNFLRKKFQT-------EERAIGLRCdrgTESPVAILAILFLGAAYAPIDP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7060 TWPEPRQLFVKSK--VSFTLENCFSCNLKL------RNFNSRTQFGSIYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQ 7131
Cdd:cd17654    74 ASPEQRSLTVMKKchVSYLLQNKELDNAPLsftpehRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7132 CM-FRSNIRVLDSVKqVFDVSVSNIIGSVLNGGVLISSEHS--------TTITDQLQKCQYAFLPAAVFNGFTDK----- 7197
Cdd:cd17654   154 FNiTSEDILFLTSPL-TFDPSVVEIFLSLSSGATLLIVPTSvkvlpsklADILFKRHRITVLQATPTLFRRFGSQsikst 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7198 TMSRLESIETLTIGGE-TVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKCKV--STLNIGSALGDsLSNETCTICN 7274
Cdd:cd17654   233 VLSATSSLRVLALGGEpFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEedSPVQLGSPLLG-TVIEVRDQNG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7275 NSVRGNVQVKGISlaRGYITSAPHGTPFSDIYSTGDIVDSKLNSLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQI 7354
Cdd:cd17654   312 SEGTGQVFLGGLN--RVCILDDEVTVPKGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESC 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7355 VVLYSN-QMLIAFIVDQ-KSKLLHDSLVKTLKNRTQIPDYFVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17654   390 AVTLSDqQRLIAFIVGEsSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
5256-6071 1.56e-153

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 519.04  E-value: 1.56e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5256 DDTRVAVIGWSAEFSGSSNIHEYWENLMDGICSTG--------NNKYL-----------------LKNPFGFDNKFFNLT 5310
Cdd:COG3321     2 ADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITevpadrwdADAYYdpdpdapgktyvrwggfLDDVDEFDALFFGIS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5311 DEDARVLDPQVRKFIQHAYLALENSGYVKQK-HELRCGVFAGAEPSDYGR--ADDHDDAMRKLFVMNMNSYLASYASYCL 5387
Cdd:COG3321    82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESlAGSRTGVFVGASSNDYALllLADPEAIDAYALTGNAKSVLAGRISYKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5388 DLKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGFDDQKktMFSKSGVCRPFDKDSEGIVRGS 5467
Cdd:COG3321   162 DLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGG--MLSPDGRCRAFDADADGYVRGE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5468 GVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRaSFMAPNPAGQLKCMTDVLARFtNKEKERISFVECHATGTTLGD 5547
Cdd:COG3321   240 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADA-GVDPATVDYVEAHGTGTPLGD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5548 TIEMNSLRTAY----SFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSE------FrDGMGqfFTVN 5617
Cdd:COG3321   318 PIEAAALTAAFgqgrPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETpnphidF-ENSP--FYVN 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5618 GKKSTISQNS---LISIDSFGIGGTNVHMVIE-FPARSQEVVKISSENLILydmiPISAKTEYSLDHTSEAISKYLQTDT 5693
Cdd:COG3321   395 TELRPWPAGGgprRAGVSSFGFGGTNAHVVLEeAPAAAPAAAAAARPPQLL----VLSAKTEEALRALAARLAAFLEAHP 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5694 NK-IAQCSSTFIHSRVPMDSRTYLSVNNNNELL---------KIRTNKKTWFNGKSPKIALFFAPQGIQFTNILPNEYLK 5763
Cdd:COG3321   471 DLdLADVAYTLATGRAHFEHRLAVVASSREELAaklralaagEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYET 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5764 NSAYRREVEYLCELASSFGIPSLEGILYPTKNfDHLIHATQFAQIAIFVQCMAIFKAIKNV-FNPTCLIGHSVGEYAAAV 5842
Cdd:COG3321   551 EPVFRAALDECDALLRPHLGWSLREVLFPDEE-ESRLDRTEVAQPALFAVEYALARLWRSWgVRPDAVIGHSVGEYAAAC 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5843 ISGALKTEEALKLLIKRSELIGKTEKA-RMLMVWNYEKQ----LPSHVHVS-AIIDANTKCVV-GPVETIDNLEKYFINN 5915
Cdd:COG3321   630 VAGVLSLEDALRLVAARGRLMQALPGGgAMLAVGLSEEEvealLAGYDGVSiAAVNGPRSTVVsGPAEAVEALAARLEAR 709
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5916 HIKYRNIETKHGFHSKMFHCISKEFEFFCESFATKVPLIPMISSITGSEIK--IFDSKYCTMHLTNPVNLELVVDHIMKL 5993
Cdd:COG3321   710 GIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTgeALDADYWVRHLRQPVRFADAVEALLAD 789
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5994 DIDIIVEVGPTGVLSNLL---AKRNSKIVVVPTCGTKKHPKISLGECIGQLWSNGVDI--RKLTPKLA---VDgqVPGYC 6065
Cdd:COG3321   790 GVRVFLEVGPGPVLTGLVrqcLAAAGDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVdwSALYPGRGrrrVP--LPTYP 867

                  ....*.
gi 392926054 6066 FdERQF 6071
Cdd:COG3321   868 F-QRED 872
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
5258-5645 5.51e-123

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 396.93  E-value: 5.51e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5258 TRVAVIGWSAEFSGSSNIHEYWENLMDGICSTG------------------------NNKYLLKNPFGFDNKFFNLTDED 5313
Cdd:cd00833     1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISeipedrwdadgyypdpgkpgktytRRGGFLDDVDAFDAAFFGISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5314 ARVLDPQVRKFIQHAYLALENSGYV-KQKHELRCGVFAGAEPSDYGRA-DDHDDAMRKLFVM-NMNSYLASYASYCLDLK 5390
Cdd:cd00833    81 AEAMDPQQRLLLEVAWEALEDAGYSpESLAGSRTGVFVGASSSDYLELlARDPDEIDAYAATgTSRAFLANRISYFFDLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5391 GEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGFDDQKktMFSKSGVCRPFDKDSEGIVRGSGVG 5470
Cdd:cd00833   161 GPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAG--MLSPDGRCRPFDADADGYVRGEGVG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5471 CFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRASFmAPNPAGQLKCMTDVLARfTNKEKERISFVECHATGTTLGDTIE 5550
Cdd:cd00833   239 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGIT-APSGEAQAALIRRAYAR-AGVDPSDIDYVEAHGTGTPLGDPIE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5551 MNSLRTAY----SFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSEFR---DGMGQFFTVNGKKSTI 5623
Cdd:cd00833   317 VEALAKVFggsrSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNpkiDFEESPLRVPTEARPW 396
                         410       420
                  ....*....|....*....|....*
gi 392926054 5624 SQNS---LISIDSFGIGGTNVHMVI 5645
Cdd:cd00833   397 PAPAgprRAGVSSFGFGGTNAHVIL 421
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
1889-2282 5.41e-122

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 394.23  E-value: 5.41e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1889 NPIGVMAAACRLPGGVSsPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYG-NPVEGGNFItQDVTQFDPSFFKISK 1967
Cdd:cd00833     1 EPIAIVGMACRFPGAAD-PDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGkTYTRRGGFL-DDVDAFDAAFFGISP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1968 SEAELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYQDMMESSSIL----AMLGSMAAVIAGRVNYIFG 2039
Cdd:cd00833    79 REAEAMDPQQRLLLEVAWEALEDAGYspesLAGSRTGVFVGASSSDYLELLARDPDEidayAATGTSRAFLANRISYFFD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2040 CYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDGCV 2119
Cdd:cd00833   159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2120 VLMLelaKP-------NFHYMSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS---PSlAIDYWEAHGTGTPLGDP 2189
Cdd:cd00833   239 VVVL---KRlsdalrdGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAgvdPS-DIDYVEAHGTGTPLGDP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2190 IEFNTLSSIL-------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDINAGSIRLPIIGEDS 2262
Cdd:cd00833   315 IEVEALAKVFggsrsadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEAR 394
                         410       420
                  ....*....|....*....|....*.
gi 392926054 2263 ELVS------AGISSFGVSGTNAAAI 2282
Cdd:cd00833   395 PWPApagprrAGVSSFGFGGTNAHVI 420
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1887-2354 1.02e-111

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 393.47  E-value: 1.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1887 AENPIGVMAAACRLPGgVSSPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNPV---EGGnFItQDVTQFDPSFF 1963
Cdd:COG3321     2 ADEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTyvrWGG-FL-DDVDEFDALFF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1964 KISKSEAELIDPQQRLLLECVQECLENSGVIET----SNVGVFVGLMEKEYQDMM----ESSSILAMLGSMAAVIAGRVN 2035
Cdd:COG3321    79 GISPREAEAMDPQQRLLLEVAWEALEDAGYDPEslagSRTGVFVGASSNDYALLLladpEAIDAYALTGNAKSVLAGRIS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2036 YIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRS 2115
Cdd:COG3321   159 YKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2116 DGCVVLMLE------------LAkpnfhymsTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQ---SPSlAIDYWEAH 2180
Cdd:COG3321   239 EGVGVVVLKrlsdalrdgdriYA--------VIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADagvDPA-TVDYVEAH 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2181 GTGTPLGDPIEFNTLSSIL-------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDIN--AG 2251
Cdd:COG3321   310 GTGTPLGDPIEAAALTAAFgqgrpadQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDfeNS 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2252 SIRLPiigedSELVS---------AGISSFGVSGTNAAAIafndnnkLE--------PYIPIHKYYILPISAKNQISLDN 2314
Cdd:COG3321   390 PFYVN-----TELRPwpagggprrAGVSSFGFGGTNAHVV-------LEeapaaapaAAAAARPPQLLVLSAKTEEALRA 457
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 392926054 2315 LEKQILSVI------PLTDVpicniASALANNRSHFTIRNALIVSN 2354
Cdd:COG3321   458 LAARLAAFLeahpdlDLADV-----AYTLATGRAHFEHRLAVVASS 498
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
13-394 9.44e-106

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 347.24  E-value: 9.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   13 PNGEDGHEMAENIFLNRNNIALLPVEKNYLSDFREKHPE------VKAALVDGIEYFDDQYFGTGESEAICMDPQQRMLM 86
Cdd:cd00833    13 PGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytRRGGFLDDVDAFDAAFFGISPREAEAMDPQQRLLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   87 QGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLL-----PPDQYMATGNSASVMCGRITYFLNSRGAAVGIETACSS 161
Cdd:cd00833    93 EVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLardpdEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSS 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  162 SLVAFHLARQAIQSGETKLALVCGANHVGS-RSFHSLYNSHMVSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENN 240
Cdd:cd00833   173 SLVALHLACQSLRSGECDLALVGGVNLILSpDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  241 LLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSDIRVMS 318
Cdd:cd00833   253 DRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARagVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQ 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  319 P------KSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEME-------LNRVAISSYGF 385
Cdd:cd00833   333 PlligsvKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARpwpapagPRRAGVSSFGF 412

                  ....*....
gi 392926054  386 GGTNACAII 394
Cdd:cd00833   413 GGTNAHVIL 421
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
54-600 3.68e-102

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 364.19  E-value: 3.68e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   54 AALVDGIEYFDDQYFGTGESEAICMDPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLLPP-----DQY 128
Cdd:COG3321    64 GGFLDDVDEFDALFFGISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLAdpeaiDAY 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  129 MATGNSASVMCGRITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNG 207
Cdd:COG3321   144 ALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNlMLTPESFILFSKGGMLSPDG 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  208 RLAAFDRSANGFVRAESFAVAVLcsKQF--AEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKD 283
Cdd:COG3321   224 RCRAFDADADGYVRGEGVGVVVL--KRLsdALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADagVDPA 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  284 SVQLVTCHGTGTKLGDQVELTAINRSFKSD------IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPS 357
Cdd:COG3321   302 TVDYVEAHGTGTPLGDPIEAAALTAAFGQGrpadqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPN 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  358 EDLGEDKSMGFVNEE-MELN------RVAISSYGFGGTNACAIIEKPEKPSLVQKESYAESNVLFLSAKSHESLKLQIEE 430
Cdd:COG3321   382 PHIDFENSPFYVNTElRPWPagggprRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAAR 461
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  431 YTQFMAQ-SDSAMEDILYTVNERKTKYDFRAAVFGKDNEEIARKL------QDGDYSLTNLQESTFEVEF---GEGNEKL 500
Cdd:COG3321   462 LAAFLEAhPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLralaagEAAPGVVTGAAAAAPKVAFlfpGQGSQYV 541
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  501 WLLRMLYEKNETFHSTVDKYCK-LAETCGFPeaRTALFFP----FKLTLT----PLTYNVsrlisSMATFELLVQYNTLP 571
Cdd:COG3321   542 GMGRELYETEPVFRAALDECDAlLRPHLGWS--LREVLFPdeeeSRLDRTevaqPALFAV-----EYALARLWRSWGVRP 614
                         570       580
                  ....*....|....*....|....*....
gi 392926054  572 NKLRGKGLGQIFCLAVAKVITFESAVQLI 600
Cdd:COG3321   615 DAVIGHSVGEYAAACVAGVLSLEDALRLV 643
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
4290-4628 2.55e-93

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 311.41  E-value: 2.55e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4290 ALLDSDARyWDPEYFGIRPSEAKFIDPQQRLLL-CSVAKLLDS-LLITSLT-SNTGVFIGCSANEFSHIVyAYGYKDPRA 4366
Cdd:cd00833    61 GFLDDVDA-FDAAFFGISPREAEAMDPQQRLLLeVAWEALEDAgYSPESLAgSRTGVFVGASSSDYLELL-ARDPDEIDA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4367 EWSGGTSNSALAGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKM-TVD 4445
Cdd:cd00833   139 YAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMlSPD 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4446 DFCKAFDVDANGYKRSEAVCSMLLTKSP----NIDSV-ATITNYATGHNGTSSSLFTPNGLSQLEVMQRATN----PLEK 4516
Cdd:cd00833   219 GRCRPFDADADGYVRGEGVGVVVLKRLSdalrDGDRIyAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYAragvDPSD 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4517 ILEIQTHCTGTKLGDPIEINAISKLVSSA------CKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLKCPTN 4590
Cdd:cd00833   299 IDYVEAHGTGTPLGDPIEVEALAKVFGGSrsadqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNP 378
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 392926054 4591 SIKTNKMICRFIGE-----DADENNSILINNFGFTGSNCSVVL 4628
Cdd:cd00833   379 KIDFEESPLRVPTEarpwpAPAGPRRAGVSSFGFGGTNAHVIL 421
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
1891-2282 1.47e-81

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 272.67  E-value: 1.47e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   1891 IGVmaaACRLPGgVSSPSELWELLKIGKNassripatrvptrntlisgskygnpveggnfitqDVTQFDPSFFKISKSEA 1970
Cdd:smart00825    4 VGM---SCRFPG-ADDPEEFWDLLLAGLD----------------------------------DVDLFDAAFFGISPREA 45
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   1971 ELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYqdmmesssilamlgsmaaviagrvnyifgcygpSVT 2046
Cdd:smart00825   46 EAMDPQQRLLLEVAWEALEDAGIdpesLRGSRTGVFVGVSSSDY---------------------------------SVT 92
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   2047 IDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILN-EKGQGLrTNGKMLSQHGMSLSFDSRASGYGRSDGCVVLMLE- 2124
Cdd:smart00825   93 VDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSpDTFVGL-SRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKr 171
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   2125 -----------LAkpnfhymsTIQSVNVNHGGRSVSLTAPNGVAHkmlltsvinqspslaidyweahgtgtplgdpiefn 2193
Cdd:smart00825  172 lsdalrdgdpiLA--------VIRGSAVNQDGRSNGITAPSGPAQ----------------------------------- 208
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   2194 tlssilqnIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDINAGSIRLPIIGEDSELVS------A 2267
Cdd:smart00825  209 --------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWPPpgrprrA 280
                           410
                    ....*....|....*
gi 392926054   2268 GISSFGVSGTNAAAI 2282
Cdd:smart00825  281 GVSSFGFGGTNAHVI 295
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
5260-5646 5.19e-81

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 271.12  E-value: 5.19e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5260 VAVIGWSAEFSGSSNIHEYWENLMDGicstgnnkylLKNPFGFDNKFFNLTDEDARVLDPQVRKFIQHAYLALENSGYVK 5339
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG----------LDDVDLFDAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDP 70
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5340 QK-HELRCGVFAGAEPSDYgraddhddamrklfvmnmnsylasyasycldlkgeAVSVYSACSTALVAVANAVKSIQSGS 5418
Cdd:smart00825   71 ESlRGSRTGVFVGVSSSDY-----------------------------------SVTVDTACSSSLVALHLACQSLRSGE 115
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5419 MDYALVGAASIAEVSGALSGFDDQKktMFSKSGVCRPFDKDSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINN 5498
Cdd:smart00825  116 CDMALAGGVNLILSPDTFVGLSRAG--MLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQ 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5499 DGHSrASFMAPNPAGQlkcmtdvlarftnkekerisfvechatgttlgdtiemnslrtaysfknkLAIGSCKANIGHAYA 5578
Cdd:smart00825  194 DGRS-NGITAPSGPAQ-------------------------------------------------LLIGSVKSNIGHLEA 223
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054   5579 ASGLAALVKCAKMLQTGIIPPQVNFSE------FRDGMgqfFTVNGKKSTISQNS---LISIDSFGIGGTNVHMVIE 5646
Cdd:smart00825  224 AAGVAGLIKVVLALKHGVIPPTLHFETpnphidLEESP---LRVPTELTPWPPPGrprRAGVSSFGFGGTNAHVILE 297
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
3649-3927 1.06e-78

Acyl transferase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 264.26  E-value: 1.06e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3649 MLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLqgDVSLWEILFNTDHYKLLQLTKHMQPIMFCFGYATAQLWLS 3728
Cdd:smart00827    1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLL--GWSLLDVLLGEDGAASLLDTEVAQPALFAVQVALARLLRS 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3729 LGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIAGLGALLAVQREiADEVL-----RKFKVSVATINSP 3803
Cdd:smart00827   79 WGVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLS-EEEVEpllagVPDRVSVAAVNSP 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3804 KQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQEThLVSLRQCLADIKFSAGRTPLVSNVTGQIINT---FS 3880
Cdd:smart00827  158 SSVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPI-LDEFRAALAGLTPRPPRIPFVSTVTGTLIDGaelDD 236
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 392926054   3881 EAYIVKHTVSAVKFVDCVETLQA-KGVTVWIDAGSAAVLATFVKRIIQ 3927
Cdd:smart00827  237 ADYWVRNLREPVRFADAVRALLAeGGVTVFLEVGPHPVLTGPIKQTLA 284
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3617-3971 1.96e-76

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 284.07  E-value: 1.96e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3617 VVGKSIRDVVSKIKEAAPQQIKLC------QESSKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLqgDV 3690
Cdd:COG3321   494 VVASSREELAAKLRALAAGEAAPGvvtgaaAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALDECDALLRPHL--GW 571
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3691 SLWEILFNTDHYKLLQLTKHMQPIMFCFGYATAQLWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAME 3770
Cdd:COG3321   572 SLREVLFPDEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLEDALRLVAARGRLMQ 651
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3771 NIAGLGALLAVQ--REIADEVLRKF-KVSVATINSPKQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQETh 3847
Cdd:COG3321   652 ALPGGGAMLAVGlsEEEVEALLAGYdGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARRLPVSHAFHSPLMEPA- 730
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3848 LVSLRQCLADIKFSAGRTPLVSNVTGQIINT--FSEAYIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:COG3321   731 LEEFRAALAGVTPRAPRIPLISNVTGTWLTGeaLDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQC 810
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 392926054 3926 IQPTElsKHRIVQTCKEKESDVDNLVQACLELEQSGLPISWTTLYG 3971
Cdd:COG3321   811 LAAAG--DAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYP 854
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
1889-2124 2.60e-75

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 252.94  E-value: 2.60e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1889 NPIGVMAAACRLPGGVSsPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNPVEGGNFITQDVTQFDPSFFKISKS 1968
Cdd:pfam00109    1 EPVAIVGMGCRFPGGND-PEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKWGGLDDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1969 EAELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYQDMMESSSI-------LAMLGSMAAVIAGRVNYI 2037
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGItpdsLDGSRTGVFIGSGIGDYAALLLLDEDggprrgsPFAVGTMPSVIAGRISYF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2038 FGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDG 2117
Cdd:pfam00109  160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239

                   ....*..
gi 392926054  2118 CVVLMLE 2124
Cdd:pfam00109  240 VGAVVLK 246
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
57-395 3.43e-72

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 245.70  E-value: 3.43e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054     57 VDGIEYFDDQYFGTGESEAICMDPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYkdllppdqymatgnsas 136
Cdd:smart00825   27 LDDVDLFDAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY----------------- 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    137 vmcgrityflnsrgaAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNGRLAAFDRS 215
Cdd:smart00825   90 ---------------SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLSPDGRCKTFDAS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    216 ANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQyevqlealknidkdsvqlvtchgtgt 295
Cdd:smart00825  155 ADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ-------------------------- 208
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    296 klgdqveltainrsfksdIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEME- 374
Cdd:smart00825  209 ------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTp 270
                           330       340
                    ....*....|....*....|....*..
gi 392926054    375 ------LNRVAISSYGFGGTNACAIIE 395
Cdd:smart00825  271 wpppgrPRRAGVSSFGFGGTNAHVILE 297
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
4290-4695 3.98e-71

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 267.12  E-value: 3.98e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4290 ALLDsDARYWDPEYFGIRPSEAKFIDPQQRLLL-CSVAKLLDS-LLITSLT-SNTGVFIGCSANEFSHIVYAYGykDPRA 4366
Cdd:COG3321    65 GFLD-DVDEFDALFFGISPREAEAMDPQQRLLLeVAWEALEDAgYDPESLAgSRTGVFVGASSNDYALLLLADP--EAID 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4367 EWSG-GTSNSALAGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKM-TV 4444
Cdd:COG3321   142 AYALtGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMlSP 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4445 DDFCKAFDVDANGYKRSEAvCSMLLTKsP------NIDSV-ATITNYATGHNGTSSSLFTPNGLSQLEVMQRAtnpleki 4517
Cdd:COG3321   222 DGRCRAFDADADGYVRGEG-VGVVVLK-RlsdalrDGDRIyAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRA------- 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4518 LE-----------IQTHCTGTKLGDPIEINAISKLVSSA------CKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRV 4580
Cdd:COG3321   293 LAdagvdpatvdyVEAHGTGTPLGDPIEAAALTAAFGQGrpadqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLP 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4581 AQLHLKCPTNSIktnkmicrfigedaDENNSIL-------------------INNFGFTGSNCSVVLK-PKNAISEHFVS 4640
Cdd:COG3321   373 PTLHFETPNPHI--------------DFENSPFyvntelrpwpagggprragVSSFGFGGTNAHVVLEeAPAAAPAAAAA 438
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054 4641 SEVFYPILLSSHSAKSLQKYVQVLCEFI-SNSAKSLHDIMMSLFQKKIH-VHRQFII 4695
Cdd:COG3321   439 ARPPQLLVLSAKTEEALRALAARLAAFLeAHPDLDLADVAYTLATGRAHfEHRLAVV 495
PRK12316 PRK12316
peptide synthase; Provisional
6457-7495 1.11e-65

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 251.80  E-value: 1.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6457 EVKAVESLKLPKSTSCEFVIAEIWKETLGISILNdANPNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEFT 6536
Cdd:PRK12316 2502 DVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVG-LDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFA 2580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6537 KFVKNLTTEKfAGNTNDKISYDAIPLTNSQTQMFMLRQIDTTSK-YNLifKITISYETKFVWEFLKYSLHSLIAYQPSYR 6615
Cdd:PRK12316 2581 ASLESGQTSR-APVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAaYHL--PSALHLRGVLDQAALEQAFDALVLRHETLR 2657
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6616 TVFKSGNSPYQYICSLTESFHDFDKRC------NLNNAISHEPNHLFEIGKSTPLRVRVAEDCDNSRIhIVFNQHHILTD 6689
Cdd:PRK12316 2658 TRFVEVGEQTRQVILPNMSLRIVLEDCagvadaAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHV-LVITQHHIVSD 2736
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6690 GWSMTVLSDTVSSLYAAYRG--ETSFPSKTKQTI--SQVAMGTKSSGDIKEALEYYQNTYHTIIPY------DSETGNTS 6759
Cdd:PRK12316 2737 GWSMQVMVDELVQAYAGARRgeQPTLPPLPLQYAdyAAWQRAWMDSGEGARQLDYWRERLGGEQPVlelpldRPRPALQS 2816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6760 PSYVRISKLIPSKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LIGYFMNNALFKTS 6838
Cdd:PRK12316 2817 HRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETErLIGFFVNTQVLRAQ 2896
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6839 LPFEiLRLEEILNIVLNSLEKSRSFATIPFYQMVEQ---NRKLNEISLFFNFRQKLDYPTVSMFGAKCEIEHLSLNNA-- 6913
Cdd:PRK12316 2897 VDAQ-LAFRDLLGQVKEQALGAQAHQDLPFEQLVEAlqpERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAat 2975
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6914 -FDFSFTIDETPTGSLITVDFDKSKYLDTTVHMFAniflKKLNNLRNMNTTIPIRRTD---------------------- 6970
Cdd:PRK12316 2976 qFDLALDTWESAEGLGASLTYATDLFDARTVERLA----RHWQNLLRGMVENPQRSVDelamldaeergqlleawnataa 3051
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6971 -FPSTLFQKGLFTSW--RLFTEPALLLSTNTVSYSDLAEKIENISKDIqkqlqiaKATSVREDELVGLDCKNSY---FAL 7044
Cdd:PRK12316 3052 eYPLERGVHRLFEEQveRTPDAVALAFGEQRLSYAELNRRANRLAHRL-------IERGVGPDVLVGVAVERSLemvVGL 3124
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7045 LACVFLGLPYAPIDPTWPEPRQLFV-------------------KSKVSFTLENCFSCNLKLRNFNSRTQFGSI-YSIFT 7104
Cdd:PRK12316 3125 LAILKAGGAYVPLDPEYPEERLAYMledsgaqlllsqshlrlplAQGVQVLDLDRGDENYAEANPAIRTMPENLaYVIYT 3204
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7105 SGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSE----HSTTITDQLQK 7180
Cdd:PRK12316 3205 SGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGpedwRDPALLVELIN 3284
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7181 CQYAFLPAAVFN----GFTDKTMSRLESIETLTIGGETVSDvviETAMKKFPRLRTIQIYGPTETCIWSLTNKCK---VS 7253
Cdd:PRK12316 3285 SEGVDVLHAYPSmlqaFLEEEDAHRCTSLKRIVCGGEALPA---DLQQQVFAGLPLYNLYGPTEATITVTHWQCVeegKD 3361
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7254 TLNIGSALGDS---LSNETCTICNNSVRGNVQVKGISLARGYItSAPHGT-------PFSD---IYSTGDIVDSKLNS-L 7319
Cdd:PRK12316 3362 AVPIGRPIANRacyILDGSLEPVPVGALGELYLGGEGLARGYH-NRPGLTaerfvpdPFVPgerLYRTGDLARYRADGvI 3440
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7320 QYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVLYSN-QMLIAFIV-DQKSKLLHDSLVKTLKNRtqIPDYFVQ-- 7395
Cdd:PRK12316 3441 EYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDgRQLVAYVVpEDEAGDLREALKAHLKAS--LPEYMVPah 3518
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7396 ---INKMPLNSSGKVD-KSLLLQAFENIRKSYkreiVVMKNSLEEKVINVFSKILG-RNVAPTDKFESIGGNSLNAIQIA 7470
Cdd:PRK12316 3519 llfLERMPLTPNGKLDrKALPRPDAALLQQDY----VAPVNELERRLAAIWADVLKlEQVGLTDNFFELGGDSIISLQVV 3594
                        1130      1140
                  ....*....|....*....|....*
gi 392926054 7471 HRlAEELKIEIKAHEILQSNSLKTF 7495
Cdd:PRK12316 3595 SR-ARQAGIRFTPKDLFQHQTIQGL 3618
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
6-236 5.34e-65

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 223.28  E-value: 5.34e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054     6 VGSWAKIPNGEDGHEMAENIFLNRNNIALLP-----VEKNYL--SDFREKHPEVKAALvDGIEYFDDQYFGTGESEAICM 78
Cdd:pfam00109    6 VGMGCRFPGGNDPEEFWENLLEGRDGISEIPadrwdPDKLYDppSRIAGKIYTKWGGL-DDIFDFDPLFFGISPREAERM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    79 DPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLL-------PPDQYM-ATGNSASVMCGRITYFLNSRG 150
Cdd:pfam00109   85 DPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLlldedggPRRGSPfAVGTMPSVIAGRISYFLGLRG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   151 AAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNGRLAAFDRSANGFVRAESFAVAV 229
Cdd:pfam00109  165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVV 244

                   ....*..
gi 392926054   230 LCSKQFA 236
Cdd:pfam00109  245 LKRLSDA 251
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
830-1197 1.30e-64

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 228.60  E-value: 1.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  830 IACdyQFAGVEGEKELWDTLLTSRLTTGKISDIRKKQCEGDAGLEV---------GLLKqDISMFDNSFFAIAKDEAEFL 900
Cdd:cd00833     8 MAC--RFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytrrgGFLD-DVDAFDAAFFGISPREAEAM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  901 DPQHRLLLNAAYNALEKSGLT--SIPDAD--LFLAISaHSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGIRGRA 976
Cdd:cd00833    85 DPQQRLLLEVAWEALEDAGYSpeSLAGSRtgVFVGAS-SSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  977 MIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL---KTLLDHHSTNSFSVDGSGFCRSDGVGVIILK 1052
Cdd:cd00833   164 LTVDTACSSSLVALHLACQSLRSGEcDLALVGGVNLILSPDMFVGFskaGMLSPDGRCRPFDADADGYVRGEGVGVVVLK 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1053 ---TAEK-GDS--AVIKiSSAKSH--HCGAVMTPVVSS----ISQLLEEAG----SFSYVEGHGTATSAGDSAE----SM 1112
Cdd:cd00833   244 rlsDALRdGDRiyAVIR-GSAVNQdgRTKGITAPSGEAqaalIRRAYARAGvdpsDIDYVEAHGTGTPLGDPIEvealAK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1113 AYQKLGSE---LIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVHNILPSEHIRNNE-NIRLPFVAEE----KQI 1184
Cdd:cd00833   323 VFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEEsPLRVPTEARPwpapAGP 402
                         410
                  ....*....|...
gi 392926054 1185 DRSAIVSFGITGT 1197
Cdd:cd00833   403 RRAGVSSFGFGGT 415
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
830-1287 5.93e-61

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 234.38  E-value: 5.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  830 IACdyQFAGVEGEKELWDTLLTSRLTTGKISDIR---KKQCEGDAGLEV-------GLLKqDISMFDNSFFAIAKDEAEF 899
Cdd:COG3321    11 MAC--RFPGADDPEEFWRNLRAGRDAITEVPADRwdaDAYYDPDPDAPGktyvrwgGFLD-DVDEFDALFFGISPREAEA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  900 LDPQHRLLLNAAYNALEKSGltsIPDADL-------FLAISaHSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGI 972
Cdd:COG3321    88 MDPQQRLLLEVAWEALEDAG---YDPESLagsrtgvFVGAS-SNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  973 RGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL-KT-LL--DHHStNSFSVDGSGFCRSDGVG 1047
Cdd:COG3321   164 RGPSVTVDTACSSSLVAVHLACQSLRSGEcDLALAGGVNLMLTPESFILFsKGgMLspDGRC-RAFDADADGYVRGEGVG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1048 VIILKTAEK----GDS--AVIKiSSAKSH--HCGAVMTPVVSS----ISQLLEEAG----SFSYVEGHGTATSAGDSAE- 1110
Cdd:COG3321   243 VVVLKRLSDalrdGDRiyAVIR-GSAVNQdgRSNGLTAPNGPAqaavIRRALADAGvdpaTVDYVEAHGTGTPLGDPIEa 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1111 ---SMAYQKLGSE---LIMSSVKAQFGHCEVASGLIQLMKVS-SIgKHGIIPsivhnilPSEHIRN-NENI---RLPF-V 1178
Cdd:COG3321   322 aalTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVlAL-RHGVLP-------PTLHFETpNPHIdfeNSPFyV 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1179 AEE----KQID---RSAIVSFGITGTKT-VVTTE--RVSQLNVDNIQNCYLLPVSAKTKDGLKKACLSLIEMIDNSCE-S 1247
Cdd:COG3321   394 NTElrpwPAGGgprRAGVSSFGFGGTNAhVVLEEapAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDlD 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 392926054 1248 LYDISTTLQKQKTNFKWRTAVVGSSHADVVLKLKQFLTSE 1287
Cdd:COG3321   474 LADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGE 513
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4242-4472 2.57e-60

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 209.80  E-value: 2.57e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4242 SEIEIVGFDISLPYNQisENSENWQHLKTN-----TVKQKLHNRSLKQDHARVALLDSDARY--------WDPEYFGIRP 4308
Cdd:pfam00109    1 EPVAIVGMGCRFPGGN--DPEEFWENLLEGrdgisEIPADRWDPDKLYDPPSRIAGKIYTKWgglddifdFDPLFFGISP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4309 SEAKFIDPQQRLLLCSVAKLLDSLLITSLT---SNTGVFIGCSANEFSHIVYAYGYKDPRAEWSG--GTSNSALAGRIAH 4383
Cdd:pfam00109   79 REAERMDPQQRLLLEAAWEALEDAGITPDSldgSRTGVFIGSGIGDYAALLLLDEDGGPRRGSPFavGTMPSVIAGRISY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4384 WLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKM-TVDDFCKAFDVDANGYKRSE 4462
Cdd:pfam00109  159 FLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMlSPDGPCKAFDPFADGFVRGE 238
                          250
                   ....*....|
gi 392926054  4463 AvCSMLLTKS 4472
Cdd:pfam00109  239 G-VGAVVLKR 247
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
4295-4628 1.52e-57

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 203.71  E-value: 1.52e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   4295 DARYWDPEYFGIRPSEAKFIDPQQRLLLCSVAKLLDSLLITSLT---SNTGVFIGCSANEFShivyaygykdpraewsgg 4371
Cdd:smart00825   29 DVDLFDAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDPESlrgSRTGVFVGVSSSDYS------------------ 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   4372 tsnsalagriahwlklkgpvVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKM-TVDDFCKA 4450
Cdd:smart00825   91 --------------------VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMlSPDGRCKT 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   4451 FDVDANGYKRSEAVCSMLLTKSP----NIDSV-ATITNYATGHNGTSSSLFTPNGLSQlevmqratnplekileiqthct 4525
Cdd:smart00825  151 FDASADGYVRGEGVGVVVLKRLSdalrDGDPIlAVIRGSAVNQDGRSNGITAPSGPAQ---------------------- 208
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   4526 gtklgdpieinaisklvssaCKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLKCPTNSIKTNKMICRFIGE- 4604
Cdd:smart00825  209 --------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTEl 268
                           330       340
                    ....*....|....*....|....*...
gi 392926054   4605 ----DADENNSILINNFGFTGSNCSVVL 4628
Cdd:smart00825  269 tpwpPPGRPRRAGVSSFGFGGTNAHVIL 296
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
825-1056 2.94e-53

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 189.38  E-value: 2.94e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   825 SDINVIACDYQFAGVEGEKELWDTLLTSRLTTGKISDIR---------KKQCEGDAGLEVGLLkQDISMFDNSFFAIAKD 895
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRwdpdklydpPSRIAGKIYTKWGGL-DDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   896 EAEFLDPQHRLLLNAAYNALEKSGLT--SIPDAD--LFLAISAH--SEYRALAEKHINELDERLWMGTVHSMVAGRLAVL 969
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITpdSLDGSRtgVFIGSGIGdyAALLLLDEDGGPRRGSPFAVGTMPSVIAGRISYF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   970 MGIRGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL---KTLLDHHSTNSFSVDGSGFCRSDG 1045
Cdd:pfam00109  160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEaDVALAGGVNLLLTPLGFAGFsaaGMLSPDGPCKAFDPFADGFVRGEG 239
                          250
                   ....*....|.
gi 392926054  1046 VGVIILKTAEK 1056
Cdd:pfam00109  240 VGAVVLKRLSD 250
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
5259-5480 3.04e-48

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 175.13  E-value: 3.04e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5259 RVAVIGWSAEFSGSSNIHEYWENLMDGICSTG------------------------NNKYLLKNPFGFDNKFFNLTDEDA 5314
Cdd:pfam00109    2 PVAIVGMGCRFPGGNDPEEFWENLLEGRDGISeipadrwdpdklydppsriagkiyTKWGGLDDIFDFDPLFFGISPREA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5315 RVLDPQVRKFIQHAYLALENSGYV-KQKHELRCGVFAGAEPSDYG--RADDHDDAMRK---LFVMNMNSYLASYASYCLD 5388
Cdd:pfam00109   82 ERMDPQQRLLLEAAWEALEDAGITpDSLDGSRTGVFIGSGIGDYAalLLLDEDGGPRRgspFAVGTMPSVIAGRISYFLG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5389 LKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGFDDQKktMFSKSGVCRPFDKDSEGIVRGSG 5468
Cdd:pfam00109  162 LRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAG--MLSPDGPCKAFDPFADGFVRGEG 239
                          250
                   ....*....|..
gi 392926054  5469 VGCFVLKRYSQA 5480
Cdd:pfam00109  240 VGAVVLKRLSDA 251
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
6678-7481 3.25e-48

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 192.76  E-value: 3.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6678 HIVFNQHHILTDGWSMTVLSDTVSSLY-AAYRGETSFPSKTKQTISQVAM---GTKSSGDIKEALEYYQNTYHTII---- 6749
Cdd:COG1020   144 LLLLALHHIISDGLSDGLLLAELLRLYlAAYAGAPLPLPPLPIQYADYALwqrEWLQGEELARQLAYWRQQLAGLPplle 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6750 -PYD-SETGNTSPSYVRISKLIPSKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LI 6826
Cdd:COG1020   224 lPTDrPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEgLV 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6827 GYFMNNALFKTSLPFEiLRLEEILNIVLNSLEKSRSFATIPFYQMVE---QNRKLNEISLF---FNFrQKLDYPTVSMFG 6900
Cdd:COG1020   304 GFFVNTLPLRVDLSGD-PSFAELLARVRETLLAAYAHQDLPFERLVEelqPERDLSRNPLFqvmFVL-QNAPADELELPG 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6901 AKCEIEHLSLNNA-FDFSFTIDETPTGSLITVDFDKSKYLDTTVHMFANIFLkklNNLRNM--NTTIPIRRTDFPSTLFQ 6977
Cdd:COG1020   382 LTLEPLELDSGTAkFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLV---TLLEALaaDPDQPLGDLPLLTAAER 458
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6978 KGLFTSW--------------RLFTE--------PALLLSTNTVSYSDLAEKIEniskdiqkqlQIA---KATSVREDEL 7032
Cdd:COG1020   459 QQLLAEWnataapypadatlhELFEAqaartpdaVAVVFGDQSLTYAELNARAN----------RLAhhlRALGVGPGDL 528
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7033 VGLdcknsYF--------ALLACVFLGLPYAPIDPTWPEPRQLFV--KSKVSF-------------------TLENCFSC 7083
Cdd:COG1020   529 VGV-----CLerslemvvALLAVLKAGAAYVPLDPAYPAERLAYMleDAGARLvltqsalaarlpelgvpvlALDALALA 603
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7084 NLKLRNFNSRTQFGSI-YSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLdsvkQV----FDVSVSNIIGS 7158
Cdd:COG1020   604 AEPATNPPVPVTPDDLaYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVL----QFaslsFDASVWEIFGA 679
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7159 VLNGG--VLISSEHSTT---ITDQLQKCQ--YAFLPAAVFNGFTDKTMSRLESIETLTIGGETVSDVVIETAMKKFPRLR 7231
Cdd:COG1020   680 LLSGAtlVLAPPEARRDpaaLAELLARHRvtVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGAR 759
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7232 TIQIYGPTETCIWSLTNKC-----KVSTLNIGSAlgdsLSNETCTICNNS-------VRGNVQVKGISLARGYI-----T 7294
Cdd:COG1020   760 LVNLYGPTETTVDSTYYEVtppdaDGGSVPIGRP----IANTRVYVLDAHlqpvpvgVPGELYIGGAGLARGYLnrpelT 835
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7295 SA-----PHGTPFSDIYSTGDIV----DsklNSLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVLY-----SN 7360
Cdd:COG1020   836 AErfvadPFGFPGARLYRTGDLArwlpD---GNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAredapGD 912
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7361 QMLIAFIVDQKSKLLHDSLVKTLKNRTQ----IPDYFVQINKMPLNSSGKVDKSLLLQAFENIRksyKREIVVMKNSLEE 7436
Cdd:COG1020   913 KRLVAYVVPEAGAAAAAALLRLALALLLppymVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA---AAAAAPPAEEEEE 989
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*
gi 392926054 7437 KVINVFSKILGRNVAPTDKFESIGGNSLNAIQIAHRLAEELKIEI 7481
Cdd:COG1020   990 EAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLL 1034
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
3203-3377 8.26e-43

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 156.49  E-value: 8.26e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTA----KALREFEHWKSKVHTIAADINDKE---KLIRELTKLNV 3275
Cdd:smart00822    1 GTYLITGGLGGLGRALARWLAERGARRLVLLSRSGPDApgaaALLAELEAAGARVTVVACDVADRDalaAVLAAIPAVEG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3276 GITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHfnYKIENFIMMSSFTAACGNEGQLNYGVSNAYLEY 3355
Cdd:smart00822   81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTAD--LPLDFFVLFSSIAGVLGSPGQANYAAANAFLDA 158
                           170       180
                    ....*....|....*....|..
gi 392926054   3356 QVQRRRRQGKSGCAIQWGNWID 3377
Cdd:smart00822  159 LAEYRRARGLPALSIAWGAWAE 180
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
3200-3424 3.72e-42

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 161.78  E-value: 3.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3200 PITGNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWK---SKVHTIAADINDKE---KLIRELTKL 3273
Cdd:cd05274   148 GLDGTYLITGGLGGLGLLVARWLAARGARHLVLLSRRGPAPRAAARAALLRaggARVSVVRCDVTDPAalaALLAELAAG 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3274 nVGITGIIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHfnyKIENFIMMSSFTAACGNEGQLNYGVSNAY 3352
Cdd:cd05274   228 -GPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGaLNLHELTPDL---PLDFFVLFSSVAALLGGAGQAAYAAANAF 303
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926054 3353 LEYQVQRRRRQGKSGCAIQWGNWIDTGMATDENVRKFLANLGFLGQHNKDALKYLRACILTKPELIMVANID 3424
Cdd:cd05274   304 LDALAAQRRRRGLPATSVQWGAWAGGGMAAAAALRARLARSGLGPLAPAEALEALEALLASDAPQAVVASVD 375
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
830-1197 5.72e-41

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 155.56  E-value: 5.72e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    830 IACdyQFAGVEGEKELWDTLLtsrlttgkisdirkkqcegdAGLEvgllkqDISMFDNSFFAIAKDEAEFLDPQHRLLLN 909
Cdd:smart00825    6 MSC--RFPGADDPEEFWDLLL--------------------AGLD------DVDLFDAAFFGISPREAEAMDPQQRLLLE 57
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    910 AAYNALEKSGltsIPDADLflaisahseyralaekhinelderlwMGTvhsmvagRLAVLMGIRGR--AMIVDTTCSSVA 987
Cdd:smart00825   58 VAWEALEDAG---IDPESL--------------------------RGS-------RTGVFVGVSSSdySVTVDTACSSSL 101
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    988 TALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSLKTL--L--DHHStNSFSVDGSGFCRSDGVGVIILKTAEK----GD 1058
Cdd:smart00825  102 VALHLACQSLRSGEcDMALAGGVNLILSPDTFVGLSRAgmLspDGRC-KTFDASADGYVRGEGVGVVVLKRLSDalrdGD 180
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   1059 S--AVIKiSSAkSHHCGA---VMTPvvSSISQLLeeagsfsyveghgtatsagdsaesmayqkLGselimsSVKAQFGHC 1133
Cdd:smart00825  181 PilAVIR-GSA-VNQDGRsngITAP--SGPAQLL-----------------------------IG------SVKSNIGHL 221
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054   1134 EVASGLIQLMKVSSIGKHGIIPSIVHNILPSEHIRNNE-NIRLPFVAEEKQID----RSAIVSFGITGT 1197
Cdd:smart00825  222 EAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEEsPLRVPTELTPWPPPgrprRAGVSSFGFGGT 290
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
3203-3377 3.20e-40

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 149.25  E-value: 3.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPT----AKALREFEHWKSKVHTIAADINDK---EKLIRELTKLNV 3275
Cdd:pfam08659    1 GTYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPrpdaQALIAELEARGVEVVVVACDVSDPdavAALLAEIKAEGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3276 GITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFNykIENFIMMSSFTAACGNEGQLNYGVSNAYLEY 3355
Cdd:pfam08659   81 PIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEP--LDFFVLFSSIAGLLGSPGQANYAAANAFLDA 158
                          170       180
                   ....*....|....*....|..
gi 392926054  3356 QVQRRRRQGKSGCAIQWGNWID 3377
Cdd:pfam08659  159 LAEYRRSQGLPATSINWGPWAE 180
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
3644-3925 3.61e-40

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272922 [Multi-domain]  Cd Length: 290  Bit Score: 153.01  E-value: 3.61e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3644 SKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQsclkKCDEYLQgdVSLWEILFNTDhYKLLQLTKHMQPIMFCFGYATA 3723
Cdd:TIGR00128    1 MKIAYVFPGQGSQTVGMGKDLYEQYPIAKELFD----QASEALG--YDLKKLCQEGP-AEELNKTQYTQPALYVVSAILY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3724 QLWL-SLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENI-----AGLGALLAVQREIADEVLRKFK--- 3794
Cdd:TIGR00128   74 LKLKeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAvpeggGAMAAVIGLDEEQLAQACEEATend 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3795 VSVATINSPKQVVFAGTKSVLDAALAFVKGQG-KQATYVNQQYPFHSNLIQETHLvSLRQCLADIKFSAGRTPLVSNVTG 3873
Cdd:TIGR00128  154 VDLANFNSPGQVVISGTKDGVEAAAALFKEMGaKRAVPLEVSGAFHSRFMKPAAE-KFAETLEACQFNDPTVPVISNVDA 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392926054  3874 QIINTFSEA--YIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:TIGR00128  233 KPYTNGDRIkeKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGLIKRI 286
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
7000-7356 5.07e-38

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 150.49  E-value: 5.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7000 SYSDLAEKIENISKdiqkqlQIAKATSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPRqlfvkskVSFT 7076
Cdd:TIGR01733    1 TYRELDERANRLAR------HLRAAGGVGPGDRVAVLLERSaelVVAILAVLKAGAAYVPLDPAYPAER-------LAFI 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7077 LENC--------------FSCNLKLRNFNSRTQFGSI-------------------YSIFTSGSTGVPKGVLMAEQSVSS 7123
Cdd:TIGR01733   68 LEDAgarllltdsalasrLAGLVLPVILLDPLELAALddapappppdapsgpddlaYVIYTSGSTGRPKGVVVTHRSLVN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7124 FMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGG--VLISSEHSTTITDQLQ------KCQYAFLPAAVFNGFT 7195
Cdd:TIGR01733  148 LLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGAtlVVPPEDEERDDAALLAaliaehPVTVLNLTPSLLALLA 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7196 DKTMSRLESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKC------KVSTLNIGSALGdslsNET 7269
Cdd:TIGR01733  228 AALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVdpddapRESPVPIGRPLA----NTR 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7270 CTICNNSVR-------GNVQVKGISLARGY-----------ITSAPHGTPFSDIYSTGDIVdsKLNS---LQYIGRMDSQ 7328
Cdd:TIGR01733  304 LYVLDDDLRpvpvgvvGELYIGGPGVARGYlnrpeltaerfVPDPFAGGDGARLYRTGDLV--RYLPdgnLEFLGRIDDQ 381
                          410       420
                   ....*....|....*....|....*...
gi 392926054  7329 VKCKGVRINISEIEKELILCLGLLQIVV 7356
Cdd:TIGR01733  382 VKIRGYRIELGEIEAALLRHPGVREAVV 409
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
5274-5641 2.07e-36

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 145.99  E-value: 2.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5274 NIHEYWENLMDGICST------------------GNNKYLLKNPFGFDNKFFNLtDEDARVLDPQVR--KFIQHA----Y 5329
Cdd:PTZ00050    8 GAESTWEALIAGKSGIrkltefpkflpdcipeqkALENLVAAMPCQIAAEVDQS-EFDPSDFAPTKResRATHFAmaaaR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5330 LALENSGyVKQKHEL---RCGVFAGaepSDYGRADDHDDAMRKL-----------FVMNM-NSYLASYASYCLDLKGEAV 5394
Cdd:PTZ00050   87 EALADAK-LDILSEKdqeRIGVNIG---SGIGSLADLTDEMKTLyekghsrvspyFIPKIlGNMAAGLVAIKHKLKGPSG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5395 SVYSACSTALVAVANAVKSIQSGSMDYALVGA--ASIAEVSgaLSGFDdQKKTMFSK-----SGVCRPFDKDSEGIVRGS 5467
Cdd:PTZ00050  163 SAVTACATGAHCIGEAFRWIKYGEADIMICGGteASITPVS--FAGFS-RMRALCTKynddpQRASRPFDKDRAGFVMGE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5468 GVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRAsfmAPNPAGQ--LKCMTDVLARFTNKEKERISFVECHATGTTL 5545
Cdd:PTZ00050  240 GAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHIT---APHPDGRgaRRCMENALKDGANININDVDYVNAHATSTPI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5546 GDTIEMNSLRTAY--SFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFsEFRDGMGQFFTVNGKKSTI 5623
Cdd:PTZ00050  317 GDKIELKAIKKVFgdSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINL-ENPDAECDLNLVQGKTAHP 395
                         410
                  ....*....|....*....
gi 392926054 5624 SQNSLISI-DSFGIGGTNV 5641
Cdd:PTZ00050  396 LQSIDAVLsTSFGFGGVNT 414
PRK12316 PRK12316
peptide synthase; Provisional
6990-7513 8.73e-35

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 149.34  E-value: 8.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLAEKIENISKDIqkqlqiaKATSVREDELVGLDCKNSY---FALLACVFLGLPYAPIDPTWPEPRq 7066
Cdd:PRK12316 2020 IAVVFGDQHLSYAELDSRANRLAHRL-------RARGVGPEVRVAIAAERSFelvVALLAVLKAGGAYVPLDPNYPAER- 2091
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7067 lfvkskVSFTLENC-------------------------FSCNLKLRNFNSRTQFGSI------YSIFTSGSTGVPKGVL 7115
Cdd:PRK12316 2092 ------LAYMLEDSgaallltqrhllerlplpagvarlpLDRDAEWADYPDTAPAVQLagenlaYVIYTSGSTGLPKGVA 2165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7116 MAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEHSTTITDQL------QKCQYAFLPAA 7189
Cdd:PRK12316 2166 VSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLydemerHGVTILDFPPV 2245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7190 VFNGFTDKTM--SRLESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKCK------VSTLNIGSAL 7261
Cdd:PRK12316 2246 YLQQLAEHAErdGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRpqdpcgAAYVPIGRAL 2325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7262 GDS---LSNETCTICNNSVRGNVQVKGISLARGYI----------TSAPHGTPFSDIYSTGDIVDSKLN-SLQYIGRMDS 7327
Cdd:PRK12316 2326 GNRrayILDADLNLLAPGMAGELYLGGEGLARGYLnrpgltaerfVPDPFSASGERLYRTGDLARYRADgVVEYLGRIDH 2405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7328 QVKCKGVRINISEIEKELILCLGLLQIVVL----YSNQMLIAFIV-DQKSKLLHDSLVKTLKNRT---QIPDYFVQINKM 7399
Cdd:PRK12316 2406 QVKIRGFRIELGEIEARLQAHPAVREAVVVaqdgASGKQLVAYVVpDDAAEDLLAELRAWLAARLpayMVPAHWVVLERL 2485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7400 PLNSSGKVDKSLLLQAFENIRksyKREIVVMKNSLEEKVINVFSKILG-RNVAPTDKFESIGGNSLNAIQIAHRLAEELK 7478
Cdd:PRK12316 2486 PLNPNGKLDRKALPKPDVSQL---RQAYVAPQEGLEQRLAAIWQAVLKvEQVGLDDHFFELGGHSLLATQVVSRVRQDLG 2562
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 392926054 7479 IEIKAHEILQSNSLKTF---CNTLKNSVQKPISKVPNV 7513
Cdd:PRK12316 2563 LEVPLRILFERPTLAAFaasLESGQTSRAPVLQKVTRV 2600
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
129-390 7.43e-30

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 126.73  E-value: 7.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  129 MATGNSAsvmcgrITYflNSRGAAVGIETACSSSLVAFHLARQAIQSGETKlALVCGA--------NHVGSRSFHSLYNS 200
Cdd:PTZ00050  146 MAAGLVA------IKH--KLKGPSGSAVTACATGAHCIGEAFRWIKYGEAD-IMICGGteasitpvSFAGFSRMRALCTK 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  201 HMVSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNP-----ISQYEVQLE 275
Cdd:PTZ00050  217 YNDDPQRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAH--HITAPHPdgrgaRRCMENALK 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  276 ALKNIDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSD----IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQL 351
Cdd:PTZ00050  295 DGANININDVDYVNAHATSTPIGDKIELKAIKKVFGDSgapkLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTI 374
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392926054  352 HLELPSEDLGEDKSMGFVNEEMELNRVAIS-SYGFGGTNA 390
Cdd:PTZ00050  375 NLENPDAECDLNLVQGKTAHPLQSIDAVLStSFGFGGVNT 414
Acyl_transf_1 pfam00698
Acyl transferase domain;
3647-3924 1.41e-29

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 123.35  E-value: 1.41e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3647 VLMLTGQGSQYPMMGRQLVENYEIFRTTLqsclKKCDEYL--QGDVSLWEILFNTDHyKLLQLTKHMQPIMFCFGYATAQ 3724
Cdd:pfam00698    1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVI----DRADEAFkpQYGFSVSDVLRNNPE-GTLDGTQFVQPALFAMQIALAA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3725 LWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIAGLGALLAVQREIADEVLRKF-KVSVATINSP 3803
Cdd:pfam00698   76 LLQSYGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPdDVVGAVVNSP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3804 KQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIqETHLVSLRQCLADIKFSAGRTPLVSNVTGQIIN--TFSE 3881
Cdd:pfam00698  156 RSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQM-DAIAPALLSALADIAPRTPRVPFISSTSIDPSDqrTLSA 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 392926054  3882 AYIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKR 3924
Cdd:pfam00698  235 EYWVRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALID 277
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
126-599 2.33e-27

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 124.73  E-value: 2.33e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   126 DQYMA------TGNSASVMCGRITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGanhVGSRSFHSLYN 199
Cdd:TIGR02813  167 DQYIHweensfPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---VCTDNSPFMYM 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   200 SHMVSP----NGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPisqyEVQLE 275
Cdd:TIGR02813  244 SFSKTPafttNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRP----EGQAK 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   276 ALKNIDKD------SVQLVTCHGTGTKLGDQVELTAINRSFKSD------IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQ 343
Cdd:TIGR02813  320 ALKRAYDDagfaphTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALH 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   344 HGIIPNQLHLELPSEDLGEDKSMGFVNEEMEL---------NRVAISSYGFGGTNACAIIEK--PEKPSLVQKESYAESN 412
Cdd:TIGR02813  400 HKVLPPTINVDQPNPKLDIENSPFYLNTETRPwmqredgtpRRAGISSFGFGGTNFHMVLEEysPKHQRDDQYRQRAVAQ 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   413 VLFLSAKSHESLklqIEEYTQFMAQSDSAMEDILYTVNERKTKYDFRA-----AVFG---KDNEEIARKLQDgdySLTNL 484
Cdd:TIGR02813  480 TLLFTAANEKAL---VSSLKDWKNKLSAKADDQPYAFNALAVENTLRTiavalARLGfvaKNADELITMLEQ---AITQL 553
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   485 QESTFE---VEFGEGNEKLWLLRMLYEKNETFHSTVDKYCKLAE--TCGFPEARTAL------FFPFKLT-LTPLTYNVS 552
Cdd:TIGR02813  554 EAKSCEewqLPSGISYRKSALVVESGKVAALFAGQGSQYLNMGRelACNFPEVRQAAadmdsvFTQAGKGaLSPVLYPIP 633
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   553 RL-----------------------ISSMATFELLVQYNTLPNKLRGKGLGQIFCLAVAKVITFESAVQL 599
Cdd:TIGR02813  634 VFndesrkaqeealtntqhaqsaigTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMML 703
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
1885-2355 6.16e-24

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 113.18  E-value: 6.16e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1885 RLAENPIGVMAAAcRLPGGVSSPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNP--VEGGNFITQdvTQFDPSF 1962
Cdd:TIGR02813    3 RLKDMPIAIVGMA-SIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADKsyCKRGGFLPE--VDFNPME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1963 FKISKSEAELIDPQQRLLLECVQECLENSGVIETSN---VGVFVG----------------------------------- 2004
Cdd:TIGR02813   80 FGLPPNILELTDISQLLSLVVAKEVLNDAGLPDGYDrdkIGITLGvgggqkqssslnarlqypvlkkvfkasgvededse 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2005 LMEKEYQDMM---ESSSILAMLGSmaaVIAGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGV--- 2078
Cdd:TIGR02813  160 MLIKKFQDQYihwEENSFPGSLGN---VISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVctd 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2079 ----NLILNEKGQGLRTNGKMlsqhgMSLSFDSRASGYGRSDGCVVLM-LELAKPNFHYM-STIQSVNVNHGGRSVSLTA 2152
Cdd:TIGR02813  237 nspfMYMSFSKTPAFTTNEDI-----QPFDIDSKGMMIGEGIGMMALKrLEDAERDGDRIyAVIKGVGASSDGKFKSIYA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2153 PNGVAHKMLLTSVINQS---PSlAIDYWEAHGTGTPLGDPIEFNTLSSI-------LQNIIIGSVKASLGHGEASAGTCG 2222
Cdd:TIGR02813  312 PRPEGQAKALKRAYDDAgfaPH-TCGLIEAHGTGTAAGDVAEFGGLVSVfsqdndqKQHIALGSVKSQIGHTKSTAGTAG 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2223 LLKLFLMLTYQYVPTLIHFHVLNKDINA--------GSIRLPIIGEDSELVSAGISSFGVSGTNAAAIafndnnkLEPYI 2294
Cdd:TIGR02813  391 MIKAVLALHHKVLPPTINVDQPNPKLDIenspfylnTETRPWMQREDGTPRRAGISSFGFGGTNFHMV-------LEEYS 463
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926054  2295 PIH----KY------YILPISAKNQISLdnlekqilsVIPLTDVPicNIASALANNRS-HFtirNALIVSNS 2355
Cdd:TIGR02813  464 PKHqrddQYrqravaQTLLFTAANEKAL---------VSSLKDWK--NKLSAKADDQPyAF---NALAVENT 521
AMP-binding pfam00501
AMP-binding enzyme;
6997-7332 5.97e-22

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 102.78  E-value: 5.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6997 NTVSYSDLAEKIENISKdiqkQLQIAKatsVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPRQLFV---- 7069
Cdd:pfam00501   20 RRLTYRELDERANRLAA----GLRALG---VGKGDRVAILLPNSpewVVAFLACLKAGAVYVPLNPRLPAEELAYIleds 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7070 KSKVSFTLENCFSCNLK------------------------LRNFNSRTQFGSIYS------------IFTSGSTGVPKG 7113
Cdd:pfam00501   93 GAKVLITDDALKLEELLealgklevvklvlvldrdpvlkeePLPEEAKPADVPPPPppppdpddlayiIYTSGTTGKPKG 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7114 VLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQV----FDVSVS-NIIGSVLNGG--VLISSEHSTTITDQLQ-----KC 7181
Cdd:pfam00501  173 VMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTlplfHDFGLSlGLLGPLLAGAtvVLPPGFPALDPAALLElieryKV 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7182 QYAFLPAAVFNGFTDK---TMSRLESIETLTIGGETVSDVVIETAMKKFPRlRTIQIYGPTETCIWSLTN----KCKVST 7254
Cdd:pfam00501  253 TVLYGVPTLLNMLLEAgapKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVTTPlpldEDLRSL 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7255 LNIGSALGDS----LSNETCTICNNSVRGNVQVKGISLARGYitsapHGTP--------FSDIYSTGDIV----DSklnS 7318
Cdd:pfam00501  332 GSVGRPLPGTevkiVDDETGEPVPPGEPGELCVRGPGVMKGY-----LNDPeltaeafdEDGWYRTGDLGrrdeDG---Y 403
                          410
                   ....*....|....
gi 392926054  7319 LQYIGRMDSQVKCK 7332
Cdd:pfam00501  404 LEIVGRKKDQIKLG 417
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
6558-6980 5.33e-21

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 100.49  E-value: 5.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6558 DAIPLTNSQTQMFMLRQIDT-TSKYNLifKITISYETKFVWEFLKYSLHSLIAYQPSYRTVF--KSGNSPYQYIcsLTES 6634
Cdd:pfam00668    3 DEYPLSPAQKRMWFLEKLEPhSSAYNM--PAVLKLTGELDPERLEKALQELINRHDALRTVFirQENGEPVQVI--LEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6635 FHDF-----------DKRCNLNNAISHEPNHLFEIGKSTPLR---VRVAEDcdnsRIHIVFNQHHILTDGWSMTVLSDTV 6700
Cdd:pfam00668   79 PFELeiidisdlsesEEEEAIEAFIQRDLQSPFDLEKGPLFRaglFRIAEN----RHHLLLSMHHIIVDGVSLGILLRDL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6701 SSLYAAYRGETSFPSKTKQTISQVAMGTKS---SGDIKEALEYYQNT-----YHTIIPYDSETgNTSPSYV--RISKLIP 6770
Cdd:pfam00668  155 ADLYQQLLKGEPLPLPPKTPYKDYAEWLQQylqSEDYQKDAAYWLEQlegelPVLQLPKDYAR-PADRSFKgdRLSFTLD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6771 SKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRN-ADNSELIGYFMNnalfktSLPFEI-----L 6844
Cdd:pfam00668  234 EDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPsPDIERMVGMFVN------TLPLRIdpkggK 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6845 RLEEILNIVLNSLEKSRSFATIPFYQMVEQNR--------KLNEISLFF-NFRQKLDYPTVSMFGAKCEIEHLSLNNAFD 6915
Cdd:pfam00668  308 TFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRlprdlsrhPLFDPMFSFqNYLGQDSQEEEFQLSELDLSVSSVIEEEAK 387
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054  6916 FSFTIDETPTGSLITVDFD--KSKYLDTTVHMFANIFLKKLNNLRNmNTTIPIRRTDFPSTLFQKGL 6980
Cdd:pfam00668  388 YDLSLTASERGGGLTIKIDynTSLFDEETIERFAEHFKELLEQAIA-HPSQPLSELDLLSDAEKQKL 453
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
4342-4628 2.02e-17

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 88.75  E-value: 2.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4342 GVFIGCS-----ANEFshivyAYGYKDPR-----AEWSGGTSN-SALAGRIAHWLKLKGPVVTLDTACSSSFYALSAACD 4410
Cdd:PRK09185   98 GVVLGTStsgilEGEL-----AYRRRDPAhgalpADYHYAQQElGSLADFLRAYLGLSGPAYTISTACSSSAKVFASARR 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4411 ALRTGQCEYAIVGTVnlvmhemttDVLqnAKMTVDDF----------CKAFDVDANGYKRSEAVCSMLLTKSPNiDSVAT 4480
Cdd:PRK09185  173 LLEAGLCDAAIVGGV---------DSL--CRLTLNGFnsleslspqpCRPFSANRDGINIGEAAAFFLLEREDD-AAVAL 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4481 ItnyatGHnGTSS-----SLFTPNGLSQLEVMQRATN-----PlEKILEIQTHCTGTKLGDPIEINAISKLVSSACKIGS 4550
Cdd:PRK09185  241 L-----GV-GESSdahhmSAPHPEGLGAILAMQQALAdaglaP-ADIGYINLHGTATPLNDAMESRAVAAVFGDGVPCSS 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4551 VKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLK-----CPTNSIKTNkmicrfigEDADENNSILINNFGFTGSNCS 4625
Cdd:PRK09185  314 TKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGqpdpaLPPLYLVEN--------AQALAIRYVLSNSFAFGGNNCS 385

                  ...
gi 392926054 4626 VVL 4628
Cdd:PRK09185  386 LIF 388
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
7527-7737 2.05e-17

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 91.30  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7527 IYLVHAIGGTIYPYYSFLQIFPKDISLYGIEF----DLKYPSNDLRELAHFYAEEIAAHAGNKRIFVMGHSMGGIMSREI 7602
Cdd:COG3319   604 LFCVHPAGGNVLCYRPLARALGPDRPVYGLQApgldGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEM 683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7603 VAELKIWGYDIPFVMLFDSWV--LRTNELDIENIKQFITYVFSGLP-----------DSEHRINRAIKLA---------- 7659
Cdd:COG3319   684 ARQLEAQGEEVALLVLLDSYApgALARLDEAELLAALLRDLARGVDlpldaeelralDPEERLARLLERLreaglpagld 763
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7660 ---------------QLLREYKTSVSDTKLYLFkskqlgdaafkkavRSDLNEELSRSMTCNGFDELSLQPVETYLIDGD 7724
Cdd:COG3319   764 aerlrrllrvfranlRALRRYRPRPYDGPVLLF--------------RAEEDPPGRADDPALGWRPLVAGGLEVHDVPGD 829
                         250
                  ....*....|...
gi 392926054 7725 HESCLKAENLKKV 7737
Cdd:COG3319   830 HFSMLREPHVAEL 842
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
6560-6954 6.24e-17

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 87.46  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6560 IPLTNSQTQMFMLRQIDTTSKynlIFKITISYETK--FVWEFLKYSLHSLIAYQPSYRTVFKSGN-SPYQYICSLTESF- 6635
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPS---AFNVAIEMFLTgsLDLARLKQALDAVMERHDVLRTRFCEEAgRYEQVVLDKTVRFr 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6636 -------HDFDKRCNLN---NAISHEPnhlFEIGKSTPLR---VRVAEDcdnsRIHIVFNQHHILTDGWSMTVLSDTVSS 6702
Cdd:cd19066    79 ieiidlrNLADPEARLLeliDQIQQTI---YDLERGPLVRvalFRLADE----RDVLVVAIHHIIVDGGSFQILFEDISS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6703 LY-AAYRGETSFPSKTKQTISQVAMGTK--SSGDIKEALEYYQNTYHTI-----IPYDSETGnTSPSY--VRISKLIPSK 6772
Cdd:cd19066   152 VYdAAERQKPTLPPPVGSYADYAAWLEKqlESEAAQADLAYWTSYLHGLppplpLPKAKRPS-QVASYevLTLEFFLRSE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6773 IWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LIGYFMNNALF--KTSLPFEilrLEEI 6849
Cdd:cd19066   231 ETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEdTIGLFLNLLPLriDTSPDAT---FPEL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6850 LNIVLNSLEKSRSFATIPFYQMVEQ--------NRKLNEISL-FFNFRQKLDYPTVSMFGAkcEIEHLSLNNAFDFSFTI 6920
Cdd:cd19066   308 LKRTKEQSREAIEHQRVPFIELVRHlgvvpeapKHPLFEPVFtFKNNQQQLGKTGGFIFTT--PVYTSSEGTVFDLDLEA 385
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 392926054 6921 DETPTGSL-ITVDFDKSKYLDTTVHMFANIFLKKL 6954
Cdd:cd19066   386 SEDPDGDLlLRLEYSRGVYDERTIDRFAERYMTAL 420
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
4991-5131 7.38e-16

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 83.59  E-value: 7.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4991 VFHLAGIVNNSLHENVKRDSLDEMVSIKLQGAKNLmkcCDET-----SHFVFSSSIANVLGSYGQSNYAFSNGLVTSFLE 5065
Cdd:cd05274   233 VIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNL---HELTpdlplDFFVLFSSVAALLGGAGQAAYAAANAFLDALAA 309
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 5066 TSST---KSTIIHWGPWKDVGMLAqpeRREIVKQIESNGWKLLPNQDAISVFYTQFMETHEQIIVFDGD 5131
Cdd:cd05274   310 QRRRrglPATSVQWGAWAGGGMAA---AAALRARLARSGLGPLAPAEALEALEALLASDAPQAVVASVD 375
PLN02752 PLN02752
[acyl-carrier protein] S-malonyltransferase
3643-3925 1.31e-15

[acyl-carrier protein] S-malonyltransferase


Pssm-ID: 215401 [Multi-domain]  Cd Length: 343  Bit Score: 82.50  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3643 SSKCVLMLTGQGSQYPMMGRQLVENyeifrTTLQSCLKKCDEYLQGDvsLWEILFNTDHYKLlQLTKHMQPIMFCFGYAT 3722
Cdd:PLN02752   37 KPTTAFLFPGQGAQAVGMGKEAAEV-----PAAKALFDKASEILGYD--LLDVCVNGPKEKL-DSTVVSQPAIYVASLAA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3723 AQLWLSLGIVP------DYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIA-----------GLG--ALLAVQR 3783
Cdd:PLN02752  109 VEKLRARDGGQavidsvDVCAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAAdagpsgmvsviGLDsdKVQELCA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3784 EIADEVLRKFKVSVATINSPKQVVFAGTKSVLDAALAFVKGQG-KQATYVNQQYPFHSNLIqETHLVSLRQCLADIKFSA 3862
Cdd:PLN02752  189 AANEEVGEDDVVQIANYLCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFM-EPAVDALEAALAAVEIRT 267
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054 3863 GRTPLVSNVTGQIintFSEAYIVKHT-----VSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:PLN02752  268 PRIPVISNVDAQP---HSDPATIKKIlarqvTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGIVKRV 332
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
867-1206 1.40e-15

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 83.24  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  867 CEGDAGLEvgllkqDISMFDNSFFA--IAK-----DEAEFLDPQH--------RLLLNAAYNALEKSGLT-SIPDADLFl 930
Cdd:PRK08439   27 CNGECGIK------KITLFDASDFPvqIAGeitdfDPTEVMDPKEvkkadrfiQLGLKAAREAMKDAGFLpEELDAERF- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  931 AISAHSEYRALA--EKHINELDER--------LWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREG 1000
Cdd:PRK08439  100 GVSSASGIGGLPniEKNSIICFEKgprkispfFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1001 ---RKFAIVATSQL----IQSSKWLYSLKTLLDH--HSTNSFSVDGSGFCRSDGVGVIILKTAEKGDSAVIKI------- 1064
Cdd:PRK08439  180 gadKMLVVGAESAIcpvgIGGFAAMKALSTRNDDpkKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIyaeiigf 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1065 -SSAKSHHcgaVMTPVV----SSISQLLEEAGS--FSYVEGHGTATSAGDSAESMAYQKL--GSELI--MSSVKAQFGHC 1133
Cdd:PRK08439  260 gESGDANH---ITSPAPegplRAMKAALEMAGNpkIDYINAHGTSTPYNDKNETAALKELfgSKEKVppVSSTKGQIGHC 336
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054 1134 EVASGLIQlmKVSSIG--KHGIIPSIVHNILPsehirnNENIRL---PFVAEEKQIDRSAIVSFGITGTKTVVTTERV 1206
Cdd:PRK08439  337 LGAAGAIE--AVISIMamRDGILPPTINQETP------DPECDLdyiPNVARKAELNVVMSNSFGFGGTNGVVIFKKV 406
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
950-1197 4.26e-15

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 84.29  E-value: 4.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   950 DERLWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVATSQLIQSSKWLYSLKTLLDHHS 1029
Cdd:TIGR02813  173 EENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFT 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1030 TNS----FSVDGSGFCRSDGVGVIILK---TAEK-GDS--AVIK-ISSAKSHHCGAVMTP----VVSSISQLLEEAG--- 1091
Cdd:TIGR02813  253 TNEdiqpFDIDSKGMMIGEGIGMMALKrleDAERdGDRiyAVIKgVGASSDGKFKSIYAPrpegQAKALKRAYDDAGfap 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1092 -SFSYVEGHGTATSAGDSAESMAYQKLGSE-------LIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVH---- 1159
Cdd:TIGR02813  333 hTCGLIEAHGTGTAAGDVAEFGGLVSVFSQdndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINvdqp 412
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 392926054  1160 ----NILPSEHIRNNENirLPFVAEEKQIDRSA-IVSFGITGT 1197
Cdd:TIGR02813  413 npklDIENSPFYLNTET--RPWMQREDGTPRRAgISSFGFGGT 453
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
6562-6789 4.95e-15

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 78.54  E-value: 4.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6562 LTNSQTQMFMLRQidTTSKYNLIFKITIsyETKFVWEFLKYSLHSLIAYQPSYRTVFKSGNS-PYQYI---CSLTESFHD 6637
Cdd:COG4908     1 LSPAQKRFLFLEP--GSNAYNIPAVLRL--EGPLDVEALERALRELVRRHPALRTRFVEEDGePVQRIdpdADLPLEVVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6638 F------DKRCNLNNAISHEPNHLFEIGKSTPLRVRVAEdCDNSRIHIVFNQHHILTDGWSMTVLSDTVSSLYAAYRG-- 6709
Cdd:COG4908    77 LsalpepEREAELEELVAEEASRPFDLARGPLLRAALIR-LGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEge 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6710 ETSFPSKTKQTISQVA--MGTKSSGDIKEALEYYQNTY-----HTIIPYD-SETGNTSPSYVRISKLIPSKIWQKLVGLS 6781
Cdd:COG4908   156 PPPLPELPIQYADYAAwqRAWLQSEALEKQLEYWRQQLagappVLELPTDrPRPAVQTFRGATLSFTLPAELTEALKALA 235

                  ....*...
gi 392926054 6782 KLYNTTMY 6789
Cdd:COG4908   236 KAHGATVN 243
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
3203-3381 7.05e-15

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 78.37  E-value: 7.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3203 GNWLITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALR-EFEHWKSKVHTIAADINDKE---KLIRELTKLNVGIT 3278
Cdd:COG0300     6 KTVLITGASSGIGRALARALAARGA-RVVLVARDAERLEALAaELRAAGARVEVVALDVTDPDavaALAEAVLARFGPID 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3279 GIIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN----FIMMSSFTAACGNEGQLNYGVSNAYL 3353
Cdd:COG0300    85 VLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGpVRLTRALLPLM---RARgrgrIVNVSSVAGLRGLPGMAAYAASKAAL 161
                         170       180       190
                  ....*....|....*....|....*....|..
gi 392926054 3354 E-YQVQRRRRQGKSG---CAIQWGnWIDTGMA 3381
Cdd:COG0300   162 EgFSESLRAELAPTGvrvTAVCPG-PVDTPFT 192
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
4991-5081 4.13e-14

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 74.06  E-value: 4.13e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   4991 VFHLAGIVNNSLHENVKRDSLDEMVSIKLQGAKNLMKCCDET--SHFVFSSSIANVLGSYGQSNYAFSNglvtSFLE--- 5065
Cdd:smart00822   85 VIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLplDFFVLFSSIAGVLGSPGQANYAAAN----AFLDala 160
                            90       100
                    ....*....|....*....|
gi 392926054   5066 ----TSSTKSTIIHWGPWKD 5081
Cdd:smart00822  161 eyrrARGLPALSIAWGAWAE 180
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
1901-2280 2.47e-13

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 76.27  E-value: 2.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1901 PGGVSsPSELWELLKIGKNASSRI---PATRVPTRNTLISGSKY--GNPVEGGNFITQDVtqFDPSFFKISKSEAELIdp 1975
Cdd:PTZ00050    4 PLGVG-AESTWEALIAGKSGIRKLtefPKFLPDCIPEQKALENLvaAMPCQIAAEVDQSE--FDPSDFAPTKRESRAT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1976 qqRLLLECVQECLENSGVIETSN-----VGVFVGLMEKEYQDMMESSS--------------ILAMLGSMAAviaGRVNY 2036
Cdd:PTZ00050   79 --HFAMAAAREALADAKLDILSEkdqerIGVNIGSGIGSLADLTDEMKtlyekghsrvspyfIPKILGNMAA---GLVAI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2037 IFGCYGPSVTIDTACSSSLVALEMAINALLDNRcSKVIVAG--------VNLILNEKGQGLRTNGKMLSQHGmSLSFDSR 2108
Cdd:PTZ00050  154 KHKLKGPSGSAVTACATGAHCIGEAFRWIKYGE-ADIMICGgteasitpVSFAGFSRMRALCTKYNDDPQRA-SRPFDKD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2109 ASGYGRSDGCVVLMLE----LAKPNFHYMSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS---PSLAIDYWEAHG 2181
Cdd:PTZ00050  232 RAGFVMGEGAGILVLEelehALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGaniNINDVDYVNAHA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2182 TGTPLGDPIEFNTLSSIL-----QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKD----INAGS 2252
Cdd:PTZ00050  312 TSTPIGDKIELKAIKKVFgdsgaPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAEcdlnLVQGK 391
                         410       420
                  ....*....|....*....|....*...
gi 392926054 2253 IRLPIIGEDSELVsagiSSFGVSGTNAA 2280
Cdd:PTZ00050  392 TAHPLQSIDAVLS----TSFGFGGVNTA 415
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
5803-6010 7.69e-12

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272922 [Multi-domain]  Cd Length: 290  Bit Score: 70.19  E-value: 7.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5803 TQFAQIAIFVQCMAIFKAIKN--VFNPTCLIGHSVGEYAAAVISGALKTEEALKLLIKRSELIGK--TEKARMLMV---W 5875
Cdd:TIGR00128   58 TQYTQPALYVVSAILYLKLKEqgGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEavPEGGGAMAAvigL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5876 NYE--KQLPSHVHVSAIIDANTKC---VV--GPVETIDNLEKYFINNHIKyRNI--ETKHGFHSKMFHCISKEFEFFCES 5946
Cdd:TIGR00128  138 DEEqlAQACEEATENDVDLANFNSpgqVVisGTKDGVEAAAALFKEMGAK-RAVplEVSGAFHSRFMKPAAEKFAETLEA 216
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5947 FATKVPLIPMISSIT------GSEIKifdsKYCTMHLTNPVNLELVVDHIMKLDIDIIVEVGPTGVLSNL 6010
Cdd:TIGR00128  217 CQFNDPTVPVISNVDakpytnGDRIK----EKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGL 282
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
1544-1759 3.71e-11

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


Pssm-ID: 434191  Cd Length: 296  Bit Score: 68.17  E-value: 3.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1544 HVVDSKIVLPGATSIRL----VHQLNGKPT-VELSNIDFLN--KITPSEAPSV---VKIEEQDGLEKLVF---------- 1603
Cdd:pfam14765   33 HRVGGTVVLPGAGYLEMaleaARQLFGGSGaVALRDVSILKalVLPEDDPVEVqtsLTPEEDGADSWWEFeifsragggw 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1604 -------------GETDAISFKLTELQNFNPIPNERLNAEVHHtdnIYERFANSHLTYRNEFQMVDSLKY--TMGKGEVR 1668
Cdd:pfam14765  113 ewtlhatgtvrlaPGEPAAPVDLESLPARCAQPADPRSVSSAE---FYERLAARGLFYGPAFQGLRRIWRgdGEALAEAR 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1669 FVSMKDLD--------ILIDGTLQAIVGCYFFENTNDNSPFVPFTIDQLSILNGDISQKQLHAVLKYDSSGN-FINGDAT 1739
Cdd:pfam14765  190 LPEAAAGGespyllhpALLDAALQLLGAALPAEAEHADQAYLPVGIERLRIYRSLPPGEPLWVHARLERRGGrTIVGDLT 269
                          250       260
                   ....*....|....*....|
gi 392926054  1740 VYDALGNIILHISNVTFKRL 1759
Cdd:pfam14765  270 LVDEDGRVVARIEGLRLRRV 289
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3354 8.72e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 66.05  E-value: 8.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKEKLIR---ELTKLNVGITGII 3281
Cdd:PRK12825   10 LVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELvEAVEALGRRAQAVQADVTDKAALEAavaAAVERFGRIDILV 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEE-----IEKHFNyKIenfIMMSSFTAACGNEGQLNYGVSNAYLE 3354
Cdd:PRK12825   90 NNAGIFEDKPLADMSDDEWDEVIDVNLSGvFHLLRAvvppmRKQRGG-RI---VNISSVAGLPGWPGRSNYAAAKAGLV 164
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2943-3024 1.00e-10

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 61.50  E-value: 1.00e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   2943 ATVDRTEIRRKVSLAVFDLATETL---SAEDLQ-SKGFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDELS 3018
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLghaAAEAIDpDRPFRDLGLDSLMAVELRNRLEAAT--GLRLPATLVFDHPTPAALA 79

                    ....*.
gi 392926054   3019 DHIVRK 3024
Cdd:smart00823   80 EHLAAE 85
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2946-3026 3.11e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 59.87  E-value: 3.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2946 DRTEIRRKVS--LA-VFDLATETLSAED-LqskgFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDELSDHI 3021
Cdd:COG0236     2 PREELEERLAeiIAeVLGVDPEEITPDDsF----FEDLGLDSLDAVELIAALEEEF--GIELPDTELFEYPTVADLADYL 75

                  ....*
gi 392926054 3022 VRKKS 3026
Cdd:COG0236    76 EEKLA 80
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
6237-6393 4.46e-10

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 66.24  E-value: 4.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6237 LVFGANGFIGSIVFR-LLQEMGMNVIPISRASIP-----------------------SCDITNIKDVQNVFKSLG--FKK 6290
Cdd:cd08953   209 LVTGGAGGIGRALARaLARRYGARLVLLGRSPLPpeeewkaqtlaalealgarvlyiSADVTDAAAVRRLLEKVRerYGA 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6291 FSVVINCVGVETSA---KMNKTSLEQeiVLSPKTFGSVNILKCLEEFsiEVDKLVNFSSLSSVVPLLGNFDYASANCF-- 6365
Cdd:cd08953   289 IDGVIHAAGVLRDAllaQKTAEDFEA--VLAPKVDGLLNLAQALADE--PLDFFVLFSSVSAFFGGAGQADYAAANAFld 364
                         170       180       190
                  ....*....|....*....|....*....|
gi 392926054 6366 --VEALTKQGskYIKQFLTLSLPPLEGSRM 6393
Cdd:cd08953   365 afAAYLRQRG--PQGRVLSINWPAWREGGM 392
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
6214-6369 1.15e-09

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 61.42  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6214 LCKHGFRTTEIPSRLHPVSRGHAlvfganGFIgsivfRLLQEMGMNVIPISrasipsCDITNIKDVQNVFKSLGFKKFSV 6293
Cdd:pfam08659   20 LAERGARHLVLLSRSAAPRPDAQ------ALI-----AELEARGVEVVVVA------CDVSDPDAVAALLAEIKAEGPPI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6294 --VINCVGVETSAKMNKTSLEQ-EIVLSPKTFGSVNILKCLEEfsIEVDKLVNFSSLSSvvpLLGNF---DYASANCFVE 6367
Cdd:pfam08659   83 rgVIHAAGVLRDALLENMTDEDwRRVLAPKVTGTWNLHEATPD--EPLDFFVLFSSIAG---LLGSPgqaNYAAANAFLD 157

                   ..
gi 392926054  6368 AL 6369
Cdd:pfam08659  158 AL 159
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
3994-4216 4.11e-09

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


Pssm-ID: 434191  Cd Length: 296  Bit Score: 62.00  E-value: 4.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3994 DEFELLEGHQLNGKIVVAGA-Y---------QLFKIDQLVKLKaagmelmlkNVKFLKPWYIEDNREYQIQ--------- 4054
Cdd:pfam14765   25 ADLPWLRDHRVGGTVVLPGAgYlemaleaarQLFGGSGAVALR---------DVSILKALVLPEDDPVEVQtsltpeedg 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4055 -----------WNSDMTiELIVNSVIVCSLEVEPQNSVLKLETI------SENEKPFEVHDFYETLFRNGLQYDSGFRRI 4117
Cdd:pfam14765   96 adswwefeifsRAGGGW-EWTLHATGTVRLAPGEPAAPVDLESLparcaqPADPRSVSSAEFYERLAARGLFYGPAFQGL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4118 ESARRSDKRCFSQIKSS----PFAWP------LIDSAMHSITASVVP--RRPDCYFLPVAMGSVTMKDTNSFTLPnLHAQ 4185
Cdd:pfam14765  175 RRIWRGDGEALAEARLPeaaaGGESPyllhpaLLDAALQLLGAALPAeaEHADQAYLPVGIERLRIYRSLPPGEP-LWVH 253
                          250       260       270
                   ....*....|....*....|....*....|..
gi 392926054  4186 TVITSETDKFIQVNVALLAGD-TPICEVRNMT 4216
Cdd:pfam14765  254 ARLERRGGRTIVGDLTLVDEDgRVVARIEGLR 285
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2790-2867 9.93e-09

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 55.72  E-value: 9.93e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054   2790 AAKTLQMAVRHKVCLAVGDVIESGLDIDESqlstgFSELGIDSLATVDLLNRLNQKYfpEIELTTSDLFDNPSIIDLS 2867
Cdd:smart00823    9 RRRLLLDLVREQVAAVLGHAAAEAIDPDRP-----FRDLGLDSLMAVELRNRLEAAT--GLRLPATLVFDHPTPAALA 79
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2800-2863 4.16e-08

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 53.34  E-value: 4.16e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926054  2800 HKVCLAVGDVIesGLDIDESQLSTGFSELGIDSLATVDLLNRLNQKYfpEIELTTSDLFDNPSI 2863
Cdd:pfam00550    1 ERLRELLAEVL--GVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEF--GVEIPPSDLFEHPTL 60
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1806-1857 5.17e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 53.79  E-value: 5.17e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 392926054   1806 DIDNTTGFFDLGLTSIQAVKLRNAIKSNYP-NASSTCVFDYPSIDLLSGYLST 1857
Cdd:smart00823   32 AIDPDRPFRDLGLDSLMAVELRNRLEAATGlRLPATLVFDHPTPAALAEHLAA 84
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2808-2875 7.99e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 52.93  E-value: 7.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054 2808 DVIESGLDIDESQLSTG---FSELGIDSLATVDLLNRLNQKYfpEIELTTSDLFDNPSIIDLSIMIEQLLN 2875
Cdd:COG0236    12 EIIAEVLGVDPEEITPDdsfFEDLGLDSLDAVELIAALEEEF--GIELPDTELFEYPTVADLADYLEEKLA 80
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
3485-3549 1.00e-07

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 52.55  E-value: 1.00e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054 3485 IKEKVSSILMCSPTKLKNNKNIM-DMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLEKLAAHI 3549
Cdd:COG0236    10 LAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
6265-6369 1.31e-07

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 55.18  E-value: 1.31e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   6265 RASIPSCDITNIKDVQNVFKSLGFKKFSV--VINCVGVETSAKMNKTSLEQ-EIVLSPKTFGSVNILKCLEEfsIEVDKL 6341
Cdd:smart00822   54 RVTVVACDVADRDALAAVLAAIPAVEGPLtgVIHAAGVLDDGVLASLTPERfAAVLAPKAAGAWNLHELTAD--LPLDFF 131
                            90       100
                    ....*....|....*....|....*...
gi 392926054   6342 VNFSSLSSVVPLLGNFDYASANCFVEAL 6369
Cdd:smart00822  132 VLFSSIAGVLGSPGQANYAAANAFLDAL 159
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
3485-3543 1.90e-07

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 51.41  E-value: 1.90e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054  3485 IKEKVSSILMCSPTKLKNNKNIMDMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLE 3543
Cdd:pfam00550    3 LRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
4943-5081 3.03e-07

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 54.11  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4943 GGIGSAIINEL--KPKSSVIIT-RKNIASEDGKTFL-------------SSDITRLD--------ISHKFNY---VFHLA 4995
Cdd:pfam08659   10 GGLGRELARWLaeRGARHLVLLsRSAAPRPDAQALIaeleargvevvvvACDVSDPDavaallaeIKAEGPPirgVIHAA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4996 GIVNNSLHENVKRDSLDEMVSIKLQGAKNLMKCCDETS--HFVFSSSIANVLGSYGQSNYAFSNGLVTSFLETSSTK--- 5070
Cdd:pfam08659   90 GVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPldFFVLFSSIAGLLGSPGQANYAAANAFLDALAEYRRSQglp 169
                          170
                   ....*....|.
gi 392926054  5071 STIIHWGPWKD 5081
Cdd:pfam08659  170 ATSINWGPWAE 180
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
6237-6299 3.85e-07

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 55.52  E-value: 3.85e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926054 6237 LVFGANGFIGSIVFRLLQEMGMNVIPISRasiPSCDITNIKDVQNVFKSLgfkKFSVVINCVG 6299
Cdd:COG1091     3 LVTGANGQLGRALVRLLAERGYEVVALDR---SELDITDPEAVAALLEEV---RPDVVINAAA 59
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3485-3552 5.34e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 50.71  E-value: 5.34e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054   3485 IKEKVSSILMCSPTKLKN-NKNIMDMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLEKLAAHIFEQ 3552
Cdd:smart00823   17 VREQVAAVLGHAAAEAIDpDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
730-803 4.71e-06

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 47.93  E-value: 4.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054  730 SDAEIESTVRTIVKQFLDIEEDDI----NLLETGAVDSLTSIEMVEAFGTAVNQTMPFDLLEAYPTILNIVDFLKTLV 803
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDPEEItpddSFFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2949-3016 6.59e-06

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 47.17  E-value: 6.59e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054  2949 EIRRKVSlAVFDLATETLSAEDlqskGFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDE 3016
Cdd:pfam00550    2 RLRELLA-EVLGVPAEEIDPDT----DLFDLGLDSLLAVELIARLEEEF--GVEIPPSDLFEHPTLAE 62
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
376-431 6.77e-06

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 48.70  E-value: 6.77e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054   376 NRVAISSYGFGGTNACAIIEKPEKPSLVQKESYAESNVLFLSAKSHESLKLQIEEY 431
Cdd:pfam16197   25 GIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKALLEKL 80
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
4614-4695 1.03e-05

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 47.92  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4614 INNFGFTGSNCSVVLK--PKNAISEhFVSSEVFYPILLSSHSAKSLQKYVQVL------CEFISnsakSLHDImmslFQK 4685
Cdd:pfam16197   29 VNSFGFGGANAHVILKsnPKPKIPP-ESPDNLPRLVLLSGRTEEAVKALLEKLenhlddAEFLS----LLNDI----HSL 99
                           90
                   ....*....|..
gi 392926054  4686 KI--HVHRQFII 4695
Cdd:pfam16197  100 PIsgHPYRGYAI 111
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
5167-5235 1.12e-04

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 44.07  E-value: 1.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 5167 EEIFFEIVGItdISSKLNIP----------FMDLGIDSLCMENLRYSLNKNFDLELTVSEMFENATYQKLQTYVETLRK 5235
Cdd:COG0236     4 EELEERLAEI--IAEVLGVDpeeitpddsfFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
736-792 3.03e-04

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 42.17  E-value: 3.03e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054   736 STVRTIVKQFLDIEEDDI----NLLETGaVDSLTSIEMVEAFGTAVNQTMPFDLLEAYPTI 792
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIdpdtDLFDLG-LDSLLAVELIARLEEEFGVEIPPSDLFEHPTL 60
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
5168-5222 3.76e-04

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 42.17  E-value: 3.76e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392926054  5168 EIFFEIVGITDISSKLNIPFMDLGIDSLCMENLRYSLNKNFDLELTVSEMFENAT 5222
Cdd:pfam00550    5 ELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
7527-7622 4.30e-04

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 45.84  E-value: 4.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7527 IYLVHAIGGTIYPYYSFLQIFPKDISLYGIEfdlkYPS--------NDLRELAHFYAEEIAAHAGNKRIFVMGHSMGGIM 7598
Cdd:pfam00975    3 LFCFPPAGGSASSFRSLARRLPPPAEVLAVQ----YPGrgrgepplNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78
                           90       100
                   ....*....|....*....|....
gi 392926054  7599 SREIVAELKIWGYDIPFVMLFDSW 7622
Cdd:pfam00975   79 AFEVARRLERQGEAVRSLFLSDAS 102
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
6475-6539 9.54e-04

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 41.85  E-value: 9.54e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054   6475 VIAEIWKETLGISILNDANPN--FFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEFTKFV 6539
Cdd:smart00823   16 LVREQVAAVLGHAAAEAIDPDrpFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
5186-5230 4.22e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 39.93  E-value: 4.22e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 392926054   5186 PFMDLGIDSL-CMEnLRYSLNKNFDLELTVSEMFENATYQKLQTYV 5230
Cdd:smart00823   38 PFRDLGLDSLmAVE-LRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1806-1848 8.24e-03

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 38.31  E-value: 8.24e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 392926054  1806 DIDNTTGFFDLGLTSIQAVKLRNAIKSNYP-NASSTCVFDYPSI 1848
Cdd:pfam00550   17 EIDPDTDLFDLGLDSLLAVELIARLEEEFGvEIPPSDLFEHPTL 60
 
Name Accession Description Interval E-value
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
6987-7412 4.74e-160

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 504.70  E-value: 4.74e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6987 FTEPALLL----STNTVSYSDLAEKIENISKDIQKQLQIakatsvrEDELVGLDC---KNSYFALLACVFLGLPYAPIDP 7059
Cdd:cd17654     1 PDRPALIIdqttSDTTVSYADLAEKISNLSNFLRKKFQT-------EERAIGLRCdrgTESPVAILAILFLGAAYAPIDP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7060 TWPEPRQLFVKSK--VSFTLENCFSCNLKL------RNFNSRTQFGSIYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQ 7131
Cdd:cd17654    74 ASPEQRSLTVMKKchVSYLLQNKELDNAPLsftpehRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7132 CM-FRSNIRVLDSVKqVFDVSVSNIIGSVLNGGVLISSEHS--------TTITDQLQKCQYAFLPAAVFNGFTDK----- 7197
Cdd:cd17654   154 FNiTSEDILFLTSPL-TFDPSVVEIFLSLSSGATLLIVPTSvkvlpsklADILFKRHRITVLQATPTLFRRFGSQsikst 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7198 TMSRLESIETLTIGGE-TVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKCKV--STLNIGSALGDsLSNETCTICN 7274
Cdd:cd17654   233 VLSATSSLRVLALGGEpFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEedSPVQLGSPLLG-TVIEVRDQNG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7275 NSVRGNVQVKGISlaRGYITSAPHGTPFSDIYSTGDIVDSKLNSLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQI 7354
Cdd:cd17654   312 SEGTGQVFLGGLN--RVCILDDEVTVPKGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESC 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7355 VVLYSN-QMLIAFIVDQ-KSKLLHDSLVKTLKNRTQIPDYFVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17654   390 AVTLSDqQRLIAFIVGEsSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
5256-6071 1.56e-153

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 519.04  E-value: 1.56e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5256 DDTRVAVIGWSAEFSGSSNIHEYWENLMDGICSTG--------NNKYL-----------------LKNPFGFDNKFFNLT 5310
Cdd:COG3321     2 ADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITevpadrwdADAYYdpdpdapgktyvrwggfLDDVDEFDALFFGIS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5311 DEDARVLDPQVRKFIQHAYLALENSGYVKQK-HELRCGVFAGAEPSDYGR--ADDHDDAMRKLFVMNMNSYLASYASYCL 5387
Cdd:COG3321    82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESlAGSRTGVFVGASSNDYALllLADPEAIDAYALTGNAKSVLAGRISYKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5388 DLKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGFDDQKktMFSKSGVCRPFDKDSEGIVRGS 5467
Cdd:COG3321   162 DLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGG--MLSPDGRCRAFDADADGYVRGE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5468 GVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRaSFMAPNPAGQLKCMTDVLARFtNKEKERISFVECHATGTTLGD 5547
Cdd:COG3321   240 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADA-GVDPATVDYVEAHGTGTPLGD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5548 TIEMNSLRTAY----SFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSE------FrDGMGqfFTVN 5617
Cdd:COG3321   318 PIEAAALTAAFgqgrPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETpnphidF-ENSP--FYVN 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5618 GKKSTISQNS---LISIDSFGIGGTNVHMVIE-FPARSQEVVKISSENLILydmiPISAKTEYSLDHTSEAISKYLQTDT 5693
Cdd:COG3321   395 TELRPWPAGGgprRAGVSSFGFGGTNAHVVLEeAPAAAPAAAAAARPPQLL----VLSAKTEEALRALAARLAAFLEAHP 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5694 NK-IAQCSSTFIHSRVPMDSRTYLSVNNNNELL---------KIRTNKKTWFNGKSPKIALFFAPQGIQFTNILPNEYLK 5763
Cdd:COG3321   471 DLdLADVAYTLATGRAHFEHRLAVVASSREELAaklralaagEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYET 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5764 NSAYRREVEYLCELASSFGIPSLEGILYPTKNfDHLIHATQFAQIAIFVQCMAIFKAIKNV-FNPTCLIGHSVGEYAAAV 5842
Cdd:COG3321   551 EPVFRAALDECDALLRPHLGWSLREVLFPDEE-ESRLDRTEVAQPALFAVEYALARLWRSWgVRPDAVIGHSVGEYAAAC 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5843 ISGALKTEEALKLLIKRSELIGKTEKA-RMLMVWNYEKQ----LPSHVHVS-AIIDANTKCVV-GPVETIDNLEKYFINN 5915
Cdd:COG3321   630 VAGVLSLEDALRLVAARGRLMQALPGGgAMLAVGLSEEEvealLAGYDGVSiAAVNGPRSTVVsGPAEAVEALAARLEAR 709
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5916 HIKYRNIETKHGFHSKMFHCISKEFEFFCESFATKVPLIPMISSITGSEIK--IFDSKYCTMHLTNPVNLELVVDHIMKL 5993
Cdd:COG3321   710 GIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTgeALDADYWVRHLRQPVRFADAVEALLAD 789
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5994 DIDIIVEVGPTGVLSNLL---AKRNSKIVVVPTCGTKKHPKISLGECIGQLWSNGVDI--RKLTPKLA---VDgqVPGYC 6065
Cdd:COG3321   790 GVRVFLEVGPGPVLTGLVrqcLAAAGDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVdwSALYPGRGrrrVP--LPTYP 867

                  ....*.
gi 392926054 6066 FdERQF 6071
Cdd:COG3321   868 F-QRED 872
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
5258-5645 5.51e-123

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 396.93  E-value: 5.51e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5258 TRVAVIGWSAEFSGSSNIHEYWENLMDGICSTG------------------------NNKYLLKNPFGFDNKFFNLTDED 5313
Cdd:cd00833     1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISeipedrwdadgyypdpgkpgktytRRGGFLDDVDAFDAAFFGISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5314 ARVLDPQVRKFIQHAYLALENSGYV-KQKHELRCGVFAGAEPSDYGRA-DDHDDAMRKLFVM-NMNSYLASYASYCLDLK 5390
Cdd:cd00833    81 AEAMDPQQRLLLEVAWEALEDAGYSpESLAGSRTGVFVGASSSDYLELlARDPDEIDAYAATgTSRAFLANRISYFFDLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5391 GEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGFDDQKktMFSKSGVCRPFDKDSEGIVRGSGVG 5470
Cdd:cd00833   161 GPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAG--MLSPDGRCRPFDADADGYVRGEGVG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5471 CFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRASFmAPNPAGQLKCMTDVLARfTNKEKERISFVECHATGTTLGDTIE 5550
Cdd:cd00833   239 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGIT-APSGEAQAALIRRAYAR-AGVDPSDIDYVEAHGTGTPLGDPIE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5551 MNSLRTAY----SFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSEFR---DGMGQFFTVNGKKSTI 5623
Cdd:cd00833   317 VEALAKVFggsrSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNpkiDFEESPLRVPTEARPW 396
                         410       420
                  ....*....|....*....|....*
gi 392926054 5624 SQNS---LISIDSFGIGGTNVHMVI 5645
Cdd:cd00833   397 PAPAgprRAGVSSFGFGGTNAHVIL 421
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
1889-2282 5.41e-122

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 394.23  E-value: 5.41e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1889 NPIGVMAAACRLPGGVSsPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYG-NPVEGGNFItQDVTQFDPSFFKISK 1967
Cdd:cd00833     1 EPIAIVGMACRFPGAAD-PDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGkTYTRRGGFL-DDVDAFDAAFFGISP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1968 SEAELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYQDMMESSSIL----AMLGSMAAVIAGRVNYIFG 2039
Cdd:cd00833    79 REAEAMDPQQRLLLEVAWEALEDAGYspesLAGSRTGVFVGASSSDYLELLARDPDEidayAATGTSRAFLANRISYFFD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2040 CYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDGCV 2119
Cdd:cd00833   159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2120 VLMLelaKP-------NFHYMSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS---PSlAIDYWEAHGTGTPLGDP 2189
Cdd:cd00833   239 VVVL---KRlsdalrdGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAgvdPS-DIDYVEAHGTGTPLGDP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2190 IEFNTLSSIL-------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDINAGSIRLPIIGEDS 2262
Cdd:cd00833   315 IEVEALAKVFggsrsadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEAR 394
                         410       420
                  ....*....|....*....|....*.
gi 392926054 2263 ELVS------AGISSFGVSGTNAAAI 2282
Cdd:cd00833   395 PWPApagprrAGVSSFGFGGTNAHVI 420
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1887-2354 1.02e-111

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 393.47  E-value: 1.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1887 AENPIGVMAAACRLPGgVSSPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNPV---EGGnFItQDVTQFDPSFF 1963
Cdd:COG3321     2 ADEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTyvrWGG-FL-DDVDEFDALFF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1964 KISKSEAELIDPQQRLLLECVQECLENSGVIET----SNVGVFVGLMEKEYQDMM----ESSSILAMLGSMAAVIAGRVN 2035
Cdd:COG3321    79 GISPREAEAMDPQQRLLLEVAWEALEDAGYDPEslagSRTGVFVGASSNDYALLLladpEAIDAYALTGNAKSVLAGRIS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2036 YIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRS 2115
Cdd:COG3321   159 YKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2116 DGCVVLMLE------------LAkpnfhymsTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQ---SPSlAIDYWEAH 2180
Cdd:COG3321   239 EGVGVVVLKrlsdalrdgdriYA--------VIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADagvDPA-TVDYVEAH 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2181 GTGTPLGDPIEFNTLSSIL-------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDIN--AG 2251
Cdd:COG3321   310 GTGTPLGDPIEAAALTAAFgqgrpadQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDfeNS 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2252 SIRLPiigedSELVS---------AGISSFGVSGTNAAAIafndnnkLE--------PYIPIHKYYILPISAKNQISLDN 2314
Cdd:COG3321   390 PFYVN-----TELRPwpagggprrAGVSSFGFGGTNAHVV-------LEeapaaapaAAAAARPPQLLVLSAKTEEALRA 457
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 392926054 2315 LEKQILSVI------PLTDVpicniASALANNRSHFTIRNALIVSN 2354
Cdd:COG3321   458 LAARLAAFLeahpdlDLADV-----AYTLATGRAHFEHRLAVVASS 498
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
13-394 9.44e-106

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 347.24  E-value: 9.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   13 PNGEDGHEMAENIFLNRNNIALLPVEKNYLSDFREKHPE------VKAALVDGIEYFDDQYFGTGESEAICMDPQQRMLM 86
Cdd:cd00833    13 PGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytRRGGFLDDVDAFDAAFFGISPREAEAMDPQQRLLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   87 QGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLL-----PPDQYMATGNSASVMCGRITYFLNSRGAAVGIETACSS 161
Cdd:cd00833    93 EVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLardpdEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSS 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  162 SLVAFHLARQAIQSGETKLALVCGANHVGS-RSFHSLYNSHMVSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENN 240
Cdd:cd00833   173 SLVALHLACQSLRSGECDLALVGGVNLILSpDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  241 LLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSDIRVMS 318
Cdd:cd00833   253 DRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARagVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQ 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  319 P------KSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEME-------LNRVAISSYGF 385
Cdd:cd00833   333 PlligsvKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARpwpapagPRRAGVSSFGF 412

                  ....*....
gi 392926054  386 GGTNACAII 394
Cdd:cd00833   413 GGTNAHVIL 421
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
54-600 3.68e-102

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 364.19  E-value: 3.68e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   54 AALVDGIEYFDDQYFGTGESEAICMDPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLLPP-----DQY 128
Cdd:COG3321    64 GGFLDDVDEFDALFFGISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLAdpeaiDAY 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  129 MATGNSASVMCGRITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNG 207
Cdd:COG3321   144 ALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNlMLTPESFILFSKGGMLSPDG 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  208 RLAAFDRSANGFVRAESFAVAVLcsKQF--AEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKD 283
Cdd:COG3321   224 RCRAFDADADGYVRGEGVGVVVL--KRLsdALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADagVDPA 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  284 SVQLVTCHGTGTKLGDQVELTAINRSFKSD------IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPS 357
Cdd:COG3321   302 TVDYVEAHGTGTPLGDPIEAAALTAAFGQGrpadqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPN 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  358 EDLGEDKSMGFVNEE-MELN------RVAISSYGFGGTNACAIIEKPEKPSLVQKESYAESNVLFLSAKSHESLKLQIEE 430
Cdd:COG3321   382 PHIDFENSPFYVNTElRPWPagggprRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAAR 461
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  431 YTQFMAQ-SDSAMEDILYTVNERKTKYDFRAAVFGKDNEEIARKL------QDGDYSLTNLQESTFEVEF---GEGNEKL 500
Cdd:COG3321   462 LAAFLEAhPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLralaagEAAPGVVTGAAAAAPKVAFlfpGQGSQYV 541
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  501 WLLRMLYEKNETFHSTVDKYCK-LAETCGFPeaRTALFFP----FKLTLT----PLTYNVsrlisSMATFELLVQYNTLP 571
Cdd:COG3321   542 GMGRELYETEPVFRAALDECDAlLRPHLGWS--LREVLFPdeeeSRLDRTevaqPALFAV-----EYALARLWRSWGVRP 614
                         570       580
                  ....*....|....*....|....*....
gi 392926054  572 NKLRGKGLGQIFCLAVAKVITFESAVQLI 600
Cdd:COG3321   615 DAVIGHSVGEYAAACVAGVLSLEDALRLV 643
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
4290-4628 2.55e-93

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 311.41  E-value: 2.55e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4290 ALLDSDARyWDPEYFGIRPSEAKFIDPQQRLLL-CSVAKLLDS-LLITSLT-SNTGVFIGCSANEFSHIVyAYGYKDPRA 4366
Cdd:cd00833    61 GFLDDVDA-FDAAFFGISPREAEAMDPQQRLLLeVAWEALEDAgYSPESLAgSRTGVFVGASSSDYLELL-ARDPDEIDA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4367 EWSGGTSNSALAGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKM-TVD 4445
Cdd:cd00833   139 YAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMlSPD 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4446 DFCKAFDVDANGYKRSEAVCSMLLTKSP----NIDSV-ATITNYATGHNGTSSSLFTPNGLSQLEVMQRATN----PLEK 4516
Cdd:cd00833   219 GRCRPFDADADGYVRGEGVGVVVLKRLSdalrDGDRIyAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYAragvDPSD 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4517 ILEIQTHCTGTKLGDPIEINAISKLVSSA------CKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLKCPTN 4590
Cdd:cd00833   299 IDYVEAHGTGTPLGDPIEVEALAKVFGGSrsadqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNP 378
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 392926054 4591 SIKTNKMICRFIGE-----DADENNSILINNFGFTGSNCSVVL 4628
Cdd:cd00833   379 KIDFEESPLRVPTEarpwpAPAGPRRAGVSSFGFGGTNAHVIL 421
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
1891-2282 1.47e-81

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 272.67  E-value: 1.47e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   1891 IGVmaaACRLPGgVSSPSELWELLKIGKNassripatrvptrntlisgskygnpveggnfitqDVTQFDPSFFKISKSEA 1970
Cdd:smart00825    4 VGM---SCRFPG-ADDPEEFWDLLLAGLD----------------------------------DVDLFDAAFFGISPREA 45
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   1971 ELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYqdmmesssilamlgsmaaviagrvnyifgcygpSVT 2046
Cdd:smart00825   46 EAMDPQQRLLLEVAWEALEDAGIdpesLRGSRTGVFVGVSSSDY---------------------------------SVT 92
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   2047 IDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILN-EKGQGLrTNGKMLSQHGMSLSFDSRASGYGRSDGCVVLMLE- 2124
Cdd:smart00825   93 VDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSpDTFVGL-SRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKr 171
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   2125 -----------LAkpnfhymsTIQSVNVNHGGRSVSLTAPNGVAHkmlltsvinqspslaidyweahgtgtplgdpiefn 2193
Cdd:smart00825  172 lsdalrdgdpiLA--------VIRGSAVNQDGRSNGITAPSGPAQ----------------------------------- 208
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   2194 tlssilqnIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDINAGSIRLPIIGEDSELVS------A 2267
Cdd:smart00825  209 --------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWPPpgrprrA 280
                           410
                    ....*....|....*
gi 392926054   2268 GISSFGVSGTNAAAI 2282
Cdd:smart00825  281 GVSSFGFGGTNAHVI 295
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
5260-5646 5.19e-81

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 271.12  E-value: 5.19e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5260 VAVIGWSAEFSGSSNIHEYWENLMDGicstgnnkylLKNPFGFDNKFFNLTDEDARVLDPQVRKFIQHAYLALENSGYVK 5339
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG----------LDDVDLFDAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDP 70
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5340 QK-HELRCGVFAGAEPSDYgraddhddamrklfvmnmnsylasyasycldlkgeAVSVYSACSTALVAVANAVKSIQSGS 5418
Cdd:smart00825   71 ESlRGSRTGVFVGVSSSDY-----------------------------------SVTVDTACSSSLVALHLACQSLRSGE 115
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5419 MDYALVGAASIAEVSGALSGFDDQKktMFSKSGVCRPFDKDSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINN 5498
Cdd:smart00825  116 CDMALAGGVNLILSPDTFVGLSRAG--MLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQ 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5499 DGHSrASFMAPNPAGQlkcmtdvlarftnkekerisfvechatgttlgdtiemnslrtaysfknkLAIGSCKANIGHAYA 5578
Cdd:smart00825  194 DGRS-NGITAPSGPAQ-------------------------------------------------LLIGSVKSNIGHLEA 223
                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054   5579 ASGLAALVKCAKMLQTGIIPPQVNFSE------FRDGMgqfFTVNGKKSTISQNS---LISIDSFGIGGTNVHMVIE 5646
Cdd:smart00825  224 AAGVAGLIKVVLALKHGVIPPTLHFETpnphidLEESP---LRVPTELTPWPPPGrprRAGVSSFGFGGTNAHVILE 297
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
3649-3927 1.06e-78

Acyl transferase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 264.26  E-value: 1.06e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3649 MLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLqgDVSLWEILFNTDHYKLLQLTKHMQPIMFCFGYATAQLWLS 3728
Cdd:smart00827    1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLL--GWSLLDVLLGEDGAASLLDTEVAQPALFAVQVALARLLRS 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3729 LGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIAGLGALLAVQREiADEVL-----RKFKVSVATINSP 3803
Cdd:smart00827   79 WGVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLS-EEEVEpllagVPDRVSVAAVNSP 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3804 KQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQEThLVSLRQCLADIKFSAGRTPLVSNVTGQIINT---FS 3880
Cdd:smart00827  158 SSVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPI-LDEFRAALAGLTPRPPRIPFVSTVTGTLIDGaelDD 236
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 392926054   3881 EAYIVKHTVSAVKFVDCVETLQA-KGVTVWIDAGSAAVLATFVKRIIQ 3927
Cdd:smart00827  237 ADYWVRNLREPVRFADAVRALLAeGGVTVFLEVGPHPVLTGPIKQTLA 284
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3617-3971 1.96e-76

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 284.07  E-value: 1.96e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3617 VVGKSIRDVVSKIKEAAPQQIKLC------QESSKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLqgDV 3690
Cdd:COG3321   494 VVASSREELAAKLRALAAGEAAPGvvtgaaAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALDECDALLRPHL--GW 571
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3691 SLWEILFNTDHYKLLQLTKHMQPIMFCFGYATAQLWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAME 3770
Cdd:COG3321   572 SLREVLFPDEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLEDALRLVAARGRLMQ 651
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3771 NIAGLGALLAVQ--REIADEVLRKF-KVSVATINSPKQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQETh 3847
Cdd:COG3321   652 ALPGGGAMLAVGlsEEEVEALLAGYdGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARRLPVSHAFHSPLMEPA- 730
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3848 LVSLRQCLADIKFSAGRTPLVSNVTGQIINT--FSEAYIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:COG3321   731 LEEFRAALAGVTPRAPRIPLISNVTGTWLTGeaLDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQC 810
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 392926054 3926 IQPTElsKHRIVQTCKEKESDVDNLVQACLELEQSGLPISWTTLYG 3971
Cdd:COG3321   811 LAAAG--DAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYP 854
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
1889-2124 2.60e-75

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 252.94  E-value: 2.60e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1889 NPIGVMAAACRLPGGVSsPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNPVEGGNFITQDVTQFDPSFFKISKS 1968
Cdd:pfam00109    1 EPVAIVGMGCRFPGGND-PEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKWGGLDDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1969 EAELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYQDMMESSSI-------LAMLGSMAAVIAGRVNYI 2037
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGItpdsLDGSRTGVFIGSGIGDYAALLLLDEDggprrgsPFAVGTMPSVIAGRISYF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2038 FGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDG 2117
Cdd:pfam00109  160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239

                   ....*..
gi 392926054  2118 CVVLMLE 2124
Cdd:pfam00109  240 VGAVVLK 246
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
57-395 3.43e-72

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 245.70  E-value: 3.43e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054     57 VDGIEYFDDQYFGTGESEAICMDPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYkdllppdqymatgnsas 136
Cdd:smart00825   27 LDDVDLFDAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY----------------- 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    137 vmcgrityflnsrgaAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNGRLAAFDRS 215
Cdd:smart00825   90 ---------------SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLSPDGRCKTFDAS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    216 ANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQyevqlealknidkdsvqlvtchgtgt 295
Cdd:smart00825  155 ADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ-------------------------- 208
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    296 klgdqveltainrsfksdIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEME- 374
Cdd:smart00825  209 ------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTp 270
                           330       340
                    ....*....|....*....|....*..
gi 392926054    375 ------LNRVAISSYGFGGTNACAIIE 395
Cdd:smart00825  271 wpppgrPRRAGVSSFGFGGTNAHVILE 297
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
4290-4695 3.98e-71

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 267.12  E-value: 3.98e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4290 ALLDsDARYWDPEYFGIRPSEAKFIDPQQRLLL-CSVAKLLDS-LLITSLT-SNTGVFIGCSANEFSHIVYAYGykDPRA 4366
Cdd:COG3321    65 GFLD-DVDEFDALFFGISPREAEAMDPQQRLLLeVAWEALEDAgYDPESLAgSRTGVFVGASSNDYALLLLADP--EAID 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4367 EWSG-GTSNSALAGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKM-TV 4444
Cdd:COG3321   142 AYALtGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMlSP 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4445 DDFCKAFDVDANGYKRSEAvCSMLLTKsP------NIDSV-ATITNYATGHNGTSSSLFTPNGLSQLEVMQRAtnpleki 4517
Cdd:COG3321   222 DGRCRAFDADADGYVRGEG-VGVVVLK-RlsdalrDGDRIyAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRA------- 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4518 LE-----------IQTHCTGTKLGDPIEINAISKLVSSA------CKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRV 4580
Cdd:COG3321   293 LAdagvdpatvdyVEAHGTGTPLGDPIEAAALTAAFGQGrpadqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLP 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4581 AQLHLKCPTNSIktnkmicrfigedaDENNSIL-------------------INNFGFTGSNCSVVLK-PKNAISEHFVS 4640
Cdd:COG3321   373 PTLHFETPNPHI--------------DFENSPFyvntelrpwpagggprragVSSFGFGGTNAHVVLEeAPAAAPAAAAA 438
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054 4641 SEVFYPILLSSHSAKSLQKYVQVLCEFI-SNSAKSLHDIMMSLFQKKIH-VHRQFII 4695
Cdd:COG3321   439 ARPPQLLVLSAKTEEALRALAARLAAFLeAHPDLDLADVAYTLATGRAHfEHRLAVV 495
PRK12316 PRK12316
peptide synthase; Provisional
6457-7495 1.11e-65

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 251.80  E-value: 1.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6457 EVKAVESLKLPKSTSCEFVIAEIWKETLGISILNdANPNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEFT 6536
Cdd:PRK12316 2502 DVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVG-LDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFA 2580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6537 KFVKNLTTEKfAGNTNDKISYDAIPLTNSQTQMFMLRQIDTTSK-YNLifKITISYETKFVWEFLKYSLHSLIAYQPSYR 6615
Cdd:PRK12316 2581 ASLESGQTSR-APVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAaYHL--PSALHLRGVLDQAALEQAFDALVLRHETLR 2657
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6616 TVFKSGNSPYQYICSLTESFHDFDKRC------NLNNAISHEPNHLFEIGKSTPLRVRVAEDCDNSRIhIVFNQHHILTD 6689
Cdd:PRK12316 2658 TRFVEVGEQTRQVILPNMSLRIVLEDCagvadaAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHV-LVITQHHIVSD 2736
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6690 GWSMTVLSDTVSSLYAAYRG--ETSFPSKTKQTI--SQVAMGTKSSGDIKEALEYYQNTYHTIIPY------DSETGNTS 6759
Cdd:PRK12316 2737 GWSMQVMVDELVQAYAGARRgeQPTLPPLPLQYAdyAAWQRAWMDSGEGARQLDYWRERLGGEQPVlelpldRPRPALQS 2816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6760 PSYVRISKLIPSKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LIGYFMNNALFKTS 6838
Cdd:PRK12316 2817 HRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETErLIGFFVNTQVLRAQ 2896
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6839 LPFEiLRLEEILNIVLNSLEKSRSFATIPFYQMVEQ---NRKLNEISLFFNFRQKLDYPTVSMFGAKCEIEHLSLNNA-- 6913
Cdd:PRK12316 2897 VDAQ-LAFRDLLGQVKEQALGAQAHQDLPFEQLVEAlqpERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAat 2975
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6914 -FDFSFTIDETPTGSLITVDFDKSKYLDTTVHMFAniflKKLNNLRNMNTTIPIRRTD---------------------- 6970
Cdd:PRK12316 2976 qFDLALDTWESAEGLGASLTYATDLFDARTVERLA----RHWQNLLRGMVENPQRSVDelamldaeergqlleawnataa 3051
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6971 -FPSTLFQKGLFTSW--RLFTEPALLLSTNTVSYSDLAEKIENISKDIqkqlqiaKATSVREDELVGLDCKNSY---FAL 7044
Cdd:PRK12316 3052 eYPLERGVHRLFEEQveRTPDAVALAFGEQRLSYAELNRRANRLAHRL-------IERGVGPDVLVGVAVERSLemvVGL 3124
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7045 LACVFLGLPYAPIDPTWPEPRQLFV-------------------KSKVSFTLENCFSCNLKLRNFNSRTQFGSI-YSIFT 7104
Cdd:PRK12316 3125 LAILKAGGAYVPLDPEYPEERLAYMledsgaqlllsqshlrlplAQGVQVLDLDRGDENYAEANPAIRTMPENLaYVIYT 3204
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7105 SGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSE----HSTTITDQLQK 7180
Cdd:PRK12316 3205 SGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGpedwRDPALLVELIN 3284
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7181 CQYAFLPAAVFN----GFTDKTMSRLESIETLTIGGETVSDvviETAMKKFPRLRTIQIYGPTETCIWSLTNKCK---VS 7253
Cdd:PRK12316 3285 SEGVDVLHAYPSmlqaFLEEEDAHRCTSLKRIVCGGEALPA---DLQQQVFAGLPLYNLYGPTEATITVTHWQCVeegKD 3361
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7254 TLNIGSALGDS---LSNETCTICNNSVRGNVQVKGISLARGYItSAPHGT-------PFSD---IYSTGDIVDSKLNS-L 7319
Cdd:PRK12316 3362 AVPIGRPIANRacyILDGSLEPVPVGALGELYLGGEGLARGYH-NRPGLTaerfvpdPFVPgerLYRTGDLARYRADGvI 3440
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7320 QYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVLYSN-QMLIAFIV-DQKSKLLHDSLVKTLKNRtqIPDYFVQ-- 7395
Cdd:PRK12316 3441 EYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDgRQLVAYVVpEDEAGDLREALKAHLKAS--LPEYMVPah 3518
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7396 ---INKMPLNSSGKVD-KSLLLQAFENIRKSYkreiVVMKNSLEEKVINVFSKILG-RNVAPTDKFESIGGNSLNAIQIA 7470
Cdd:PRK12316 3519 llfLERMPLTPNGKLDrKALPRPDAALLQQDY----VAPVNELERRLAAIWADVLKlEQVGLTDNFFELGGDSIISLQVV 3594
                        1130      1140
                  ....*....|....*....|....*
gi 392926054 7471 HRlAEELKIEIKAHEILQSNSLKTF 7495
Cdd:PRK12316 3595 SR-ARQAGIRFTPKDLFQHQTIQGL 3618
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
6-236 5.34e-65

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 223.28  E-value: 5.34e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054     6 VGSWAKIPNGEDGHEMAENIFLNRNNIALLP-----VEKNYL--SDFREKHPEVKAALvDGIEYFDDQYFGTGESEAICM 78
Cdd:pfam00109    6 VGMGCRFPGGNDPEEFWENLLEGRDGISEIPadrwdPDKLYDppSRIAGKIYTKWGGL-DDIFDFDPLFFGISPREAERM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    79 DPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLL-------PPDQYM-ATGNSASVMCGRITYFLNSRG 150
Cdd:pfam00109   85 DPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLlldedggPRRGSPfAVGTMPSVIAGRISYFLGLRG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   151 AAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNGRLAAFDRSANGFVRAESFAVAV 229
Cdd:pfam00109  165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVV 244

                   ....*..
gi 392926054   230 LCSKQFA 236
Cdd:pfam00109  245 LKRLSDA 251
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
830-1197 1.30e-64

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 228.60  E-value: 1.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  830 IACdyQFAGVEGEKELWDTLLTSRLTTGKISDIRKKQCEGDAGLEV---------GLLKqDISMFDNSFFAIAKDEAEFL 900
Cdd:cd00833     8 MAC--RFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytrrgGFLD-DVDAFDAAFFGISPREAEAM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  901 DPQHRLLLNAAYNALEKSGLT--SIPDAD--LFLAISaHSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGIRGRA 976
Cdd:cd00833    85 DPQQRLLLEVAWEALEDAGYSpeSLAGSRtgVFVGAS-SSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  977 MIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL---KTLLDHHSTNSFSVDGSGFCRSDGVGVIILK 1052
Cdd:cd00833   164 LTVDTACSSSLVALHLACQSLRSGEcDLALVGGVNLILSPDMFVGFskaGMLSPDGRCRPFDADADGYVRGEGVGVVVLK 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1053 ---TAEK-GDS--AVIKiSSAKSH--HCGAVMTPVVSS----ISQLLEEAG----SFSYVEGHGTATSAGDSAE----SM 1112
Cdd:cd00833   244 rlsDALRdGDRiyAVIR-GSAVNQdgRTKGITAPSGEAqaalIRRAYARAGvdpsDIDYVEAHGTGTPLGDPIEvealAK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1113 AYQKLGSE---LIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVHNILPSEHIRNNE-NIRLPFVAEE----KQI 1184
Cdd:cd00833   323 VFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEEsPLRVPTEARPwpapAGP 402
                         410
                  ....*....|...
gi 392926054 1185 DRSAIVSFGITGT 1197
Cdd:cd00833   403 RRAGVSSFGFGGT 415
PRK12467 PRK12467
peptide synthase; Provisional
6470-7488 1.81e-64

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 247.77  E-value: 1.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6470 TSCEFVIAEIWKETLGISI--LNDanpNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQeftKFVKNLTTEKF 6547
Cdd:PRK12467 1029 TELEKRLAAIWADVLKVERvgLTD---NFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLA---GFAQAVAAQQQ 1102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6548 AGNTN-DKISYDA-IPLTNSQTQMFMLRQIDTTSK-YNLIFKITISYETKFvwEFLKYSLHSLIAYQPSYRTVF-KSGNS 6623
Cdd:PRK12467 1103 GAQPAlPDVDRDQpLPLSYAQERQWFLWQLEPGSAaYHIPQALRLKGPLDI--EALERSFDALVARHESLRTTFvQEDGR 1180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6624 PYQYI---CSLT----ESFHDFDKRCNLNNAISHEPNHLFEIGKSTPLRV---RVAEDcdnsrIHI-VFNQHHILTDGWS 6692
Cdd:PRK12467 1181 TRQVIhpvGSLTleepLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVgllRLAAD-----EHVlVLTLHHIVSDGWS 1255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6693 MTVLSDTVSSLYAAYRGETS--FPSKTKQTISQVAMGTK--SSGDIKEALEYYQNTY---HTII--PYD-SETGNTSPSY 6762
Cdd:PRK12467 1256 MQVLVDELVALYAAYSQGQSlqLPALPIQYADYAVWQRQwmDAGERARQLAYWKAQLggeQPVLelPTDrPRPAVQSHRG 1335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6763 VRISKLIPSKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LIGYFMNNALFKTSLPF 6841
Cdd:PRK12467 1336 ARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEgLIGFFVNTQVLRAEVDG 1415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6842 EiLRLEEILNIVLNSLEKSRSFATIPFYQMVEQ---NRKLNEISLF---FNFRQKLDYPTVSMFGakCEIEHLSLNN--- 6912
Cdd:PRK12467 1416 Q-ASFQQLLQQVKQAALEAQAHQDLPFEQLVEAlqpERSLSHSPLFqvmFNHQRDDHQAQAQLPG--LSVESLSWESqta 1492
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6913 AFDFSFTIDETPTGSLITVDFDKSKYLDTTVHMFANIFLKKLN--------NLRNMNTTIPIRR-----------TDFPS 6973
Cdd:PRK12467 1493 QFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQglvadperRLGELDLLDEAERrqilegwnathTGYPL 1572
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6974 TLFQKGLFTSW--RLFTEPALLLSTNTVSYSDLAEKIENISKDIqkqlqIAKAtsVREDELVGLDCKNSY---FALLACV 7048
Cdd:PRK12467 1573 ARLVHQLIEDQaaATPEAVALVFGEQELTYGELNRRANRLAHRL-----IALG--VGPEVLVGIAVERSLemvVGLLAIL 1645
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7049 FLGLPYAPIDPTWPEPRQLFV--KSKVSFTLENCFSCNL-----KLR-----------------NFNSRTQFGSI-YSIF 7103
Cdd:PRK12467 1646 KAGGAYVPLDPEYPRERLAYMieDSGIELLLTQSHLQARlplpdGLRslvldqeddwlegysdsNPAVNLAPQNLaYVIY 1725
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7104 TSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEHST---------TI 7174
Cdd:PRK12467 1726 TSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAhrdpeqliqLI 1805
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7175 TDQlQKCQYAFLPAAvFNGF--TDKTMSRLESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKCKV 7252
Cdd:PRK12467 1806 ERQ-QVTTLHFVPSM-LQQLlqMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRR 1883
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7253 STL--NIGSALGDSLSNETCTICNNS-------VRGNVQVKGISLARGYI----TSA------PHGTPFSDIYSTGDIVD 7313
Cdd:PRK12467 1884 KDLegRDSVPIGQPIANLSTYILDASlnpvpigVAGELYLGGVGLARGYLnrpaLTAerfvadPFGTVGSRLYRTGDLAR 1963
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7314 SKLNS-LQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL----YSNQMLIAFIVDQKSKLLHD-----SLVKTL 7383
Cdd:PRK12467 1964 YRADGvIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIaqdgANGKQLVAYVVPTDPGLVDDdeaqvALRAIL 2043
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7384 KN--RTQIPDY-----FVQINKMPLNSSGKVDKSLL--LQAFEnIRKSYkreiVVMKNSLEEKVINVFSKILG-RNVAPT 7453
Cdd:PRK12467 2044 KNhlKASLPEYmvpahLVFLARMPLTPNGKLDRKALpaPDASE-LQQAY----VAPQSELEQRLAAIWQDVLGlEQVGLH 2118
                        1130      1140      1150
                  ....*....|....*....|....*....|....*
gi 392926054 7454 DKFESIGGNSLNAIQIAHRlAEELKIEIKAHEILQ 7488
Cdd:PRK12467 2119 DNFFELGGDSIISIQVVSR-ARQAGIRFTPKDLFQ 2152
PRK12467 PRK12467
peptide synthase; Provisional
6557-7511 5.71e-63

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 242.76  E-value: 5.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6557 YDAIPLTNSQTQMFMLRQIDTTS-KYNLIFKITISYETKFvwEFLKYSLHSLIAYQPSYRTVFKS-GNSPYQYI---CSL 6631
Cdd:PRK12467   47 FERIPLSYAQERQWFLWQLDPDSaAYNIPTALRLRGELDV--SALRRAFDALVARHESLRTRFVQdEEGFRQVIdasLSL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6632 TESFHDFD------KRCNLNNAISHEPNHLFEIGKSTPLRVRVAEDCDNSRIhIVFNQHHILTDGWSMTVLSDTVSSLYA 6705
Cdd:PRK12467  125 TIPLDDLAneqgraRESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHV-LVVTLHHIISDGWSMRVLVEELVQLYS 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6706 AYRG--ETSFPSKTKQtISQVAMGTKS---SGDIKEALEYYQN---TYHTII--PYDSETgNTSPSY--VRISKLIPSKI 6773
Cdd:PRK12467  204 AYSQgrEPSLPALPIQ-YADYAIWQRSwleAGERERQLAYWQEqlgGEHTVLelPTDRPR-PAVPSYrgARLRVDLPQAL 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6774 WQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LIGYFMNNALFKTSLPfEILRLEEILNI 6852
Cdd:PRK12467  282 SAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETErLIGFFVNTQVLKAEVD-PQASFLELLQQ 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6853 VLNSLEKSRSFATIPFYQMVEQ---NRKLNEISLF---FNFRqkldyPTVSMFGAK-------CEIEHLSL---NNAFDF 6916
Cdd:PRK12467  361 VKRTALGAQAHQDLPFEQLVEAlqpERSLSHSPLFqvmFNHQ-----NTATGGRDRegaqlpgLTVEELSWarhTAQFDL 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6917 SFTIDETPTGSLITVDFDKSKYLDTTVHMFANIFLKKLNNL----RNMNTTIP----------IRRTDFPSTLFQKGlfT 6982
Cdd:PRK12467  436 ALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIvaepRRRLGELPlldaeerareLVRWNAPATEYAPD--C 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6983 SWRLFTE--------PALLLSTNTVSYSDLAEKIENISKDIQkqlqiakATSVREDELVGLDCKNSY---FALLACVFLG 7051
Cdd:PRK12467  514 VHQLIEAqarqhperPALVFGEQVLSYAELNRQANRLAHVLI-------AAGVGPDVLVGIAVERSIemvVGLLAVLKAG 586
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7052 LPYAPIDPTWPEPRQ-----------LFVKSKVSFTLENCFSCNLKLRNFNSRTQFGS--------------IYSIFTSG 7106
Cdd:PRK12467  587 GAYVPLDPEYPQDRLaymlddsgvrlLLTQSHLLAQLPVPAGLRSLCLDEPADLLCGYsghnpevaldpdnlAYVIYTSG 666
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7107 STGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGG-VLISSEHSTTITDQL------Q 7179
Cdd:PRK12467  667 STGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGAtLHLLPPDCARDAEAFaalmadQ 746
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7180 KCQYAFLPAAVFNGFTDKTMSRL-ESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKCKVSTLNIG 7258
Cdd:PRK12467  747 GVTVLKIVPSHLQALLQASRVALpRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFG 826
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7259 -SALGDSLSNETCTICNNS-------VRGNVQVKGISLARGYITSA----------PHGTPFSDIYSTGDIVDSKLNS-L 7319
Cdd:PRK12467  827 nVPIGQPLANLGLYILDHYlnpvpvgVVGELYIGGAGLARGYHRRPaltaerfvpdPFGADGGRLYRTGDLARYRADGvI 906
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7320 QYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL----YSNQMLIAFIV------DQKSKLLHDSLVKTLknRTQI 7389
Cdd:PRK12467  907 EYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLaqpgDAGLQLVAYLVpaavadGAEHQATRDELKAQL--RQVL 984
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7390 PDY-----FVQINKMPLNSSGKVDKSLLLQAFEN-IRKSYkreiVVMKNSLEEKVINVFSKILG-RNVAPTDKFESIGGN 7462
Cdd:PRK12467  985 PDYmvpahLLLLDSLPLTPNGKLDRKALPKPDASaVQATF----VAPQTELEKRLAAIWADVLKvERVGLTDNFFELGGH 1060
                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392926054 7463 SLNAIQIAHRLAEELKIEIKAHEILQSNSLKTFCNTL---KNSVQKPISKVP 7511
Cdd:PRK12467 1061 SLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVaaqQQGAQPALPDVD 1112
FabD COG0331
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...
3644-3925 1.73e-61

Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440100 [Multi-domain]  Cd Length: 306  Bit Score: 215.38  E-value: 1.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3644 SKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQsclkKCDEYLqgDVSLWEILFNTDhYKLLQLTKHMQPIMFCFGYATA 3723
Cdd:COG0331     1 MKLAFLFPGQGSQYVGMGKDLYENFPVAREVFE----EASEAL--GYDLSALCFEGP-EEELNLTENTQPAILAASVAAY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3724 QLWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIA--GLGALLAVQ-------REIADEVLRKFK 3794
Cdd:COG0331    74 RALEEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVpaGPGGMAAVLglddeevEALCAEAAQGEV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3795 VSVATINSPKQVVFAGTKSVLDAALAFVKGQG-KQATYVNQQYPFHSNLIQEThLVSLRQCLADIKFSAGRTPLVSNVTG 3873
Cdd:COG0331   154 VEIANYNSPGQIVISGEKEAVEAAAELAKEAGaKRAVPLPVSGPFHTPLMAPA-AEKLAEALAAVTFADPKIPVVSNVDA 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392926054 3874 QIINTFSE--AYIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:COG0331   233 APVTDPEEirELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRI 286
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
830-1287 5.93e-61

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 234.38  E-value: 5.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  830 IACdyQFAGVEGEKELWDTLLTSRLTTGKISDIR---KKQCEGDAGLEV-------GLLKqDISMFDNSFFAIAKDEAEF 899
Cdd:COG3321    11 MAC--RFPGADDPEEFWRNLRAGRDAITEVPADRwdaDAYYDPDPDAPGktyvrwgGFLD-DVDEFDALFFGISPREAEA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  900 LDPQHRLLLNAAYNALEKSGltsIPDADL-------FLAISaHSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGI 972
Cdd:COG3321    88 MDPQQRLLLEVAWEALEDAG---YDPESLagsrtgvFVGAS-SNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  973 RGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL-KT-LL--DHHStNSFSVDGSGFCRSDGVG 1047
Cdd:COG3321   164 RGPSVTVDTACSSSLVAVHLACQSLRSGEcDLALAGGVNLMLTPESFILFsKGgMLspDGRC-RAFDADADGYVRGEGVG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1048 VIILKTAEK----GDS--AVIKiSSAKSH--HCGAVMTPVVSS----ISQLLEEAG----SFSYVEGHGTATSAGDSAE- 1110
Cdd:COG3321   243 VVVLKRLSDalrdGDRiyAVIR-GSAVNQdgRSNGLTAPNGPAqaavIRRALADAGvdpaTVDYVEAHGTGTPLGDPIEa 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1111 ---SMAYQKLGSE---LIMSSVKAQFGHCEVASGLIQLMKVS-SIgKHGIIPsivhnilPSEHIRN-NENI---RLPF-V 1178
Cdd:COG3321   322 aalTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVlAL-RHGVLP-------PTLHFETpNPHIdfeNSPFyV 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1179 AEE----KQID---RSAIVSFGITGTKT-VVTTE--RVSQLNVDNIQNCYLLPVSAKTKDGLKKACLSLIEMIDNSCE-S 1247
Cdd:COG3321   394 NTElrpwPAGGgprRAGVSSFGFGGTNAhVVLEEapAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDlD 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 392926054 1248 LYDISTTLQKQKTNFKWRTAVVGSSHADVVLKLKQFLTSE 1287
Cdd:COG3321   474 LADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGE 513
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4242-4472 2.57e-60

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 209.80  E-value: 2.57e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4242 SEIEIVGFDISLPYNQisENSENWQHLKTN-----TVKQKLHNRSLKQDHARVALLDSDARY--------WDPEYFGIRP 4308
Cdd:pfam00109    1 EPVAIVGMGCRFPGGN--DPEEFWENLLEGrdgisEIPADRWDPDKLYDPPSRIAGKIYTKWgglddifdFDPLFFGISP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4309 SEAKFIDPQQRLLLCSVAKLLDSLLITSLT---SNTGVFIGCSANEFSHIVYAYGYKDPRAEWSG--GTSNSALAGRIAH 4383
Cdd:pfam00109   79 REAERMDPQQRLLLEAAWEALEDAGITPDSldgSRTGVFIGSGIGDYAALLLLDEDGGPRRGSPFavGTMPSVIAGRISY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4384 WLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKM-TVDDFCKAFDVDANGYKRSE 4462
Cdd:pfam00109  159 FLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMlSPDGPCKAFDPFADGFVRGE 238
                          250
                   ....*....|
gi 392926054  4463 AvCSMLLTKS 4472
Cdd:pfam00109  239 G-VGAVVLKR 247
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
4295-4628 1.52e-57

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 203.71  E-value: 1.52e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   4295 DARYWDPEYFGIRPSEAKFIDPQQRLLLCSVAKLLDSLLITSLT---SNTGVFIGCSANEFShivyaygykdpraewsgg 4371
Cdd:smart00825   29 DVDLFDAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDPESlrgSRTGVFVGVSSSDYS------------------ 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   4372 tsnsalagriahwlklkgpvVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKM-TVDDFCKA 4450
Cdd:smart00825   91 --------------------VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMlSPDGRCKT 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   4451 FDVDANGYKRSEAVCSMLLTKSP----NIDSV-ATITNYATGHNGTSSSLFTPNGLSQlevmqratnplekileiqthct 4525
Cdd:smart00825  151 FDASADGYVRGEGVGVVVLKRLSdalrDGDPIlAVIRGSAVNQDGRSNGITAPSGPAQ---------------------- 208
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   4526 gtklgdpieinaisklvssaCKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLKCPTNSIKTNKMICRFIGE- 4604
Cdd:smart00825  209 --------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTEl 268
                           330       340
                    ....*....|....*....|....*...
gi 392926054   4605 ----DADENNSILINNFGFTGSNCSVVL 4628
Cdd:smart00825  269 tpwpPPGRPRRAGVSSFGFGGTNAHVIL 296
PRK12316 PRK12316
peptide synthase; Provisional
6558-7511 5.01e-55

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 216.36  E-value: 5.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6558 DAIPLTNSQTQMFMLRQIDTTS-KYNLIFKITISYETKFvwEFLKYSLHSLIAYQPSYRTVFKSG-NSPYQYI---CSLT 6632
Cdd:PRK12316   48 ERDRLSYAQQRMWFLWQLEPQSgAYNLPSAVRLNGPLDR--QALERAFASLVQRHETLRTVFPRGaDDSLAQVpldRPLE 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6633 ESFHDF------DKRCNLNNAISHEPNHLFEIGKSTPLRVRVAEdCDNSRIHIVFNQHHILTDGWSMTVLSDTVSSLYAA 6706
Cdd:PRK12316  126 VEFEDCsglpeaEQEARLRDEAQRESLQPFDLCEGPLLRVRLLR-LGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSA 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6707 YRGETS--FPSKTKQtISQVAMGTKS---SGDIKEALEYYQNTY---HTII--PYDSETgNTSPSY--VRISKLIPSKIW 6774
Cdd:PRK12316  205 YATGAEpgLPALPIQ-YADYALWQRSwleAGEQERQLEYWRAQLgeeHPVLelPTDHPR-PAVPSYrgSRYEFSIDPALA 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6775 QKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LIGYFMNNALFKTSLPFEIlRLEEILNIV 6853
Cdd:PRK12316  283 EALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEgLIGFFVNTQVLRSVFDGRT-RVATLLAGV 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6854 LNSLEKSRSFATIPFYQMVEQ---NRKLNEISLF---FNFRqkldyPTVSMFGAKCEIEHLSL--------NNAFDFSFT 6919
Cdd:PRK12316  362 KDTVLGAQAHQDLPFERLVEAlkvERSLSHSPLFqvmYNHQ-----PLVADIEALDTVAGLEFgqlewksrTTQFDLTLD 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6920 IDETPTGSLITVDFDKSKYLDTTVHMFANIFLkklNNLRNMNTTIPIRRTDFP--STLFQKGLFTSW------------- 6984
Cdd:PRK12316  437 TYEKGGRLHAALTYATDLFEARTVERMARHWQ---NLLRGMVENPQARVDELPmlDAEERGQLVEGWnataaeyplqrgv 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6985 -RLFTE--------PALLLSTNTVSYSDLAEKIENISKDIQKQlqiakatSVREDELVGLDCKNS---YFALLACVFLGL 7052
Cdd:PRK12316  514 hRLFEEqvertpeaPALAFGEETLDYAELNRRANRLAHALIER-------GVGPDVLVGVAMERSiemVVALLAILKAGG 586
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7053 PYAPIDPTWPEPRQLFV--KSKVSFTLENCF-----------------SCNLKLRNFNSRTQFGSI------YSIFTSGS 7107
Cdd:PRK12316  587 AYVPLDPEYPAERLAYMleDSGVQLLLSQSHlgrklplaagvqvldldRPAAWLEGYSEENPGTELnpenlaYVIYTSGS 666
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7108 TGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLI---SSEH-------STTITDQ 7177
Cdd:PRK12316  667 TGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVvaaPGDHrdpaklvELINREG 746
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7178 LQKCQyaFLPAAVFNGFTDKTMSRLESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIwSLTNKCKVSTLNI 7257
Cdd:PRK12316  747 VDTLH--FVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAI-DVTHWTCVEEGGD 823
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7258 GSALGDSLSNETCTI-------CNNSVRGNVQVKGISLARGYitsapHG-----------TPFSD---IYSTGDIVDSKL 7316
Cdd:PRK12316  824 SVPIGRPIANLACYIldanlepVPVGVLGELYLAGRGLARGY-----HGrpgltaerfvpSPFVAgerMYRTGDLARYRA 898
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7317 NS-LQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL-YSNQMLIAFIVDQKSKllhDSLVKTLKN--RTQIPDY 7392
Cdd:PRK12316  899 DGvIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLaVDGKQLVGYVVLESEG---GDWREALKAhlAASLPEY 975
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7393 FVQ-----INKMPLNSSGKVDKSLLLQAFENIRksyKREIVVMKNSLEEKVINVFSKILG-RNVAPTDKFESIGGNSLNA 7466
Cdd:PRK12316  976 MVPaqwlaLERLPLTPNGKLDRKALPAPEASVA---QQGYVAPRNALERTLAAIWQDVLGvERVGLDDNFFELGGDSIVS 1052
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*
gi 392926054 7467 IQIAHRlAEELKIEIKAHEILQSNSLKTFCNTLKNSVQKPISKVP 7511
Cdd:PRK12316 1053 IQVVSR-ARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGP 1096
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
6989-7412 1.11e-54

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 200.45  E-value: 1.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6989 EPALLLSTNTVSYSDLAEKIENISKDIQKQlqiakatSVREDELVGL---DCKNSYFALLACVFLGLPYAPIDPTWPEPR 7065
Cdd:cd05930     3 AVAVVDGDQSLTYAELDARANRLARYLRER-------GVGPGDLVAVlleRSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7066 qlfvkskVSFTLENCfSCNLKLRNFNSRtqfgsIYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVK 7145
Cdd:cd05930    76 -------LAYILEDS-GAKLVLTDPDDL-----AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTS 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7146 QVFDVSVSNIIGSVLNGG--VLISSEHSTTItDQL------QKCQYAFLPAAVFNGFTD-KTMSRLESIETLTIGGETVS 7216
Cdd:cd05930   143 FSFDVSVWEIFGALLAGAtlVVLPEEVRKDP-EALadllaeEGITVLHLTPSLLRLLLQeLELAALPSLRLVLVGGEALP 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7217 DVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKCK-----VSTLNIGSALGDS---LSNETCTICNNSVRGNVQVKGISL 7288
Cdd:cd05930   222 PDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPpddeeDGRVPIGRPIPNTrvyVLDENLRPVPPGVPGELYIGGAGL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7289 ARGYItSAPHGT-------PFSD---IYSTGDIVdsKLNS---LQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIV 7355
Cdd:cd05930   302 ARGYL-NRPELTaerfvpnPFGPgerMYRTGDLV--RWLPdgnLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAA 378
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054 7356 VL-----YSNQMLIAFIV-DQKSKLLHDSLVKTLKNRTQ---IPDYFVQINKMPLNSSGKVDKSLL 7412
Cdd:cd05930   379 VVaredgDGEKRLVAYVVpDEGGELDEEELRAHLAERLPdymVPSAFVVLDALPLTPNGKVDRKAL 444
PRK12467 PRK12467
peptide synthase; Provisional
6656-7633 6.32e-54

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 212.71  E-value: 6.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6656 FEIGKSTPLR---VRVAEDcdnsRIHIVFNQHHILTDGWSMTVLsdtVSSLYAAYRGETSFP--SKTKQTISQVAMGTKS 6730
Cdd:PRK12467 2751 FDLLSAPLLRltlVRTGED----RHHLIYTNHHILMDGWSGSQL---LGEVLQRYFGQPPPAreGRYRDYIAWLQAQDAE 2823
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6731 SGDI--KEALEYYQNTYH-----TIIPYDSETGNTSpsyvRISKLIPSKIwQKLVGLSKLYNTTMYNLALSVFCDAVRSF 6803
Cdd:PRK12467 2824 ASEAfwKEQLAALEEPTRlaralYPAPAEAVAGHGA----HYLHLDATQT-RQLIEFARRHRVTLNTLVQGAWLLLLQRF 2898
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6804 TGQADILLAYAISGRNAD---NSELIGYFMNnalfktSLP-FEILRLEEILNIVLNSLEKS----RSFATIPFYQMVEQN 6875
Cdd:PRK12467 2899 TGQDTVCFGATVAGRPAQlrgAEQQLGLFIN------TLPvIASPRAEQTVSDWLQQVQAQnlalREFEHTPLADIQRWA 2972
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6876 RKLNE-----ISLFFNF----RQKLDYPTVSMFGAKCEIEHLslNNAFDFSFTIDETPTgslITVDFDKSKYLDTTVHMF 6946
Cdd:PRK12467 2973 GQGGEalfdsILVFENYpiseALKQGAPSGLRFGAVSSREQT--NYPLTLAVGLGDTLE---LEFSYDRQHFDAAAIERL 3047
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6947 ANIF---LKKLNN-----LRNMNTTIP-IRRTDFPSTLFQKGLFTSWRLFTE------------PALLLSTNTVSYSDLA 7005
Cdd:PRK12467 3048 AESFdrlLQAMLNnpaarLGELPTLAAhERRQVLHAWNATAAAYPSERLVHQlieaqvartpeaPALVFGDQQLSYAELN 3127
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7006 EKIENISkdiQKQLQIAkatsVREDELVGLDCKNSY---FALLACVFLGLPYAPIDPTWPEPRQLF-------------- 7068
Cdd:PRK12467 3128 RRANRLA---HRLIAIG----VGPDVLVGVAVERSVemiVALLAVLKAGGAYVPLDPEYPRERLAYmiedsgvkllltqa 3200
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7069 --------VKSKVSFTLENCFSCNLKLRNFNSRTQFGSI-YSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIR 7139
Cdd:PRK12467 3201 hlleqlpaPAGDTALTLDRLDLNGYSENNPSTRVMGENLaYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDR 3280
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7140 VLDSVKQVFDVSVSNIIGSVLNGGVLI--SSEHST--TITDQLQKCQYA---FLPAAVFNGFTDKTMSRLESIETLTIGG 7212
Cdd:PRK12467 3281 VLLFMSFSFDGAQERFLWTLICGGCLVvrDNDLWDpeELWQAIHAHRISiacFPPAYLQQFAEDAGGADCASLDIYVFGG 3360
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7213 ETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKCKVSTLNIGSAL--GDSLSNETCTICNNS-------VRGNVQV 7283
Cdd:PRK12467 3361 EAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYApiGRPVAGRSIYVLDGQlnpvpvgVAGELYI 3440
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7284 KGISLARGYiTSAPHGT-------PFSD----IYSTGDIVDSKLNSL-QYIGRMDSQVKCKGVRINISEIEKELILCLGL 7351
Cdd:PRK12467 3441 GGVGLARGY-HQRPSLTaerfvadPFSGsggrLYRTGDLARYRADGViEYLGRIDHQVKIRGFRIELGEIEARLLQHPSV 3519
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7352 LQIVVL----YSNQMLIAFIV-DQKSKLLHDSLVKTLknRTQIPDYFVQ-----INKMPLNSSGKVDKslllQAFENIRK 7421
Cdd:PRK12467 3520 REAVVLardgAGGKQLVAYVVpADPQGDWRETLRDHL--AASLPDYMVPaqllvLAAMPLGPNGKVDR----KALPDPDA 3593
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7422 SYKREIVVMKNSLEEKVINVFSKILGR-NVAPTDKFESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLKTFCNTLk 7500
Cdd:PRK12467 3594 KGSREYVAPRSEVEQQLAAIWADVLGVeQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS- 3672
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7501 nsvqkPISKVP-NVITKLREVPNSKFNIYLVHAIGGTIYPYYSFLQIFPKDISLYGIEF----DLKYPSNDLRELAHFYA 7575
Cdd:PRK12467 3673 -----PLGDVPvNLLLDLNRLETGFPALFCRHEGLGTVFDYEPLAVILEGDRHVLGLTCrhllDDGWQDTSLQAMAVQYA 3747
                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054 7576 EEIAAHAGNKRIFVMGHSMGGIMSREIVAELKIWGYDIPFVMLFDSWVLRTNELDIEN 7633
Cdd:PRK12467 3748 DYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNTLPLPDEFVPQA 3805
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
825-1056 2.94e-53

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 189.38  E-value: 2.94e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   825 SDINVIACDYQFAGVEGEKELWDTLLTSRLTTGKISDIR---------KKQCEGDAGLEVGLLkQDISMFDNSFFAIAKD 895
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRwdpdklydpPSRIAGKIYTKWGGL-DDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   896 EAEFLDPQHRLLLNAAYNALEKSGLT--SIPDAD--LFLAISAH--SEYRALAEKHINELDERLWMGTVHSMVAGRLAVL 969
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITpdSLDGSRtgVFIGSGIGdyAALLLLDEDGGPRRGSPFAVGTMPSVIAGRISYF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   970 MGIRGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL---KTLLDHHSTNSFSVDGSGFCRSDG 1045
Cdd:pfam00109  160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEaDVALAGGVNLLLTPLGFAGFsaaGMLSPDGPCKAFDPFADGFVRGEG 239
                          250
                   ....*....|.
gi 392926054  1046 VGVIILKTAEK 1056
Cdd:pfam00109  240 VGAVVLKRLSD 250
PRK05691 PRK05691
peptide synthase; Validated
6472-7510 7.19e-50

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 199.24  E-value: 7.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6472 CEFVIAEIWKETLGISILnDANPNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEFTKFVKNLTTEkfAGNT 6551
Cdd:PRK05691  587 LQARIAAIWCEQLKVEQV-AADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAG--GGAA 663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6552 NDKI----SYDAIPLTNSQTQMFMLRQID-TTSKYNLIFKITISYETKFVweFLKYSLHSLIAYQPSYRTVFKSGNS-PY 6625
Cdd:PRK05691  664 QAAIarlpRGQALPQSLAQNRLWLLWQLDpQSAAYNIPGGLHLRGELDEA--ALRASFQRLVERHESLRTRFYERDGvAL 741
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6626 QYICSLTE-SFHDFD-------KRCNLNNAISHEPNHL-FEIGKSTPLRVRVAEdCDNSRIHIVFNQHHILTDGWSMTVL 6696
Cdd:PRK05691  742 QRIDAQGEfALQRIDlsdlpeaEREARAAQIREEEARQpFDLEKGPLLRVTLVR-LDDEEHQLLVTLHHIVADGWSLNIL 820
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6697 SDTVSSLYAAY-RGET-----------SFPSKTKQTISQvamgtkssGDIKEALEYYQNTY---HTIIPYDSE---TGNT 6758
Cdd:PRK05691  821 LDEFSRLYAAAcQGQTaelaplplgyaDYGAWQRQWLAQ--------GEAARQLAYWKAQLgdeQPVLELATDhprSARQ 892
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6759 SPSYVRISKLIPSKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAyaISGRNADNSE---LIGYFMNN--- 6832
Cdd:PRK05691  893 AHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIG--VPNANRPRLEtqgLVGFFINTqvl 970
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6833 -ALFKTSLPFEilrleEILNIVLNSLEKSRSFATIPFYQMVEQNRKLNEISLF---FNFRQKlDyptvsmFGAKCEIEHL 6908
Cdd:PRK05691  971 rAQLDGRLPFT-----ALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQGLFqvmFNHQQR-D------LSALRRLPGL 1038
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6909 --------SLNNAFDFSFTIDETPTGSLiTVDFDKSKYL--DTTVHMFANIFL-----------KKLNNLRNMNTTIPIR 6967
Cdd:PRK05691 1039 laeelpwhSREAKFDLQLHSEEDRNGRL-TLSFDYAAELfdAATIERLAEHFLalleqvcedpqRALGDVQLLDAAERAQ 1117
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6968 RTDF-------PSTLFQKGLFTSWRLFTEP-ALLLSTNTVSYSDLAEKIENISKDIQKQlqiakatSVREDELVGLDCKN 7039
Cdd:PRK05691 1118 LAQWgqapcapAQAWLPELLNEQARQTPERiALVWDGGSLDYAELHAQANRLAHYLRDK-------GVGPDVCVAIAAER 1190
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7040 S---YFALLACVFLGLPYAPIDPTWPEPRQLFV--KSKVSFTLEN-------------CFSC--NLKLRNFNSRTQFGSI 7099
Cdd:PRK05691 1191 SpqlLVGLLAILKAGGAYVPLDPDYPAERLAYMlaDSGVELLLTQshllerlpqaegvSAIAldSLHLDSWPSQAPGLHL 1270
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7100 ------YSIFTSGSTGVPKGV-----LMAEQ---SVSSFMTSASKQCMFRSNIRvldsvkqvFDVSVSN-----IIGS-- 7158
Cdd:PRK05691 1271 hgdnlaYVIYTSGSTGQPKGVgnthaALAERlqwMQATYALDDSDVLMQKAPIS--------FDVSVWEcfwplITGCrl 1342
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7159 VLNG----------GVLISSEHSTTItdqlqkcqyAFLPAaVFNGFTDKTMS-RLESIETLTIGGETVSDVVIETAMKKF 7227
Cdd:PRK05691 1343 VLAGpgehrdpqriAELVQQYGVTTL---------HFVPP-LLQLFIDEPLAaACTSLRRLFSGGEALPAELRNRVLQRL 1412
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7228 PRLRTIQIYGPTETCIWSLTNKCKVSTlNIGSALGDSLSNETCTICNNS-------VRGNVQVKGISLARGYITSA---- 7296
Cdd:PRK05691 1413 PQVQLHNRYGPTETAINVTHWQCQAED-GERSPIGRPLGNVLCRVLDAElnllppgVAGELCIGGAGLARGYLGRPalta 1491
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7297 ------PHGTPFSDIYSTGDIVDSKLN-SLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVLY----SNQMLIA 7365
Cdd:PRK05691 1492 erfvpdPLGEDGARLYRTGDRARWNADgALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVregaAGAQLVG 1571
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7366 FIVDQKSKLLHDSLVKT-LKnrTQIPDY-----FVQINKMPLNSSGKVD-KSLLLQAFEnirksyKREIVVMKNSLEEKV 7438
Cdd:PRK05691 1572 YYTGEAGQEAEAERLKAaLA--AELPEYmvpaqLIRLDQMPLGPSGKLDrRALPEPVWQ------QREHVEPRTELQQQI 1643
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7439 INVFSKILG-RNVAPTDKFESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLKTFCNTL-------KNSVQKPISKV 7510
Cdd:PRK05691 1644 AAIWREVLGlPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVariqaagERNSQGAIARV 1723
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
5259-5480 3.04e-48

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 175.13  E-value: 3.04e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5259 RVAVIGWSAEFSGSSNIHEYWENLMDGICSTG------------------------NNKYLLKNPFGFDNKFFNLTDEDA 5314
Cdd:pfam00109    2 PVAIVGMGCRFPGGNDPEEFWENLLEGRDGISeipadrwdpdklydppsriagkiyTKWGGLDDIFDFDPLFFGISPREA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5315 RVLDPQVRKFIQHAYLALENSGYV-KQKHELRCGVFAGAEPSDYG--RADDHDDAMRK---LFVMNMNSYLASYASYCLD 5388
Cdd:pfam00109   82 ERMDPQQRLLLEAAWEALEDAGITpDSLDGSRTGVFIGSGIGDYAalLLLDEDGGPRRgspFAVGTMPSVIAGRISYFLG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5389 LKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGFDDQKktMFSKSGVCRPFDKDSEGIVRGSG 5468
Cdd:pfam00109  162 LRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAG--MLSPDGPCKAFDPFADGFVRGEG 239
                          250
                   ....*....|..
gi 392926054  5469 VGCFVLKRYSQA 5480
Cdd:pfam00109  240 VGAVVLKRLSDA 251
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
6678-7481 3.25e-48

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 192.76  E-value: 3.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6678 HIVFNQHHILTDGWSMTVLSDTVSSLY-AAYRGETSFPSKTKQTISQVAM---GTKSSGDIKEALEYYQNTYHTII---- 6749
Cdd:COG1020   144 LLLLALHHIISDGLSDGLLLAELLRLYlAAYAGAPLPLPPLPIQYADYALwqrEWLQGEELARQLAYWRQQLAGLPplle 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6750 -PYD-SETGNTSPSYVRISKLIPSKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LI 6826
Cdd:COG1020   224 lPTDrPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEgLV 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6827 GYFMNNALFKTSLPFEiLRLEEILNIVLNSLEKSRSFATIPFYQMVE---QNRKLNEISLF---FNFrQKLDYPTVSMFG 6900
Cdd:COG1020   304 GFFVNTLPLRVDLSGD-PSFAELLARVRETLLAAYAHQDLPFERLVEelqPERDLSRNPLFqvmFVL-QNAPADELELPG 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6901 AKCEIEHLSLNNA-FDFSFTIDETPTGSLITVDFDKSKYLDTTVHMFANIFLkklNNLRNM--NTTIPIRRTDFPSTLFQ 6977
Cdd:COG1020   382 LTLEPLELDSGTAkFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLV---TLLEALaaDPDQPLGDLPLLTAAER 458
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6978 KGLFTSW--------------RLFTE--------PALLLSTNTVSYSDLAEKIEniskdiqkqlQIA---KATSVREDEL 7032
Cdd:COG1020   459 QQLLAEWnataapypadatlhELFEAqaartpdaVAVVFGDQSLTYAELNARAN----------RLAhhlRALGVGPGDL 528
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7033 VGLdcknsYF--------ALLACVFLGLPYAPIDPTWPEPRQLFV--KSKVSF-------------------TLENCFSC 7083
Cdd:COG1020   529 VGV-----CLerslemvvALLAVLKAGAAYVPLDPAYPAERLAYMleDAGARLvltqsalaarlpelgvpvlALDALALA 603
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7084 NLKLRNFNSRTQFGSI-YSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLdsvkQV----FDVSVSNIIGS 7158
Cdd:COG1020   604 AEPATNPPVPVTPDDLaYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVL----QFaslsFDASVWEIFGA 679
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7159 VLNGG--VLISSEHSTT---ITDQLQKCQ--YAFLPAAVFNGFTDKTMSRLESIETLTIGGETVSDVVIETAMKKFPRLR 7231
Cdd:COG1020   680 LLSGAtlVLAPPEARRDpaaLAELLARHRvtVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGAR 759
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7232 TIQIYGPTETCIWSLTNKC-----KVSTLNIGSAlgdsLSNETCTICNNS-------VRGNVQVKGISLARGYI-----T 7294
Cdd:COG1020   760 LVNLYGPTETTVDSTYYEVtppdaDGGSVPIGRP----IANTRVYVLDAHlqpvpvgVPGELYIGGAGLARGYLnrpelT 835
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7295 SA-----PHGTPFSDIYSTGDIV----DsklNSLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVLY-----SN 7360
Cdd:COG1020   836 AErfvadPFGFPGARLYRTGDLArwlpD---GNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAredapGD 912
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7361 QMLIAFIVDQKSKLLHDSLVKTLKNRTQ----IPDYFVQINKMPLNSSGKVDKSLLLQAFENIRksyKREIVVMKNSLEE 7436
Cdd:COG1020   913 KRLVAYVVPEAGAAAAAALLRLALALLLppymVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA---AAAAAPPAEEEEE 989
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*
gi 392926054 7437 KVINVFSKILGRNVAPTDKFESIGGNSLNAIQIAHRLAEELKIEI 7481
Cdd:COG1020   990 EAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLL 1034
PRK12316 PRK12316
peptide synthase; Provisional
6630-7495 1.53e-47

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 191.71  E-value: 1.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6630 SLTESFHDFDKRCNLNNAI----SHEPNHLFEIGKSTPLR---VRVAEDcdnsRIHIVFNQHHILTDGWSMTVLSDTVss 6702
Cdd:PRK12316 4177 SLPFAELDWRGRADLQAALdalaAAERERGFDLQRAPLLRlvlVRTAEG----RHHLIYTNHHILMDGWSNSQLLGEV-- 4250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6703 lYAAYRGETSFPS--KTKQTIS--QVAMGTKSSGDIKEALEYYQNTYHTIIPYDSETGNTSPSYVRISKLIPSKIWQKLV 6778
Cdd:PRK12316 4251 -LERYSGRPPAQPggRYRDYIAwlQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRSANGYGEHVRELDATATARLR 4329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6779 GLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNAD---NSELIGYFMNNALFKTSlPFEILRLEEILNIVLN 6855
Cdd:PRK12316 4330 EFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAElpgIEGQIGLFINTLPVIAT-PRAQQSVVEWLQQVQR 4408
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6856 SLEKSRSFATIPFYQmVEQNRKLNEISLF---FNFRqklDYPTVSMF--GAKCEIE------HLSLNNAFDFSFTIDETP 6924
Cdd:PRK12316 4409 QNLALREHEHTPLYE-IQRWAGQGGEALFdslLVFE---NYPVSEALqqGAPGGLRfgevtnHEQTNYPLTLAVGLGETL 4484
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6925 TGSLitvDFDKSKYLDTTVHMFANIFLkklNNLRNMNTTIPIR--------------------RTD--FPSTLFQKGLFT 6982
Cdd:PRK12316 4485 SLQF---SYDRGHFDAATIERLARHLT---NLLEAMAEDPQRRlgelqllekaeqqrivalwnRTDagYPATRCVHQLVA 4558
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6983 SW-RLFTE-PALLLSTNTVSYSDLAEKIENISKDIqkqlqIAKAtsVREDELVGLDCKNS---YFALLACVFLGLPYAPI 7057
Cdd:PRK12316 4559 ERaRMTPDaVAVVFDEEKLTYAELNRRANRLAHAL-----IARG--VGPEVLVGIAMERSaemMVGLLAVLKAGGAYVPL 4631
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7058 DPTWPEPRQLFV--KSKVSFTLENC-----------FSCnLKLRNFNSRTQFGS------------IYSIFTSGSTGVPK 7112
Cdd:PRK12316 4632 DPEYPRERLAYMmeDSGAALLLTQShllqrlpipdgLAS-LALDRDEDWEGFPAhdpavrlhpdnlAYVIYTSGSTGRPK 4710
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7113 GVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEHSTTITDQL------QKCQYAFL 7186
Cdd:PRK12316 4711 GVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLyaeiheHRVTVLVF 4790
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7187 PAAVFNGFTDKTMSRLE--SIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKCKVSTLNIGSA--LG 7262
Cdd:PRK12316 4791 PPVYLQQLAEHAERDGEppSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYmpIG 4870
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7263 DSLSNETCTICNNS-------VRGNVQVKGISLARGY-----ITSA-----PHGTPFSDIYSTGDIVDSKLNS-LQYIGR 7324
Cdd:PRK12316 4871 TPLGNRSGYVLDGQlnplpvgVAGELYLGGEGVARGYlerpaLTAErfvpdPFGAPGGRLYRTGDLARYRADGvIDYLGR 4950
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7325 MDSQVKCKGVRINISEIEKELILCLGLLQIVVL----YSNQMLIAFIVDQKSKLLHDSLVKT-----LKN--RTQIPDY- 7392
Cdd:PRK12316 4951 VDHQVKIRGFRIELGEIEARLREHPAVREAVVIaqegAVGKQLVGYVVPQDPALADADEAQAelrdeLKAalRERLPEYm 5030
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7393 ----FVQINKMPLNSSGKVDK--------SLLLQAFenirksykreiVVMKNSLEEKVINVFSKILG-RNVAPTDKFESI 7459
Cdd:PRK12316 5031 vpahLVFLARMPLTPNGKLDRkalpqpdaSLLQQAY-----------VAPRSELEQQVAAIWAEVLQlERVGLDDNFFEL 5099
                         970       980       990
                  ....*....|....*....|....*....|....*.
gi 392926054 7460 GGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLKTF 7495
Cdd:PRK12316 5100 GGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAF 5135
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
7027-7419 2.02e-47

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 180.05  E-value: 2.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7027 VREDELVGLD---CKNSYFALLACVFLGLPYAPIDPTWPEPRQLF----VKSKVSFTLEncfSCNLklrnfnsrtqfgsI 7099
Cdd:cd05918    46 VGPGVFVPLCfekSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEilqdTGAKVVLTSS---PSDA-------------A 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7100 YSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGG-VLISSEHstTITDQL 7178
Cdd:cd05918   110 YVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGcLCIPSEE--DRLNDL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7179 QKC------QYAFLPAAVFNGFTDKTmsrLESIETLTIGGETVSDVVIET-AmkkfPRLRTIQIYGPTETCIWSLTNKCK 7251
Cdd:cd05918   188 AGFinrlrvTWAFLTPSVARLLDPED---VPSLRTLVLGGEALTQSDVDTwA----DRVRLINAYGPAECTIAATVSPVV 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7252 VST--LNIGSALGdslsnetCTIC----NNSVR-------GNVQVKGISLARGYI-----TSA-----------PHGTPF 7302
Cdd:cd05918   261 PSTdpRNIGRPLG-------ATCWvvdpDNHDRlvpigavGELLIEGPILARGYLndpekTAAafiedpawlkqEGSGRG 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7303 SDIYSTGDIV----DSklnSLQYIGRMDSQVKCKGVRINISEIEKELILCL-GLLQIVVLY-------SNQMLIAFIVDQ 7370
Cdd:cd05918   334 RRLYRTGDLVrynpDG---SLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLpGAKEVVVEVvkpkdgsSSPQLVAFVVLD 410
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7371 KSKLLHD--------------SLVKTLKNRTQ-------IPDYFVQINKMPLNSSGKVDKSLLLQAFENI 7419
Cdd:cd05918   411 GSSSGSGdgdslflepsdefrALVAELRSKLRqrlpsymVPSVFLPLSHLPLTASGKIDRRALRELAESL 480
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
6991-7414 1.23e-45

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 173.65  E-value: 1.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6991 ALLLSTNTVSYSDLAEKIENISKDIQKQLQIAKATSVredeLVGLDCKNSYFALLACVFLGLPYAPIDPTWPEPRqlfvk 7070
Cdd:cd17653    15 AVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVP----LLSDRSLEMLVAILAILKAGAAYVPLDAKLPSAR----- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7071 skVSFTLENCfSCNLKLrnFNSRTQFGSiYSIFTSGSTGVPKGVLMAEQSVSSFMTSASkqcmFRSNIRVLDSVKQV--- 7147
Cdd:cd17653    86 --IQAILRTS-GATLLL--TTDSPDDLA-YIIFTSGSTGIPKGVMVPHRGVLNYVSQPP----ARLDVGPGSRVAQVlsi 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7148 -FDVSVSNIIGSVLNGGVLISSEHSTTITDQLQKCQyaFLPAavfngfTDKTMSRLE-----SIETLTIGGETVSDVVIE 7221
Cdd:cd17653   156 aFDACIGEIFSTLCNGGTLVLADPSDPFAHVARTVD--ALMS------TPSILSTLSpqdfpNLKTIFLGGEAVPPSLLD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7222 tamKKFPRLRTIQIYGPTETCIWSLTnkckvSTLNIGSA--LGDSLSNETCTICNN-------SVRGNVQVKGISLARGY 7292
Cdd:cd17653   228 ---RWSPGRRLYNAYGPTECTISSTM-----TELLPGQPvtIGKPIPNSTCYILDAdlqpvpeGVVGEICISGVQVARGY 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7293 I------TSAPHGTPF---SDIYSTGDI--VDSKlNSLQYIGRMDSQVKCKGVRINISEIEKELILCLGLL-QIVVLYSN 7360
Cdd:cd17653   300 LgnpaltASKFVPDPFwpgSRMYRTGDYgrWTED-GGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVtQAAAIVVN 378
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054 7361 QMLIAFIVDQKSKL--LHDSLVKTLkNRTQIPDYFVQINKMPLNSSGKVDKSLLLQ 7414
Cdd:cd17653   379 GRLVAFVTPETVDVdgLRSELAKHL-PSYAVPDRIIALDSFPLTANGKVDRKALRE 433
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
5259-5645 2.86e-45

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 171.57  E-value: 2.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5259 RVAVIGWSAEFSGSSNIHEYWENLMDGICSTGNNKYLLKNPF----GFDNKFFNLTDEDARVLDPQVRKFIQHAYL---- 5330
Cdd:cd00834     2 RVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFpsriAGEVPDFDPEDYLDRKELRRMDRFAQFALAaaee 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5331 ALENSGYVKQKHEL-RCGVFAGaepSDYGRADDHDDAMRKL------------FVMNMNSYLASYASYCLDLKGEAVSVY 5397
Cdd:cd00834    82 ALADAGLDPEELDPeRIGVVIG---SGIGGLATIEEAYRALlekgprrvspffVPMALPNMAAGQVAIRLGLRGPNYTVS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5398 SACSTALVAVANAVKSIQSGSMDYALVGA--ASIAEVS-------GALS-GFDDQKKTmfsksgvCRPFDKDSEGIVRGS 5467
Cdd:cd00834   159 TACASGAHAIGDAARLIRLGRADVVIAGGaeALITPLTlagfaalRALStRNDDPEKA-------SRPFDKDRDGFVLGE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5468 GVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRASfMAPNPAGQLKCMTDVLARfTNKEKERISFVECHATGTTLGD 5547
Cdd:cd00834   232 GAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITA-PDPDGEGAARAMRAALAD-AGLSPEDIDYINAHGTSTPLND 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5548 TIEMNSLRTAY-SFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSEFRDGMGQFFTVNGKKSTISQN 5626
Cdd:cd00834   310 AAESKAIKRVFgEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRY 389
                         410
                  ....*....|....*....
gi 392926054 5627 SLisIDSFGIGGTNVHMVI 5645
Cdd:cd00834   390 AL--SNSFGFGGHNASLVF 406
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
13-394 3.14e-45

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 171.57  E-value: 3.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   13 PNGEDGHEMAENIFLNRNNIAllPVEKNYLSDFREKHpevkAALVDGieyFDDQYFGTgESEAICMDPQQRMLMQGVIKG 92
Cdd:cd00834    13 PLGNGVEEFWEALLAGRSGIR--PITRFDASGFPSRI----AGEVPD---FDPEDYLD-RKELRRMDRFAQFALAAAEEA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   93 LENAGITLEMASEARVAVY-------TAAWCYDYKDLL--------PPDQYMATGNSASvmcGRITYFLNSRGAAVGIET 157
Cdd:cd00834    83 LADAGLDPEELDPERIGVVigsgiggLATIEEAYRALLekgprrvsPFFVPMALPNMAA---GQVAIRLGLRGPNYTVST 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  158 ACSSSLVAFHLARQAIQSGETKLALVCGA----NHVGSRSFHSLY--NSHMVSPNGRLAAFDRSANGFVRAESFAVAVLC 231
Cdd:cd00834   160 ACASGAHAIGDAARLIRLGRADVVIAGGAealiTPLTLAGFAALRalSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  232 SKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNP--ISQYEVQLEALK--NIDKDSVQLVTCHGTGTKLGDQVELTAIN 307
Cdd:cd00834   240 SLEHAKARGAKIYAEILGYGASSDAY--HITAPDPdgEGAARAMRAALAdaGLSPEDIDYINAHGTSTPLNDAAESKAIK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  308 RSFKSD---IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDksmgFVNEEME--LNRVAIS- 381
Cdd:cd00834   318 RVFGEHakkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLD----YVPNEAReaPIRYALSn 393
                         410
                  ....*....|...
gi 392926054  382 SYGFGGTNACAII 394
Cdd:cd00834   394 SFGFGGHNASLVF 406
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
3203-3377 8.26e-43

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 156.49  E-value: 8.26e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTA----KALREFEHWKSKVHTIAADINDKE---KLIRELTKLNV 3275
Cdd:smart00822    1 GTYLITGGLGGLGRALARWLAERGARRLVLLSRSGPDApgaaALLAELEAAGARVTVVACDVADRDalaAVLAAIPAVEG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   3276 GITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHfnYKIENFIMMSSFTAACGNEGQLNYGVSNAYLEY 3355
Cdd:smart00822   81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTAD--LPLDFFVLFSSIAGVLGSPGQANYAAANAFLDA 158
                           170       180
                    ....*....|....*....|..
gi 392926054   3356 QVQRRRRQGKSGCAIQWGNWID 3377
Cdd:smart00822  159 LAEYRRARGLPALSIAWGAWAE 180
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
6991-7412 1.23e-42

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 165.69  E-value: 1.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6991 ALLLSTNTVSYSDLAEKIENISKDIQkqlqiakATSVREDELVGLDCKNSY---FALLACVFLGLPYAPIDPTWPEPRQL 7067
Cdd:cd17644    18 AVVFEDQQLTYEELNTKANQLAHYLQ-------SLGVKSESLVGICVERSLemiIGLLAILKAGGAYVPLDPNYPQERLT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7068 FV--KSKVSFTLENcfSCNLklrnfnsrtqfgsIYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVK 7145
Cdd:cd17644    91 YIleDAQISVLLTQ--PENL-------------AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFAS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7146 QVFDVSVSNIIGSVLNGG--VLISSEHSTTITDQLQKCQYAFL-----PAAVF----NGFTDKTMSRLESIETLTIGGET 7214
Cdd:cd17644   156 IAFDVAAEEIYVTLLSGAtlVLRPEEMRSSLEDFVQYIQQWQLtvlslPPAYWhllvLELLLSTIDLPSSLRLVIVGGEA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7215 VSDVVIETAMKKF-PRLRTIQIYGPTE----TCIWSLTNKCKVSTLNIgsALGDSLSNETCTICNNS-------VRGNVQ 7282
Cdd:cd17644   236 VQPELVRQWQKNVgNFIQLINVYGPTEatiaATVCRLTQLTERNITSV--PIGRPIANTQVYILDENlqpvpvgVPGELH 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7283 VKGISLARGY-----------ITSAPHGTPFSDIYSTGDIV----DSklnSLQYIGRMDSQVKCKGVRINISEIEKELIL 7347
Cdd:cd17644   314 IGGVGLARGYlnrpeltaekfISHPFNSSESERLYKTGDLArylpDG---NIEYLGRIDNQVKIRGFRIELGEIEAVLSQ 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926054 7348 CLGLLQIVVLY-----SNQMLIAFIVDQKSK-LLHDSLVKTLKNRT---QIPDYFVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17644   391 HNDVKTAVVIVredqpGNKRLVAYIVPHYEEsPSTVELRQFLKAKLpdyMIPSAFVVLEELPLTPNGKIDRRAL 464
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
3200-3424 3.72e-42

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 161.78  E-value: 3.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3200 PITGNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWK---SKVHTIAADINDKE---KLIRELTKL 3273
Cdd:cd05274   148 GLDGTYLITGGLGGLGLLVARWLAARGARHLVLLSRRGPAPRAAARAALLRaggARVSVVRCDVTDPAalaALLAELAAG 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3274 nVGITGIIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHfnyKIENFIMMSSFTAACGNEGQLNYGVSNAY 3352
Cdd:cd05274   228 -GPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGaLNLHELTPDL---PLDFFVLFSSVAALLGGAGQAAYAAANAF 303
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926054 3353 LEYQVQRRRRQGKSGCAIQWGNWIDTGMATDENVRKFLANLGFLGQHNKDALKYLRACILTKPELIMVANID 3424
Cdd:cd05274   304 LDALAAQRRRRGLPATSVQWGAWAGGGMAAAAALRARLARSGLGPLAPAEALEALEALLASDAPQAVVASVD 375
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
5258-5645 3.21e-41

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 159.88  E-value: 3.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5258 TRVAVIGWSAEFSGSSNIHEYWENLMDGICSTGNNKYLlkNPFGFDNKF------FNLTD----EDARVLDPqvrkFIQH 5327
Cdd:COG0304     1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRF--DASGLPVRIagevkdFDPEEyldrKELRRMDR----FTQY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5328 AY----LALENSGYVKQKHEL-RCGVFAGaepSDYGRADDHDDAMRKL------------FVMNMNSYLASYASYCLDLK 5390
Cdd:COG0304    75 ALaaarEALADAGLDLDEVDPdRTGVIIG---SGIGGLDTLEEAYRALlekgprrvspffVPMMMPNMAAGHVSIRFGLK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5391 GEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASiAEVS----------GALSGFDDQKKTmfsksgVCRPFDKDS 5460
Cdd:COG0304   152 GPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAE-AAITplglagfdalGALSTRNDDPEK------ASRPFDKDR 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5461 EGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHsRASFMAPNPAGQLKCMTDVLARfTNKEKERISFVECHA 5540
Cdd:COG0304   225 DGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAY-HITAPAPDGEGAARAMRAALKD-AGLSPEDIDYINAHG 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5541 TGTTLGDTIEMNSLRTAysFKN---KLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSEFRDGMGQFFTVN 5617
Cdd:COG0304   303 TSTPLGDAAETKAIKRV--FGDhayKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPN 380
                         410       420       430
                  ....*....|....*....|....*....|...
gi 392926054 5618 GKKSTisqnsliSID-----SFGIGGTNVHMVI 5645
Cdd:COG0304   381 EAREA-------KIDyalsnSFGFGGHNASLVF 406
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
13-396 5.05e-41

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 159.49  E-value: 5.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   13 PNGEDGHEMAENIFLNRNNIAllPVEKNYLSDFREKHpevkAALVDGieyFD-DQYFGtgESEAICMDPQQRMLMQGVIK 91
Cdd:COG0304    13 PLGNGVEEFWEALLAGRSGIR--PITRFDASGLPVRI----AGEVKD---FDpEEYLD--RKELRRMDRFTQYALAAARE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   92 GLENAGITLEMASEARVAVY-------TAAWCYDYKDL-------LPPDQY-MATGNSASvmcGRITYFLNSRGAAVGIE 156
Cdd:COG0304    82 ALADAGLDLDEVDPDRTGVIigsgiggLDTLEEAYRALlekgprrVSPFFVpMMMPNMAA---GHVSIRFGLKGPNYTVS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  157 TACSSSLVAFHLARQAIQSGETKLALVCGA----NHVGSRSFHSLynsHMVSP-NGRLAA----FDRSANGFVRAESFAV 227
Cdd:COG0304   159 TACASGAHAIGEAYRLIRRGRADVMIAGGAeaaiTPLGLAGFDAL---GALSTrNDDPEKasrpFDKDRDGFVLGEGAGV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  228 AVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTA 305
Cdd:COG0304   236 LVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDagLSPEDIDYINAHGTSTPLGDAAETKA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  306 INRSFK---SDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDksmgFV-NE--EMELNRVA 379
Cdd:COG0304   316 IKRVFGdhaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLD----YVpNEarEAKIDYAL 391
                         410
                  ....*....|....*..
gi 392926054  380 ISSYGFGGTNACAIIEK 396
Cdd:COG0304   392 SNSFGFGGHNASLVFKR 408
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
830-1197 5.72e-41

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 155.56  E-value: 5.72e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    830 IACdyQFAGVEGEKELWDTLLtsrlttgkisdirkkqcegdAGLEvgllkqDISMFDNSFFAIAKDEAEFLDPQHRLLLN 909
Cdd:smart00825    6 MSC--RFPGADDPEEFWDLLL--------------------AGLD------DVDLFDAAFFGISPREAEAMDPQQRLLLE 57
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    910 AAYNALEKSGltsIPDADLflaisahseyralaekhinelderlwMGTvhsmvagRLAVLMGIRGR--AMIVDTTCSSVA 987
Cdd:smart00825   58 VAWEALEDAG---IDPESL--------------------------RGS-------RTGVFVGVSSSdySVTVDTACSSSL 101
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054    988 TALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSLKTL--L--DHHStNSFSVDGSGFCRSDGVGVIILKTAEK----GD 1058
Cdd:smart00825  102 VALHLACQSLRSGEcDMALAGGVNLILSPDTFVGLSRAgmLspDGRC-KTFDASADGYVRGEGVGVVVLKRLSDalrdGD 180
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   1059 S--AVIKiSSAkSHHCGA---VMTPvvSSISQLLeeagsfsyveghgtatsagdsaesmayqkLGselimsSVKAQFGHC 1133
Cdd:smart00825  181 PilAVIR-GSA-VNQDGRsngITAP--SGPAQLL-----------------------------IG------SVKSNIGHL 221
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054   1134 EVASGLIQLMKVSSIGKHGIIPSIVHNILPSEHIRNNE-NIRLPFVAEEKQID----RSAIVSFGITGT 1197
Cdd:smart00825  222 EAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEEsPLRVPTELTPWPPPgrprRAGVSSFGFGGT 290
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
6985-7412 1.40e-40

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 160.19  E-value: 1.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6985 RLFTE--------PALLLSTNTVSYSDLAEKIENISkdiqkqlQIAKATSVREDELVGLDCKNS---YFALLACVFLGLP 7053
Cdd:cd17655     1 ELFEEqaektpdhTAVVFEDQTLTYRELNERANQLA-------RTLREKGVGPDTIVGIMAERSlemIVGILGILKAGGA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7054 YAPIDPTWPEPR-QLFVK-SKVSFTL-ENCFSCNLKLRNFNSRTQFGSIYS------------------IFTSGSTGVPK 7112
Cdd:cd17655    74 YLPIDPDYPEERiQYILEdSGADILLtQSHLQPPIAFIGLIDLLDEDTIYHeesenlepvsksddlayvIYTSGSTGKPK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7113 GVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEHStTITDQLQKCQY--------A 7184
Cdd:cd17655   154 GVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKE-TVLDGQALTQYirqnritiI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7185 FLPAAVFNGFTDKTMSRLESIETLTIGGETVSDVVIETAMKKFPRLRTI-QIYGPTETCIWSLTNKCKVSTLNIGS-ALG 7262
Cdd:cd17655   233 DLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTItNAYGPTETTVDASIYQYEPETDQQVSvPIG 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7263 DSLSNETCTICNNS-------VRGNVQVKGISLARGY-----ITSA---PHgtPF---SDIYSTGDIV----DSklnSLQ 7320
Cdd:cd17655   313 KPLGNTRIYILDQYgrpqpvgVAGELYIGGEGVARGYlnrpeLTAEkfvDD--PFvpgERMYRTGDLArwlpDG---NIE 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7321 YIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL-----YSNQMLIAFIV---DQKSKLLHDSLVKTLKNrTQIPDY 7392
Cdd:cd17655   388 FLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIarkdeQGQNYLCAYIVsekELPVAQLREFLARELPD-YMIPSY 466
                         490       500
                  ....*....|....*....|
gi 392926054 7393 FVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17655   467 FIKLDEIPLTPNGKVDRKAL 486
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
3203-3377 3.20e-40

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 149.25  E-value: 3.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPT----AKALREFEHWKSKVHTIAADINDK---EKLIRELTKLNV 3275
Cdd:pfam08659    1 GTYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPrpdaQALIAELEARGVEVVVVACDVSDPdavAALLAEIKAEGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3276 GITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFNykIENFIMMSSFTAACGNEGQLNYGVSNAYLEY 3355
Cdd:pfam08659   81 PIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEP--LDFFVLFSSIAGLLGSPGQANYAAANAFLDA 158
                          170       180
                   ....*....|....*....|..
gi 392926054  3356 QVQRRRRQGKSGCAIQWGNWID 3377
Cdd:pfam08659  159 LAEYRRSQGLPATSINWGPWAE 180
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
3644-3925 3.61e-40

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272922 [Multi-domain]  Cd Length: 290  Bit Score: 153.01  E-value: 3.61e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3644 SKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQsclkKCDEYLQgdVSLWEILFNTDhYKLLQLTKHMQPIMFCFGYATA 3723
Cdd:TIGR00128    1 MKIAYVFPGQGSQTVGMGKDLYEQYPIAKELFD----QASEALG--YDLKKLCQEGP-AEELNKTQYTQPALYVVSAILY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3724 QLWL-SLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENI-----AGLGALLAVQREIADEVLRKFK--- 3794
Cdd:TIGR00128   74 LKLKeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAvpeggGAMAAVIGLDEEQLAQACEEATend 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3795 VSVATINSPKQVVFAGTKSVLDAALAFVKGQG-KQATYVNQQYPFHSNLIQETHLvSLRQCLADIKFSAGRTPLVSNVTG 3873
Cdd:TIGR00128  154 VDLANFNSPGQVVISGTKDGVEAAAALFKEMGaKRAVPLEVSGAFHSRFMKPAAE-KFAETLEACQFNDPTVPVISNVDA 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392926054  3874 QIINTFSEA--YIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:TIGR00128  233 KPYTNGDRIkeKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGLIKRI 286
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
5488-5603 2.45e-39

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 144.25  E-value: 2.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5488 HFVIKDFAINNDGHSrASFMAPNPAGQLKCMTDVLARfTNKEKERISFVECHATGTTLGDTIEMNSLRTAYSFKNK---L 5564
Cdd:pfam02801    1 YAVIKGSAVNHDGRH-NGLTAPNGEGQARAIRRALAD-AGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqpL 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 392926054  5565 AIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNF 5603
Cdd:pfam02801   79 AIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
81-394 3.61e-39

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 151.63  E-value: 3.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   81 QQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLLPPDQ-------YMATGNSASVMCGRITYFLNSRGAAV 153
Cdd:cd00825    11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADamravgpYVVTKAMFPGASGQIATPLGIHGPAY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  154 GIETACSSSLVAFHLARQAIQSGETKLALvCGANHVGSRSFHSLYNSH--MVSPNGRLAAFDRSANGFVRAESFAVAVLC 231
Cdd:cd00825    91 DVSAACAGSLHALSLAADAVQNGKQDIVL-AGGSEELAAPMDCEFDAMgaLSTPEKASRTFDAAADGFVFGDGAGALVVE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  232 SKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALK--NIDKDSVQLVTCHGTGTKLGDQVELTAINRS 309
Cdd:cd00825   170 ELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAvaGLTVWDIDYLVAHGTGTPIGDVKELKLLRSE 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  310 FKSDIR-VMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLgeDKSMGFVNEEmELNRVAISSYGFGGT 388
Cdd:cd00825   250 FGDKSPaVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAG--LNIVTETTPR-ELRTALLNGFGLGGT 326

                  ....*.
gi 392926054  389 NACAII 394
Cdd:cd00825   327 NATLVL 332
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
6990-7412 6.12e-39

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 155.05  E-value: 6.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLAEKIENISKDIQKQlqiakatSVREDELVGLDCKNSY---FALLACVFLGLPYAPIDPTWPEPRQ 7066
Cdd:cd12117    14 VAVVYGDRSLTYAELNERANRLARRLRAA-------GVGPGDVVGVLAERSPelvVALLAVLKAGAAYVPLDPELPAERL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7067 LFV-------------KSKVSFTLENCFSCNLKLRNF----NSRTQFGS---IYSIFTSGSTGVPKGVLMAEQSV----- 7121
Cdd:cd12117    87 AFMladagakvlltdrSLAGRAGGLEVAVVIDEALDAgpagNPAVPVSPddlAYVMYTSGSTGRPKGVAVTHRGVvrlvk 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7122 -SSFMTsaskqcmFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEHSTTIT-DQL------QKCQYAFLPAAVFNG 7193
Cdd:cd12117   167 nTNYVT-------LGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDpDALgaliaeEGVTVLWLTAALFNQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7194 FTDKTMSRLESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTE----TCIWSLTNKCKV-STLNIGSALGDS---L 7265
Cdd:cd12117   240 LADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEnttfTTSHVVTELDEVaGSIPIGRPIANTrvyV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7266 SNETCTICNNSVRGNVQVKGISLARGYItSAPHGT-------PFSD---IYSTGDIVdsKLN---SLQYIGRMDSQVKCK 7332
Cdd:cd12117   320 LDEDGRPVPPGVPGELYVGGDGLALGYL-NRPALTaerfvadPFGPgerLYRTGDLA--RWLpdgRLEFLGRIDDQVKIR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7333 GVRINISEIEKELILCLGLLQIVVL-----YSNQMLIAFIVdQKSKLLHDSLVKTLKNRT---QIPDYFVQINKMPLNSS 7404
Cdd:cd12117   397 GFRIELGEIEAALRAHPGVREAVVVvredaGGDKRLVAYVV-AEGALDAAELRAFLRERLpayMVPAAFVVLDELPLTAN 475

                  ....*...
gi 392926054 7405 GKVDKSLL 7412
Cdd:cd12117   476 GKVDRRAL 483
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
78-394 1.79e-38

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 151.82  E-value: 1.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   78 MDPQQRMLMQGVIKGLENAGIT-LEMASEARVAVYT-------AAWCYDYKDLLP---PDQYMATGNSASVMCGRI-TYF 145
Cdd:cd00828    69 VDRTTLLALVATEEALADAGITdPYEVHPSEVGVVVgsgmgglRFLRRGGKLDARavnPYVSPKWMLSPNTVAGWVnILL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  146 LNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGANHVGSRSFHSLYNSHMVS-----PNGRLAAFDRSANGFV 220
Cdd:cd00828   149 LSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALStaeeePEEMSRPFDETRDGFV 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  221 RAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISqYEVQLEALK--NIDKDSVQLVTCHGTGTKLG 298
Cdd:cd00828   229 EAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGI-ARAIRTALAkaGLSLDDLDVISAHGTSTPAN 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  299 DQVELTAINRSFK---SDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDkSMGFVNEEMEL 375
Cdd:cd00828   308 DVAESRAIAEVAGalgAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHL-SVVGLSRDLNL 386
                         330       340
                  ....*....|....*....|.
gi 392926054  376 N-RVAIS-SYGFGGTNACAII 394
Cdd:cd00828   387 KvRAALVnAFGFGGSNAALVL 407
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
5345-5645 2.75e-38

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 148.94  E-value: 2.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5345 RCGVFAGAEPSDYGRADDHDDAMRKLFVMNMNSYLASYASYC----LDLKGEAVSVYSACSTALVAVANAVKSIQSGSMD 5420
Cdd:cd00825    37 IVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGASGQiatpLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5421 YALVGAASIaeVSGALSGFDDQKKTMFSKSGVCRPFDKDSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDG 5500
Cdd:cd00825   117 IVLAGGSEE--LAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5501 HSRASFmAPNPAGQLKCMTDVLARfTNKEKERISFVECHATGTTLGDTIEMNSLRTAYSFKnKLAIGSCKANIGHAYAAS 5580
Cdd:cd00825   195 AGMGAF-APSAEGLARAAKEALAV-AGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDK-SPAVSATKAMTGNLSSAA 271
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926054 5581 GLAALVKCAKMLQTGIIPPQVNFSEFRDGMGQFFTvngkKSTISQNSLISIDSFGIGGTNVHMVI 5645
Cdd:cd00825   272 VVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVT----ETTPRELRTALLNGFGLGGTNATLVL 332
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
3203-3425 2.91e-38

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 150.51  E-value: 2.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKA---LREFEHWKSKVHTIAADINDKEKLIRELTKLNVG--- 3276
Cdd:cd08955   150 ATYLITGGLGGLGLLVAEWLVERGARHLVLTGRRAPSAAArqaIAALEEAGAEVVVLAADVSDRDALAAALAQIRASlpp 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3277 ITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFNykIENFIMMSSFTAACGNEGQLNYGVSNAYLEYQ 3356
Cdd:cd08955   230 LRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLP--LDFFVLFSSVASLLGSPGQANYAAANAFLDAL 307
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 3357 VQRRRRQGKSGCAIQWGNWIDTGMATDENVRKFLANLGFLGQHNKDALKYLRACILTKPELIMVANIDW 3425
Cdd:cd08955   308 AHYRRARGLPALSINWGPWAEVGMAASLARQARLEARGVGAISPAAGLQALGQLLRTGSTQVGVAPVDW 376
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
7000-7356 5.07e-38

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 150.49  E-value: 5.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7000 SYSDLAEKIENISKdiqkqlQIAKATSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPRqlfvkskVSFT 7076
Cdd:TIGR01733    1 TYRELDERANRLAR------HLRAAGGVGPGDRVAVLLERSaelVVAILAVLKAGAAYVPLDPAYPAER-------LAFI 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7077 LENC--------------FSCNLKLRNFNSRTQFGSI-------------------YSIFTSGSTGVPKGVLMAEQSVSS 7123
Cdd:TIGR01733   68 LEDAgarllltdsalasrLAGLVLPVILLDPLELAALddapappppdapsgpddlaYVIYTSGSTGRPKGVVVTHRSLVN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7124 FMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGG--VLISSEHSTTITDQLQ------KCQYAFLPAAVFNGFT 7195
Cdd:TIGR01733  148 LLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGAtlVVPPEDEERDDAALLAaliaehPVTVLNLTPSLLALLA 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7196 DKTMSRLESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKC------KVSTLNIGSALGdslsNET 7269
Cdd:TIGR01733  228 AALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVdpddapRESPVPIGRPLA----NTR 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7270 CTICNNSVR-------GNVQVKGISLARGY-----------ITSAPHGTPFSDIYSTGDIVdsKLNS---LQYIGRMDSQ 7328
Cdd:TIGR01733  304 LYVLDDDLRpvpvgvvGELYIGGPGVARGYlnrpeltaerfVPDPFAGGDGARLYRTGDLV--RYLPdgnLEFLGRIDDQ 381
                          410       420
                   ....*....|....*....|....*...
gi 392926054  7329 VKCKGVRINISEIEKELILCLGLLQIVV 7356
Cdd:TIGR01733  382 VKIRGYRIELGEIEAALLRHPGVREAVV 409
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
244-354 2.06e-37

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 138.86  E-value: 2.06e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   244 HCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSD-----IRV 316
Cdd:pfam02801    1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADagVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGarkqpLAI 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 392926054   317 MSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLE 354
Cdd:pfam02801   81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
3203-3424 1.08e-36

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 147.51  E-value: 1.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRR------QPTAKALREFEHWKSKVHTIAADINDKE---KLIRELTKL 3273
Cdd:cd08953   206 GVYLVTGGAGGIGRALARALARRYGARLVLLGRSplppeeEWKAQTLAALEALGARVLYISADVTDAAavrRLLEKVRER 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3274 NVGITGIIHSAGVLKDSKIERQNKESFNQVFTPKANG----FHVLEEIEKHFnykienFIMMSSFTAACGNEGQLNYGVS 3349
Cdd:cd08953   286 YGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGllnlAQALADEPLDF------FVLFSSVSAFFGGAGQADYAAA 359
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054 3350 NAYLEYQVQRRRRQGKSG--CAIQWGNWIDTGMATDENVRKFLANLGFLGQHNKDALKYLRACILTKPELIMVANID 3424
Cdd:cd08953   360 NAFLDAFAAYLRQRGPQGrvLSINWPAWREGGMAADLGARELLARAGLLPIEPEEGLQALEQALSSDLPQVLVSPGD 436
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
5274-5641 2.07e-36

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 145.99  E-value: 2.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5274 NIHEYWENLMDGICST------------------GNNKYLLKNPFGFDNKFFNLtDEDARVLDPQVR--KFIQHA----Y 5329
Cdd:PTZ00050    8 GAESTWEALIAGKSGIrkltefpkflpdcipeqkALENLVAAMPCQIAAEVDQS-EFDPSDFAPTKResRATHFAmaaaR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5330 LALENSGyVKQKHEL---RCGVFAGaepSDYGRADDHDDAMRKL-----------FVMNM-NSYLASYASYCLDLKGEAV 5394
Cdd:PTZ00050   87 EALADAK-LDILSEKdqeRIGVNIG---SGIGSLADLTDEMKTLyekghsrvspyFIPKIlGNMAAGLVAIKHKLKGPSG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5395 SVYSACSTALVAVANAVKSIQSGSMDYALVGA--ASIAEVSgaLSGFDdQKKTMFSK-----SGVCRPFDKDSEGIVRGS 5467
Cdd:PTZ00050  163 SAVTACATGAHCIGEAFRWIKYGEADIMICGGteASITPVS--FAGFS-RMRALCTKynddpQRASRPFDKDRAGFVMGE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5468 GVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRAsfmAPNPAGQ--LKCMTDVLARFTNKEKERISFVECHATGTTL 5545
Cdd:PTZ00050  240 GAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHIT---APHPDGRgaRRCMENALKDGANININDVDYVNAHATSTPI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5546 GDTIEMNSLRTAY--SFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFsEFRDGMGQFFTVNGKKSTI 5623
Cdd:PTZ00050  317 GDKIELKAIKKVFgdSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINL-ENPDAECDLNLVQGKTAHP 395
                         410
                  ....*....|....*....
gi 392926054 5624 SQNSLISI-DSFGIGGTNV 5641
Cdd:PTZ00050  396 LQSIDAVLsTSFGFGGVNT 414
PRK05691 PRK05691
peptide synthase; Validated
6476-7494 3.28e-36

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 154.17  E-value: 3.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6476 IAEIWKETLGISI--LNDanpNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEFTKFVKNLtteKFAGNTND 6553
Cdd:PRK05691 1643 IAAIWREVLGLPRvgLRD---DFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARI---QAAGERNS 1716
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6554 KISYD------AIPLTNSQTQMFMLRQIDTTS-KYNL----IFKITISYETkfvwefLKYSLHSLIAYQPSYRTVFKSGN 6622
Cdd:PRK05691 1717 QGAIArvdrsqPVPLSYSQQRMWFLWQMEPDSpAYNVggmaRLSGVLDVDR------FEAALQALILRHETLRTTFPSVD 1790
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6623 S-PYQYICS---LTESFHDF------DKRCNLNNAISHEPNHLFEIGKSTPLR---VRVAEdcdnsRIH-IVFNQHHILT 6688
Cdd:PRK05691 1791 GvPVQQVAEdsgLRMDWQDFsalpadARQQRLQQLADSEAHQPFDLERGPLLRaclVKAAE-----REHyFVLTLHHIVT 1865
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6689 DGWSMTVLSDTVSSLYAAYRGETSFPSKTKQT----ISQVAMGTKSSGDIKEALEYYQN---TYHTII---------PYD 6752
Cdd:PRK05691 1866 EGWAMDIFARELGALYEAFLDDRESPLEPLPVqyldYSVWQRQWLESGERQRQLDYWKAqlgNEHPLLelpadrprpPVQ 1945
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6753 SETG-----NTSPSYV-RIsklipsKIWQKLVGLSkLYNTTMYNLALSVFcdavrSFTGQADILLAYAISGRNADNSE-L 6825
Cdd:PRK05691 1946 SHRGelyrfDLSPELAaRV------RAFNAQRGLT-LFMTMTATLAALLY-----RYSGQRDLRIGAPVANRIRPESEgL 2013
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6826 IGYFMNNALFKTSLPFEiLRLEEILNIVLNSLEKSRSFATIPFYQMVEQ---NRKLNEISLF--------FNFRQkldyp 6894
Cdd:PRK05691 2014 IGAFLNTQVLRCQLDGQ-MSVSELLEQVRQTVIEGQSHQDLPFDHLVEAlqpPRSAAYNPLFqvmcnvqrWEFQQ----- 2087
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6895 tvSMFGAKCEIEHLsLNNA----FDFSFTIDETP--TGSLITVD---FDKSKYLDTTVHmFANIFLKKLNNLRNMNTTIP 6965
Cdd:PRK05691 2088 --SRQLAGMTVEYL-VNDAratkFDLNLEVTDLDgrLGCCLTYSrdlFDEPRIARMAEH-WQNLLEALLGDPQQRLAELP 2163
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6966 ---------------IRRTDFPSTLFQKGLFTSWRLFTE--PALLLSTNTVSYSDLAEKIENISKDIQKQlqiakatSVR 7028
Cdd:PRK05691 2164 llaaaeqqqlldslaGEAGEARLDQTLHGLFAAQAARTPqaPALTFAGQTLSYAELDARANRLARALRER-------GVG 2236
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7029 EDELVGLDCKNSY---FALLACVFLGLPYAPIDPTWPEPRQLFV--KSKVSFTLEN-----------------CFSCNLK 7086
Cdd:PRK05691 2237 PQVRVGLALERSLemvVGLLAILKAGGAYVPLDPEYPLERLHYMieDSGIGLLLSDralfealgelpagvarwCLEDDAA 2316
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7087 LRNFNSRTQFGSI-------YSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSV 7159
Cdd:PRK05691 2317 ALAAYSDAPLPFLslpqhqaYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPL 2396
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7160 LNGGVLI--------SSEHSTTITDQlqkcQYAFLpaavfnGFTDKTMSRLESI-----ETLTI-----GGETVSDVVIE 7221
Cdd:PRK05691 2397 LCGARVVlraqgqwgAEEICQLIREQ----QVSIL------GFTPSYGSQLAQWlagqgEQLPVrmcitGGEALTGEHLQ 2466
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7222 TAMKKFPRLRTIQIYGPTETCIWSL------TNKCKVSTLNIGSALGDSLS---NETCTICNNSVRGNVQVKGISLARGY 7292
Cdd:PRK05691 2467 RIRQAFAPQLFFNAYGPTETVVMPLaclapeQLEEGAASVPIGRVVGARVAyilDADLALVPQGATGELYVGGAGLAQGY 2546
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7293 itsapHG-----------TPFSD----IYSTGDIVDSKLNSL-QYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVV 7356
Cdd:PRK05691 2547 -----HDrpgltaerfvaDPFAAdggrLYRTGDLVRLRADGLvEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVV 2621
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7357 LY----SNQMLIAFIVDQKSKL---LHDSLVKTLKN--RTQIPDYFVQ-----INKMPLNSSGKVD-KSLLLQAFENIRK 7421
Cdd:PRK05691 2622 LAldtpSGKQLAGYLVSAVAGQddeAQAALREALKAhlKQQLPDYMVPahlilLDSLPLTANGKLDrRALPAPDPELNRQ 2701
                        1130      1140      1150      1160      1170      1180      1190
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926054 7422 SYkreiVVMKNSLEEKVINVFSKILG-RNVAPTDKFESIGGNSLNAIQIAHRlAEELKIEIKAHEILQSNSLKT 7494
Cdd:PRK05691 2702 AY----QAPRSELEQQLAQIWREVLNvERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQT 2770
PRK12316 PRK12316
peptide synthase; Provisional
6990-7513 8.73e-35

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 149.34  E-value: 8.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLAEKIENISKDIqkqlqiaKATSVREDELVGLDCKNSY---FALLACVFLGLPYAPIDPTWPEPRq 7066
Cdd:PRK12316 2020 IAVVFGDQHLSYAELDSRANRLAHRL-------RARGVGPEVRVAIAAERSFelvVALLAVLKAGGAYVPLDPNYPAER- 2091
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7067 lfvkskVSFTLENC-------------------------FSCNLKLRNFNSRTQFGSI------YSIFTSGSTGVPKGVL 7115
Cdd:PRK12316 2092 ------LAYMLEDSgaallltqrhllerlplpagvarlpLDRDAEWADYPDTAPAVQLagenlaYVIYTSGSTGLPKGVA 2165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7116 MAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEHSTTITDQL------QKCQYAFLPAA 7189
Cdd:PRK12316 2166 VSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLydemerHGVTILDFPPV 2245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7190 VFNGFTDKTM--SRLESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNKCK------VSTLNIGSAL 7261
Cdd:PRK12316 2246 YLQQLAEHAErdGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRpqdpcgAAYVPIGRAL 2325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7262 GDS---LSNETCTICNNSVRGNVQVKGISLARGYI----------TSAPHGTPFSDIYSTGDIVDSKLN-SLQYIGRMDS 7327
Cdd:PRK12316 2326 GNRrayILDADLNLLAPGMAGELYLGGEGLARGYLnrpgltaerfVPDPFSASGERLYRTGDLARYRADgVVEYLGRIDH 2405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7328 QVKCKGVRINISEIEKELILCLGLLQIVVL----YSNQMLIAFIV-DQKSKLLHDSLVKTLKNRT---QIPDYFVQINKM 7399
Cdd:PRK12316 2406 QVKIRGFRIELGEIEARLQAHPAVREAVVVaqdgASGKQLVAYVVpDDAAEDLLAELRAWLAARLpayMVPAHWVVLERL 2485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7400 PLNSSGKVDKSLLLQAFENIRksyKREIVVMKNSLEEKVINVFSKILG-RNVAPTDKFESIGGNSLNAIQIAHRLAEELK 7478
Cdd:PRK12316 2486 PLNPNGKLDRKALPKPDVSQL---RQAYVAPQEGLEQRLAAIWQAVLKvEQVGLDDHFFELGGHSLLATQVVSRVRQDLG 2562
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 392926054 7479 IEIKAHEILQSNSLKTF---CNTLKNSVQKPISKVPNV 7513
Cdd:PRK12316 2563 LEVPLRILFERPTLAAFaasLESGQTSRAPVLQKVTRV 2600
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
7027-7412 1.68e-34

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 140.85  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7027 VREDELVGLDCKNSY---FALLACVFLGLPYAPIDPTWPEPRqlfvkskVSFTLENCfSCNLKLrnfnsrTQFGSI-YSI 7102
Cdd:cd17652    34 VGPERLVALALPRSAelvVAILAVLKAGAAYLPLDPAYPAER-------IAYMLADA-RPALLL------TTPDNLaYVI 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7103 FTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEHSTTI-----TDQ 7177
Cdd:cd17652   100 YTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLpgeplADL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7178 L--QKCQYAFLPAAVFNGFTDKTmsrLESIETLTIGGETVS-DVVIETAmkkfPRLRTIQIYGPTETCIWSLTNKCKV-- 7252
Cdd:cd17652   180 LreHRITHVTLPPAALAALPPDD---LPDLRTLVVAGEACPaELVDRWA----PGRRMINAYGPTETTVCATMAGPLPgg 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7253 STLNIGSAlgdsLSNETCTICNNSVR-------GNVQVKGISLARGYITSA----------PHGTPFSDIYSTGDIVDSK 7315
Cdd:cd17652   253 GVPPIGRP----VPGTRVYVLDARLRpvppgvpGELYIAGAGLARGYLNRPgltaerfvadPFGAPGSRMYRTGDLARWR 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7316 LN-SLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL-----YSNQMLIAFIV-DQKSKLLHDSLVKTLKNRT- 7387
Cdd:cd17652   329 ADgQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVvrddrPGDKRLVAYVVpAPGAAPTAAELRAHLAERLp 408
                         410       420
                  ....*....|....*....|....*..
gi 392926054 7388 --QIPDYFVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17652   409 gyMVPAAFVVLDALPLTPNGKLDRRAL 435
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
6998-7412 1.85e-34

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 141.66  E-value: 1.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6998 TVSYSDLAEKIENISKDIQkqlqiakATSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPRQLFV--KSK 7072
Cdd:cd12116    12 SLSYAELDERANRLAARLR-------ARGVGPGDRVAVYLPRSarlVAAMLAVLKAGAAYVPLDPDYPADRLRYIleDAE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7073 VSFTLENCFSCNLKLRNF---------------NSRTQF---GSIYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMF 7134
Cdd:cd12116    85 PALVLTDDALPDRLPAGLpvlllalaaaaaapaAPRTPVspdDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7135 RSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEhSTTITDQLQKCQY-------------AFLPAAVFNGFTDKtmsr 7201
Cdd:cd12116   165 GPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAP-RETQRDPEALARLieahsitvmqatpATWRMLLDAGWQGR---- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7202 lesiETLTI--GGETVSDVVIETAMKKFPRLrtIQIYGPTETCIWSLtnkckVSTLNIGSA---LGDSLSNETCTICNNS 7276
Cdd:cd12116   240 ----AGLTAlcGGEALPPDLAARLLSRVGSL--WNLYGPTETTIWST-----AARVTAAAGpipIGRPLANTQVYVLDAA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7277 VR-------GNVQVKGISLARGY-----ITSA-----PHGTPFSDIYSTGDIV----DSklnSLQYIGRMDSQVKCKGVR 7335
Cdd:cd12116   309 LRpvppgvpGELYIGGDGVAQGYlgrpaLTAErfvpdPFAGPGSRLYRTGDLVrrraDG---RLEYLGRADGQVKIRGHR 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7336 INISEIEKELILCLGLLQIVVLY----SNQMLIAFIVDQKSKLLH-DSLVKTLKNR---TQIPDYFVQINKMPLNSSGKV 7407
Cdd:cd12116   386 IELGEIEAALAAHPGVAQAAVVVredgGDRRLVAYVVLKAGAAPDaAALRAHLRATlpaYMVPSAFVRLDALPLTANGKL 465

                  ....*
gi 392926054 7408 DKSLL 7412
Cdd:cd12116   466 DRKAL 470
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
6991-7408 3.93e-34

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 140.23  E-value: 3.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6991 ALLLSTNTVSYSDLAEKIENISKDIQKQLQIakatsvREDELVGLDCKNSYF---ALLACVFLGLPYAPIDPTWPEPRQL 7067
Cdd:cd17648     5 AVVYGDKRLTYRELNERANRLAHYLLSVAEI------RPDDLVGLVLDKSELmiiAILAVWKAGAAYVPIDPSYPDERIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7068 FVKSKVSFTLENCFSCNLKlrnfnsrtqfgsiYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNI--RVLDSVK 7145
Cdd:cd17648    79 FILEDTGARVVITNSTDLA-------------YAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGdeAVLFFSN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7146 QVFDVSVSNIIGSVLNGGVLISSEHSTTITDQ-----LQKCQYAFLPA--AVFNGFTdktMSRLESIETLTIGGETVSDV 7218
Cdd:cd17648   146 YVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDrfyayINREKVTYLSGtpSVLQQYD---LARLPHLKRVDAAGEEFTAP 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7219 VIETAMKKFPRlRTIQIYGPTETCIWSLTNKCKVSTlNIGSALGDSLSNETCTICNNSVR-------GNVQVKGISLARG 7291
Cdd:cd17648   223 VFEKLRSRFAG-LIINAYGPTETTVTNHKRFFPGDQ-RFDKSLGRPVRNTKCYVLNDAMKrvpvgavGELYLGGDGVARG 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7292 YIT----------SAPHGTP-------FSDIYSTGDIVDSKLN-SLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQ 7353
Cdd:cd17648   301 YLNrpeltaerflPNPFQTEqerargrNARLYKTGDLVRWLPSgELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRE 380
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7354 IVVLY----------SNQMLIAFIVDQKSKLLHDSLVKTLknRTQIPDYFV-----QINKMPLNSSGKVD 7408
Cdd:cd17648   381 CAVVAkedasqaqsrIQKYLVGYYLPEPGHVPESDLLSFL--RAKLPRYMVparlvRLEGIPVTINGKLD 448
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
6990-7409 8.97e-34

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 138.92  E-value: 8.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLAEKIENISKDIQKQlqiakatSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPRQ 7066
Cdd:cd05945     8 PAVVEGGRTLTYRELKERADALAAALASL-------GLDAGDPVVVYGHKSpdaIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7067 LFVKSKVSFTLencfscnlkLRNFNSrtqfGSIYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQ 7146
Cdd:cd05945    81 REILDAAKPAL---------LIADGD----DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7147 VFDVSVSNIIGSVLNGGVLISSEHsttitDQLQKCQ--YAFLPAAVFNGFT-------------DKTMSRLESIETLTIG 7211
Cdd:cd05945   148 SFDLSVMDLYPALASGATLVPVPR-----DATADPKqlFRFLAEHGITVWVstpsfaamcllspTFTPESLPSLRHFLFC 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7212 GETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNK------CKVSTLNIGSALGDS---LSNETCTICNNSVRGNVQ 7282
Cdd:cd05945   223 GEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEvtpevlDGYDRLPIGYAKPGAklvILDEDGRPVPPGEKGELV 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7283 VKGISLARGYI------TSAPHGTPFSDIYSTGDIVD-SKLNSLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIV 7355
Cdd:cd05945   303 ISGPSVSKGYLnnpektAAAFFPDEGQRAYRTGDLVRlEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAV 382
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926054 7356 VL--YSN---QMLIAFIV------DQKSKLLHDSLVKTLkNRTQIPDYFVQINKMPLNSSGKVDK 7409
Cdd:cd05945   383 VVpkYKGekvTELIAFVVpkpgaeAGLTKAIKAELAERL-PPYMIPRRFVYLDELPLNANGKIDR 446
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
2133-2242 1.54e-33

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 127.68  E-value: 1.54e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2133 MSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS--PSLAIDYWEAHGTGTPLGDPIEFNTLSSIL------QNIII 2204
Cdd:pfam02801    1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAgvDPEDVDYVEAHGTGTPLGDPIEAEALKRVFgsgarkQPLAI 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 392926054  2205 GSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFH 2242
Cdd:pfam02801   81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
1976-2282 3.02e-32

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 131.60  E-value: 3.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1976 QQRLLLECVQECLENSG----VIETSNVGVFVGLMEKEY------QDMMESSSILAMLGSMAAVIAGRVNYIFGCYGPSV 2045
Cdd:cd00825    11 VSILGFEAAERAIADAGlsreYQKNPIVGVVVGTGGGSPrfqvfgADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2046 TIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDGCVVLMLE- 2124
Cdd:cd00825    91 DVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEe 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2125 ---LAKPNFHYMSTIQSVNVNHGGRSVSLTAP--NGVAHKMLLT-SVINQSPSlAIDYWEAHGTGTPLGDPIEFNTLSSI 2198
Cdd:cd00825   171 lehALARGAHIYAEIVGTAATIDGAGMGAFAPsaEGLARAAKEAlAVAGLTVW-DIDYLVAHGTGTPIGDVKELKLLRSE 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2199 LQ--NIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDInagsirLPIIGE--DSELVSAGISSFGV 2274
Cdd:cd00825   250 FGdkSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAG------LNIVTEttPRELRTALLNGFGL 323

                  ....*...
gi 392926054 2275 SGTNAAAI 2282
Cdd:cd00825   324 GGTNATLV 331
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
3177-3398 2.66e-31

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 131.80  E-value: 2.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3177 KNPLISFAWYQNV-----QQVSFVDSDSPITGNWLITGGLSGIGLEIGKFIANNGA-ENVILISRRQP---TAKALREFE 3247
Cdd:cd08954   188 KNVYKSGSWGDFRhllldLSILKTNYPINLGKSYLITGGSGGLGLEILKWLVKRGAvENIIILSRSGMkweLELLIREWK 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3248 HWKSKVHTIAADINDK---EKLIRELTKLN--VGITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFN 3322
Cdd:cd08954   268 SQNIKFHFVSVDVSDVsslEKAINLILNAPkiGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRC 347
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054 3323 YKIENFIMMSSFTAACGNEGQLNYGVSNAYLEYQVQRRRRQGKSGCAIQWGNWIDTGM-ATDENVRKFLANLGFLGQ 3398
Cdd:cd08954   348 WKLDYFVLFSSVSSIRGSAGQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGFvSRNESVDTLLGGQGLLPQ 424
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
6985-7412 4.57e-31

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 131.70  E-value: 4.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6985 RLFTEPALLLSTNTVSYSDLAEKIENISKDIqkqlqiaKATSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTW 7061
Cdd:cd17651     7 RTPDAPALVAEGRRLTYAELDRRANRLAHRL-------RARGVGPGDLVALCARRSaelVVALLAILKAGAAYVPLDPAY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7062 PEPRQLFV-----------KSKVSFTLENCFSCNLKLRNFNSRTQFGS-----------IYSIFTSGSTGVPKGVLMAEQ 7119
Cdd:cd17651    80 PAERLAFMladagpvlvltHPALAGELAVELVAVTLLDQPGAAAGADAepdpaldaddlAYVIYTSGSTGRPKGVVMPHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7120 SVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVL-ISSEH----STTITDQL--QKCQYAFLPAAVFN 7192
Cdd:cd17651   160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLvLPPEEvrtdPPALAAWLdeQRISRVFLPTVALR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7193 GFT---DKTMSRLESIETLTIGGETVsdvVIETAMKKF----PRLRTIQIYGPTETCI---WSLTNKCKV--STLNIGSA 7260
Cdd:cd17651   240 ALAehgRPLGVRLAALRYLLTGGEQL---VLTEDLREFcaglPGLRLHNHYGPTETHVvtaLSLPGDPAAwpAPPPIGRP 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7261 LGDS---LSNETCTICNNSVRGNVQVKGISLARGYItSAPHGT-------PFSD---IYSTGDIVDSKLN-SLQYIGRMD 7326
Cdd:cd17651   317 IDNTrvyVLDAALRPVPPGVPGELYIGGAGLARGYL-NRPELTaerfvpdPFVPgarMYRTGDLARWLPDgELEFLGRAD 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7327 SQVKCKGVRINISEIEKELILCLGLLQIVVL-----YSNQMLIAFIV-DQKSKLLHDSLVKTLknRTQIPDY-----FVQ 7395
Cdd:cd17651   396 DQVKIRGFRIELGEIEAALARHPGVREAVVLaredrPGEKRLVAYVVgDPEAPVDAAELRAAL--ATHLPEYmvpsaFVL 473
                         490
                  ....*....|....*..
gi 392926054 7396 INKMPLNSSGKVDKSLL 7412
Cdd:cd17651   474 LDALPLTPNGKLDRRAL 490
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
129-390 7.43e-30

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 126.73  E-value: 7.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  129 MATGNSAsvmcgrITYflNSRGAAVGIETACSSSLVAFHLARQAIQSGETKlALVCGA--------NHVGSRSFHSLYNS 200
Cdd:PTZ00050  146 MAAGLVA------IKH--KLKGPSGSAVTACATGAHCIGEAFRWIKYGEAD-IMICGGteasitpvSFAGFSRMRALCTK 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  201 HMVSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNP-----ISQYEVQLE 275
Cdd:PTZ00050  217 YNDDPQRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAH--HITAPHPdgrgaRRCMENALK 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  276 ALKNIDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSD----IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQL 351
Cdd:PTZ00050  295 DGANININDVDYVNAHATSTPIGDKIELKAIKKVFGDSgapkLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTI 374
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392926054  352 HLELPSEDLGEDKSMGFVNEEMELNRVAIS-SYGFGGTNA 390
Cdd:PTZ00050  375 NLENPDAECDLNLVQGKTAHPLQSIDAVLStSFGFGGVNT 414
Acyl_transf_1 pfam00698
Acyl transferase domain;
3647-3924 1.41e-29

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 123.35  E-value: 1.41e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3647 VLMLTGQGSQYPMMGRQLVENYEIFRTTLqsclKKCDEYL--QGDVSLWEILFNTDHyKLLQLTKHMQPIMFCFGYATAQ 3724
Cdd:pfam00698    1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVI----DRADEAFkpQYGFSVSDVLRNNPE-GTLDGTQFVQPALFAMQIALAA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3725 LWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIAGLGALLAVQREIADEVLRKF-KVSVATINSP 3803
Cdd:pfam00698   76 LLQSYGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPdDVVGAVVNSP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3804 KQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIqETHLVSLRQCLADIKFSAGRTPLVSNVTGQIIN--TFSE 3881
Cdd:pfam00698  156 RSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQM-DAIAPALLSALADIAPRTPRVPFISSTSIDPSDqrTLSA 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 392926054  3882 AYIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKR 3924
Cdd:pfam00698  235 EYWVRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALID 277
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
7043-7412 1.83e-29

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 125.89  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7043 ALLACVFLGLPYAPIDPTWPEPRqlfvkskVSFTLENCfSCNLKLrnfnsrTQFGSI-YSIFTSGSTGVPKGVLMAEQSV 7121
Cdd:cd12115    65 ALLAVLKAGAAYVPLDPAYPPER-------LRFILEDA-QARLVL------TDPDDLaYVIYTSGSTGRPKGVAIEHRNA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7122 SSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEHSTTITDQLQKCQYAFL---PAAVfngftdKT 7198
Cdd:cd12115   131 AAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAAEVTLIntvPSAA------AE 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7199 MSRLE----SIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSltNKCKVSTLNIGSA-LGDSLSNETCTIC 7273
Cdd:cd12115   205 LLRHDalpaSVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYS--TVAPVPPGASGEVsIGRPLANTQAYVL 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7274 NNS-------VRGNVQVKGISLARGYIT----------SAPHGtPFSDIYSTGDIVDSKLN-SLQYIGRMDSQVKCKGVR 7335
Cdd:cd12115   283 DRAlqpvplgVPGELYIGGAGVARGYLGrpgltaerflPDPFG-PGARLYRTGDLVRWRPDgLLEFLGRADNQVKVRGFR 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7336 INISEIEKELILCLGLLQIVVL-----YSNQMLIAFIV-DQKSKLLHDSLVKTLknRTQIPDY-----FVQINKMPLNSS 7404
Cdd:cd12115   362 IELGEIEAALRSIPGVREAVVVaigdaAGERRLVAYIVaEPGAAGLVEDLRRHL--GTRLPAYmvpsrFVRLDALPLTPN 439

                  ....*...
gi 392926054 7405 GKVDKSLL 7412
Cdd:cd12115   440 GKIDRSAL 447
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
6990-7622 2.31e-29

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 130.93  E-value: 2.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLAEKIeniskdiqkqlqIAKATSVRE-----DELVGLDCKNSYF---ALLACVFLGLPYAPIDPTW 7061
Cdd:PRK10252  475 PALADARYQFSYREMREQV------------VALANLLRErgvkpGDSVAVALPRSVFltlALHAIVEAGAAWLPLDTGY 542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7062 PE-----------PRQLFVKSKVSFTLENcfSCNLKLRNFNS-----------RTQFGSI-YSIFTSGSTGVPKGVLMAE 7118
Cdd:PRK10252  543 PDdrlkmmledarPSLLITTADQLPRFAD--VPDLTSLCYNAplapqgaaplqLSQPHHTaYIIFTSGSTGRPKGVMVGQ 620
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7119 QSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSN-----IIGSVLnggV---------------LISSEHSTT---IT 7175
Cdd:PRK10252  621 TAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEffwpfIAGAKL---VmaepeahrdplamqqFFAEYGVTTthfVP 697
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7176 DQLQkcqyAFLPAAVFNGFTDKTMSRLE---SIETLTIGgetvsdvvietAMKKFPRLRTIQI---YGPTETCIwsltnk 7249
Cdd:PRK10252  698 SMLA----AFVASLTPEGARQSCASLRQvfcSGEALPAD-----------LCREWQQLTGAPLhnlYGPTEAAV------ 756
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7250 cKVSTLnigSALGDSLSNETCT-------ICNNSVR--------------GNVQVKGISLARGYItSAPHGT-------P 7301
Cdd:PRK10252  757 -DVSWY---PAFGEELAAVRGSsvpigypVWNTGLRildarmrpvppgvaGDLYLTGIQLAQGYL-GRPDLTasrfiadP 831
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7302 FSD---IYSTGDIVDSKLN-SLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL--YSNQ---------MLIAF 7366
Cdd:PRK10252  832 FAPgerMYRTGDVARWLDDgAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHacVINQaaatggdarQLVGY 911
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7367 IVDQKSKLLHDSLVKTLKnRTQIPDY-----FVQINKMPLNSSGKVDKSLLLQAfENIRKSYKREIvvmKNSLEEKVINV 7441
Cdd:PRK10252  912 LVSQSGLPLDTSALQAQL-RERLPPHmvpvvLLQLDQLPLSANGKLDRKALPLP-ELKAQVPGRAP---KTGTETIIAAA 986
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7442 FSKILGRNVAPTD-KFESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLKTFCNTLKNSVQKPISKVPNVITKLREv 7520
Cdd:PRK10252  987 FSSLLGCDVVDADaDFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRRLGFGTILPLRE- 1065
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7521 pNSKFNIYLVHAIGGTIYPYYSFLQIFPKDISLYGIEFDLKYP----SNDLRELAHFYAEEIAAHAGNKRIFVMGHSMGG 7596
Cdd:PRK10252 1066 -GDGPTLFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGpmqtATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGG 1144
                         730       740
                  ....*....|....*....|....*.
gi 392926054 7597 IMSREIVAELKIWGYDIPFVMLFDSW 7622
Cdd:PRK10252 1145 TLAQGIAARLRARGEEVAFLGLLDTW 1170
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
5761-6023 3.78e-29

Acyl transferase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 121.36  E-value: 3.78e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5761 YLKNSAYRREVEYLCELASSFGIPSLEGILYPTKNFDHLIHaTQFAQIAIF-VQcMAIFKA-----IKnvfnPTCLIGHS 5834
Cdd:smart00827   17 YETEPVFREALDECDAALQPLLGWSLLDVLLGEDGAASLLD-TEVAQPALFaVQ-VALARLlrswgVR----PDAVVGHS 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5835 VGEYAAAVISGALKTEEALKLLIKRSELIGKT-EKARMLMV-------WNYEKQLPSHVHVSAIidaN--TKCVV-GPVE 5903
Cdd:smart00827   91 SGEIAAAYVAGVLSLEDAARLVAARGRLMQALpGGGAMLAVglseeevEPLLAGVPDRVSVAAV---NspSSVVLsGDED 167
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   5904 TIDNLEKYFINNHIKYRNIETKHGFHSKMFHCISKEFEFFCESFATKVPLIPMISSITGSEI---KIFDSKYCTMHLTNP 5980
Cdd:smart00827  168 AVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIdgaELDDADYWVRNLREP 247
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 392926054   5981 VNLELVVDHIMK-LDIDIIVEVGPTGVLSNLL---AKRNSKIVVVPT 6023
Cdd:smart00827  248 VRFADAVRALLAeGGVTVFLEVGPHPVLTGPIkqtLAAAGSAVVLPS 294
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
6990-7412 6.69e-29

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 124.34  E-value: 6.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLAEKIENISkdiqkqlQIAKATSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPRq 7066
Cdd:cd17643     4 VAVVDEDRRLTYGELDARANRLA-------RTLRAEGVGPGDRVALALPRSaelIVALLAILKAGGAYVPIDPAYPVER- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7067 lfvkskVSFTLENcfscnlklrnfnSRTQF------GSIYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRV 7140
Cdd:cd17643    76 ------IAFILAD------------SGPSLlltdpdDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVW 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7141 LDSVKQVFDVSVSNIIGSVLNGGVLISSEHST----------------TITDQLQKCQYAFLPAAVFNGftdktmSRLES 7204
Cdd:cd17643   138 TLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVarspedfarllrdegvTVLNQTPSAFYQLVEAADRDG------RDPLA 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7205 IETLTIGGETVSDVVIETAMKKFPRLRT--IQIYGPTETCIwsLTNKCKVSTLNI----GSALGDSLSNETCTICNNSVR 7278
Cdd:cd17643   212 LRYVIFGGEALEAAMLRPWAGRFGLDRPqlVNMYGITETTV--HVTFRPLDAADLpaaaASPIGRPLPGLRVYVLDADGR 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7279 -------GNVQVKGISLARGYI----------TSAPHGTPFSDIYSTGDIVDSKLN-SLQYIGRMDSQVKCKGVRINISE 7340
Cdd:cd17643   290 pvppgvvGELYVSGAGVARGYLgrpeltaerfVANPFGGPGSRMYRTGDLARRLPDgELEYLGRADEQVKIRGFRIELGE 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7341 IEKELILCLGLLQIVVLYS-----NQMLIAFIVDQKSK-LLHDSLVKTLKNRtqIPDY-----FVQINKMPLNSSGKVDK 7409
Cdd:cd17643   370 IEAALATHPSVRDAAVIVRedepgDTRLVAYVVADDGAaADIAELRALLKEL--LPDYmvparYVPLDALPLTVNGKLDR 447

                  ...
gi 392926054 7410 SLL 7412
Cdd:cd17643   448 AAL 450
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
6990-7412 1.97e-28

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 122.86  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLaekiENISKDIQKQLQiakATSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPRQ 7066
Cdd:cd17649     4 VALVFGDQSLSYAEL----DARANRLAHRLR---ALGVGPEVRVGIALERSlemVVALLAILKAGGAYVPLDPEYPAERL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7067 LF--VKSKVSFTLencfscnlklrnfnsrTQFGS--IYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLD 7142
Cdd:cd17649    77 RYmlEDSGAGLLL----------------THHPRqlAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7143 SVKQVFDVSVSNIIGSVLNGGVLI--------SSEHSTTITDQLQKCQYAFLPAAVFN---GFTDKTMSRLESIETLTIG 7211
Cdd:cd17649   141 FASFNFDGAHEQLLPPLICGACVVlrpdelwaSADELAEMVRELGVTVLDLPPAYLQQlaeEADRTGDGRPPSLRLYIFG 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7212 GETVSdvvIETAMKKFP-RLRTIQIYGPTETCIWSLTNKCKVST------LNIGSALGDS---LSNETCTICNNSVRGNV 7281
Cdd:cd17649   221 GEALS---PELLRRWLKaPVRLFNAYGPTEATVTPLVWKCEAGAaragasMPIGRPLGGRsayILDADLNPVPVGVTGEL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7282 QVKGISLARGYI----TSA------PHGTPFSDIYSTGDIVDSKLN-SLQYIGRMDSQVKCKGVRINISEIEKELILCLG 7350
Cdd:cd17649   298 YIGGEGLARGYLgrpeLTAerfvpdPFGAPGSRLYRTGDLARWRDDgVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPG 377
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926054 7351 LLQIVVL----YSNQMLIAFIVDQKSKLLHDsLVKTLKN--RTQIPDY-----FVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17649   378 VREAAVValdgAGGKQLVAYVVLRAAAAQPE-LRAQLRTalRASLPDYmvpahLVFLARLPLTPNGKLDRKAL 449
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
6989-7412 2.24e-28

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 122.96  E-value: 2.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6989 EPALLLSTNTVSYSDLAEKIENISKDIQKQlqiakatSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPR 7065
Cdd:cd17650     3 AIAVSDATRQLTYRELNERANQLARTLRGL-------GVAPGSVVGVCADRSldaIVGLLAVLKAGGAYVPIDPDYPAER 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7066 QLFV--KSKVSFTLencfscnlklrnfnsrTQFGSI-YSIFTSGSTGVPKGVLMAEQSVSSfMTSASKQ--CMFRSNIRV 7140
Cdd:cd17650    76 LQYMleDSGAKLLL----------------TQPEDLaYVIYTSGTTGKPKGVMVEHRNVAH-AAHAWRReyELDSFPVRL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7141 LDSVKQVFDVSVSNIIGSVLNGGVLISSEHST-----TITDQLQKCQ---YAFLPAAVFN--GFTDKTMSRLESIETLTI 7210
Cdd:cd17650   139 LQMASFSFDVFAGDFARSLLNGGTLVICPDEVkldpaALYDLILKSRitlMESTPALIRPvmAYVYRNGLDLSAMRLLIV 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7211 GGETVSDVVIETAMKKF-PRLRTIQIYGPTETCIWS------LTNKCKVSTLNIGSALGDS---LSNETCTICNNSVRGN 7280
Cdd:cd17650   219 GSDGCKAQDFKTLAARFgQGMRIINSYGVTEATIDStyyeegRDPLGDSANVPIGRPLPNTamyVLDERLQPQPVGVAGE 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7281 VQVKGISLARGYItSAPHGT-------PFS---DIYSTGDIVDSKLN-SLQYIGRMDSQVKCKGVRINISEIEKELILCL 7349
Cdd:cd17650   299 LYIGGAGVARGYL-NRPELTaerfvenPFApgeRMYRTGDLARWRADgNVELLGRVDHQVKIRGFRIELGEIESQLARHP 377
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054 7350 GLLQIVVLY-----SNQMLIAFIV-DQKSKL--LHDSLVKTLKNrTQIPDYFVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17650   378 AIDEAVVAVredkgGEARLCAYVVaAATLNTaeLRAFLAKELPS-YMIPSYYVQLDALPLTPNGKVDRRAL 447
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
126-599 2.33e-27

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 124.73  E-value: 2.33e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   126 DQYMA------TGNSASVMCGRITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGanhVGSRSFHSLYN 199
Cdd:TIGR02813  167 DQYIHweensfPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---VCTDNSPFMYM 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   200 SHMVSP----NGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPisqyEVQLE 275
Cdd:TIGR02813  244 SFSKTPafttNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRP----EGQAK 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   276 ALKNIDKD------SVQLVTCHGTGTKLGDQVELTAINRSFKSD------IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQ 343
Cdd:TIGR02813  320 ALKRAYDDagfaphTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALH 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   344 HGIIPNQLHLELPSEDLGEDKSMGFVNEEMEL---------NRVAISSYGFGGTNACAIIEK--PEKPSLVQKESYAESN 412
Cdd:TIGR02813  400 HKVLPPTINVDQPNPKLDIENSPFYLNTETRPwmqredgtpRRAGISSFGFGGTNFHMVLEEysPKHQRDDQYRQRAVAQ 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   413 VLFLSAKSHESLklqIEEYTQFMAQSDSAMEDILYTVNERKTKYDFRA-----AVFG---KDNEEIARKLQDgdySLTNL 484
Cdd:TIGR02813  480 TLLFTAANEKAL---VSSLKDWKNKLSAKADDQPYAFNALAVENTLRTiavalARLGfvaKNADELITMLEQ---AITQL 553
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   485 QESTFE---VEFGEGNEKLWLLRMLYEKNETFHSTVDKYCKLAE--TCGFPEARTAL------FFPFKLT-LTPLTYNVS 552
Cdd:TIGR02813  554 EAKSCEewqLPSGISYRKSALVVESGKVAALFAGQGSQYLNMGRelACNFPEVRQAAadmdsvFTQAGKGaLSPVLYPIP 633
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   553 RL-----------------------ISSMATFELLVQYNTLPNKLRGKGLGQIFCLAVAKVITFESAVQL 599
Cdd:TIGR02813  634 VFndesrkaqeealtntqhaqsaigTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMML 703
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
6991-7412 2.57e-27

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 120.27  E-value: 2.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6991 ALLLSTNTVSYSDLAEKIENISKDIQKQlqiakatSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPRQL 7067
Cdd:cd17656     6 AVVFENQKLTYRELNERSNQLARFLREK-------GVKKDSIVAIMMERSaemIVGILGILKAGGAFVPIDPEYPEERRI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7068 FV---------------KSKVSFTLENCF----------SCNLKLRNFNSRTqfgsIYSIFTSGSTGVPKGVLMAEQSVS 7122
Cdd:cd17656    79 YImldsgvrvvltqrhlKSKLSFNKSTILledpsisqedTSNIDYINNSDDL----LYIIYTSGTTGKPKGVQLEHKNMV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7123 SFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVL-ISSEHSTTITDQL------QKCQYAFLPAAVFNG-F 7194
Cdd:cd17656   155 NLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRDVEQLfdlvkrHNIEVVFLPVAFLKFiF 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7195 TDKTM--SRLESIETLTIGGEtvsDVVIETAMKKFPRLRTIQI---YGPTETCIwsltnkckVSTLNIGSA--------L 7261
Cdd:cd17656   235 SEREFinRFPTCVKHIITAGE---QLVITNEFKEMLHEHNVHLhnhYGPSETHV--------VTTYTINPEaeipelppI 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7262 GDSLSNETCTICNNS-------VRGNVQVKGISLARGY-----ITS---APHG-TPFSDIYSTGDIV----DSklnSLQY 7321
Cdd:cd17656   304 GKPISNTWIYILDQEqqlqpqgIVGELYISGASVARGYlnrqeLTAekfFPDPfDPNERMYRTGDLArylpDG---NIEF 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7322 IGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL-YSNQM----LIAFIVDQKSklLHDSLVKTlKNRTQIPDY---- 7392
Cdd:cd17656   381 LGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLdKADDKgekyLCAYFVMEQE--LNISQLRE-YLAKQLPEYmips 457
                         490       500
                  ....*....|....*....|.
gi 392926054 7393 -FVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17656   458 fFVPLDQLPLTPNGKVDRKAL 478
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
6990-7412 5.47e-27

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 118.43  E-value: 5.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLAEKIENISKdiqkqlqIAKATSVREDELVGLDCKNSY---FALLACVFLGLPYAPIDPTWPEPRQ 7066
Cdd:cd17645    15 VAVVDRGQSLTYKQLNEKANQLAR-------HLRGKGVKPDDQVGIMLDKSLdmiAAILGVLKAGGAYVPIDPDYPGERI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7067 LFV--KSKVSFTLENcfSCNLklrnfnsrtqfgsIYSIFTSGSTGVPKGVLMAEQSVSSF---------MTSASKQCMFR 7135
Cdd:cd17645    88 AYMlaDSSAKILLTN--PDDL-------------AYVIYTSGSTGLPKGVMIEHHNLVNLcewhrpyfgVTPADKSLVYA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7136 SnirvldsvkQVFDVSVSNIIGSVLNGGVL--ISSE--------------HSTTITdqlqkcqyaFLPAAVFNGFT--DK 7197
Cdd:cd17645   153 S---------FSFDASAWEIFPHLTAGAALhvVPSErrldldalndyfnqEGITIS---------FLPTGAAEQFMqlDN 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7198 TmsrleSIETLTIGGEtvsdvVIETAMKKFPRLrtIQIYGPTETCIWSLTNKCKVS--TLNIGSALGDS---LSNETCTI 7272
Cdd:cd17645   215 Q-----SLRVLLTGGD-----KLKKIERKGYKL--VNNYGPTENTVVATSFEIDKPyaNIPIGKPIDNTrvyILDEALQL 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7273 CNNSVRGNVQVKGISLARGYITSAPH------GTPF---SDIYSTGDIVD-SKLNSLQYIGRMDSQVKCKGVRINISEIE 7342
Cdd:cd17645   283 QPIGVAGELCIAGEGLARGYLNRPELtaekfiVHPFvpgERMYRTGDLAKfLPDGNIEFLGRLDQQVKIRGYRIEPGEIE 362
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 7343 KELiLCLGLLQIVVLYS------NQMLIAFIVdQKSKLLHDSLVKTLKNRT---QIPDYFVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17645   363 PFL-MNHPLIELAAVLAkedadgRKYLVAYVT-APEEIPHEELREWLKNDLpdyMIPTYFVHLKALPLTANGKVDRKAL 439
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
139-396 1.44e-26

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 116.67  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  139 CGRITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGA----NHVGSRSFHSL-------YNSHmvsPNG 207
Cdd:PRK07103  147 VGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGAlmdlSYWECQALRSLgamgsdrFADE---PEA 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  208 RLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPISQYEVQLEALK--NIDKDSV 285
Cdd:PRK07103  224 ACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDAN--RGPDPSLEGEMRVIRAALRraGLGPEDI 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  286 QLVTCHGTGTKLGDQVELTAINRSFKSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGiipnQLHlelPSEDLGE--D 363
Cdd:PRK07103  302 DYVNPHGTGSPLGDETELAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAG----FLH---PSRNLDEpiD 374
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392926054  364 KSMGFVNEEME--LNRVAIS-SYGFGGTNACAIIEK 396
Cdd:PRK07103  375 ERFRWVGSTAEsaRIRYALSlSFGFGGINTALVLER 410
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
3639-3962 3.11e-26

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 120.88  E-value: 3.11e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3639 LCQESSKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLQGDVS--LWEI-LFNTDHYK----LLQLTKHM 3711
Cdd:TIGR02813  574 LVVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSpvLYPIpVFNDESRKaqeeALTNTQHA 653
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3712 QPIMFCFGYATAQLWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAM-----ENIAGL--GALLAVQRE 3784
Cdd:TIGR02813  654 QSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMaaptgEADIGFmyAVILAVVGS 733
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3785 IADE--VLRKFK-VSVATINSPKQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQETHlVSLRQCLADIKFS 3861
Cdd:TIGR02813  734 PTVIanCIKDFEgVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTPLVAHAQ-KPFSAAIDKAKFN 812
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3862 AGRTPLVSNVTGQIINTFSEAY---IVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRIIQPTELSKHRIVQ 3938
Cdd:TIGR02813  813 TPLVPLYSNGTGKLHSNDAAAIkkaLKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNILQKLVENTLKDKENELCAISI 892
                          330       340
                   ....*....|....*....|....
gi 392926054  3939 TCKEKESDVDNLVQACLELEQSGL 3962
Cdd:TIGR02813  893 NPNPKGDSDMQLRQAAVQLAVLGL 916
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
6990-7417 1.49e-25

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 114.52  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLAEKIENISKdiqkQLQiakATSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPRq 7066
Cdd:COG0318    16 PALVFGGRRLTYAELDARARRLAA----ALR---ALGVGPGDRVALLLPNSpefVVAFLAALRAGAVVVPLNPRLTAEE- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7067 lfvkskVSFTLENCfscnlklrnfNSRTQFGSIYsIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQ 7146
Cdd:COG0318    88 ------LAYILEDS----------GARALVTALI-LYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7147 VFDVS-VSNIIGSVLNGG--VLISSEHSTTITDQLQ--KCQYAFLPAAVFNGFTDKTMSR---LESIETLTIGGETVSDV 7218
Cdd:COG0318   151 FHVFGlTVGLLAPLLAGAtlVLLPRFDPERVLELIEreRVTVLFGVPTMLARLLRHPEFArydLSSLRLVVSGGAPLPPE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7219 VIETAMKKF-PRLrtIQIYGPTETCIWSLTNKCKVSTLNIGSAlGDSLSNETCTICN-------NSVRGNVQVKGISLAR 7290
Cdd:COG0318   231 LLERFEERFgVRI--VEGYGLTETSPVVTVNPEDPGERRPGSV-GRPLPGVEVRIVDedgrelpPGEVGEIVVRGPNVMK 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7291 GYITsAPHGT--PFSD-IYSTGDIVdsKLNS---LQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL-----YS 7359
Cdd:COG0318   308 GYWN-DPEATaeAFRDgWLRTGDLG--RLDEdgyLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVgvpdeKW 384
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926054 7360 NQMLIAFIV-DQKSKLLHDSLVKTLKNR---TQIPDYFVQINKMPLNSSGKVDKSLLLQAFE 7417
Cdd:COG0318   385 GERVVAFVVlRPGAELDAEELRAFLRERlarYKVPRRVEFVDELPRTASGKIDRRALRERYA 446
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
4332-4628 2.04e-25

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 111.57  E-value: 2.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4332 LLITSLTSNTGVFIGCSANEFSHIVYAYgykdpraewSGGTSNSALAGRIAHWLKLKGPVVTLDTACSSSFYALSAACDA 4411
Cdd:cd00825    39 GVVVGTGGGSPRFQVFGADAMRAVGPYV---------VTKAMFPGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4412 LRTGQCEYAIVGTVNLVMHEM-TTDVLQNAKMTVDDFCKAFDVDANGYKRSEAVCSMLLTKSPNI-----DSVATITNYA 4485
Cdd:cd00825   110 VQNGKQDIVLAGGSEELAAPMdCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEELEHAlargaHIYAEIVGTA 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4486 TGHNGTSSSLFTPNGLSQLEVMQRATNPL----EKILEIQTHCTGTKLGDPIEINAI-SKLVSSACKIGSVKSNIGHTEG 4560
Cdd:cd00825   190 ATIDGAGMGAFAPSAEGLARAAKEALAVAgltvWDIDYLVAHGTGTPIGDVKELKLLrSEFGDKSPAVSATKAMTGNLSS 269
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4561 SSGLVSLCSSLMSFRSKYRVAQLHLK--CPTNSIKTnkmicrfIGEDADENNSILINNFGFTGSNCSVVL 4628
Cdd:cd00825   270 AAVVLAVDEAVLMLEHGFIPPSIHIEelDEAGLNIV-------TETTPRELRTALLNGFGLGGTNATLVL 332
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
1974-2281 2.33e-25

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 112.92  E-value: 2.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1974 DPQQRLLLECVQECLENSGV-----IETSNVGVFVG-----LMEKEYQDMMES------SSILAMLG--SMAAVIAGRVN 2035
Cdd:cd00828    70 DRTTLLALVATEEALADAGItdpyeVHPSEVGVVVGsgmggLRFLRRGGKLDAravnpyVSPKWMLSpnTVAGWVNILLL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2036 yifGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRtNGKMLS-----QHGMSLSFDSRAS 2110
Cdd:cd00828   150 ---SSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFA-NMGALStaeeePEEMSRPFDETRD 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2111 GYGRSDGCVVLMLE------------LAKPNFHYMSTIQSvnvnhgGRSVSLTAPnGVAHKMLLTSVINQSPSLAIDYWE 2178
Cdd:cd00828   226 GFVEAEGAGVLVLEraelalargapiYGRVAGTASTTDGA------GRSVPAGGK-GIARAIRTALAKAGLSLDDLDVIS 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2179 AHGTGTPLGDPIEFNTLSSILQNII----IGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTliHFHVLNKDINAGSIR 2254
Cdd:cd00828   299 AHGTSTPANDVAESRAIAEVAGALGaplpVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPP--TANLDDVDPDVEHLS 376
                         330       340
                  ....*....|....*....|....*....
gi 392926054 2255 LPIIGEDSEL--VSAGISSFGVSGTNAAA 2281
Cdd:cd00828   377 VVGLSRDLNLkvRAALVNAFGFGGSNAAL 405
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
7102-7408 5.19e-25

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 110.45  E-value: 5.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7102 IFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEHStTITDQLQ-- 7179
Cdd:cd04433     6 LYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF-DPEAALEli 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7180 ---KCQYAFLPAAVFNGFTDKTMSR---LESIETLTIGGETVSDVVIETAMKKFpRLRTIQIYGPTETCIWSLTN----- 7248
Cdd:cd04433    85 ereKVTILLGVPTLLARLLKAPESAgydLSSLRALVSGGAPLPPELLERFEEAP-GIKLVNGYGLTETGGTVATGppddd 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7249 KCKVSTlnIGSALGDS---LSNETCTICNNSVRGNVQVKGISLARGYiTSAPHGTPFSDI---YSTGDI--VDSKlNSLQ 7320
Cdd:cd04433   164 ARKPGS--VGRPVPGVevrIVDPDGGELPPGEIGELVVRGPSVMKGY-WNNPEATAAVDEdgwYRTGDLgrLDED-GYLY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7321 YIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL-----YSNQMLIAFIV-DQKSKLLHDSLVKTLKNRT---QIPD 7391
Cdd:cd04433   240 IVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVgvpdpEWGERVVAVVVlRPGADLDAEELRAHVRERLapyKVPR 319
                         330
                  ....*....|....*..
gi 392926054 7392 YFVQINKMPLNSSGKVD 7408
Cdd:cd04433   320 RVVFVDALPRTASGKID 336
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
5331-5645 9.59e-25

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 110.99  E-value: 9.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5331 ALENSGYVKQK--HELRCGVFAGA-----EPSDYGRADDHDDAMRKLF--VMNMNSYLASYASYCLDLK-GEAVSVYSAC 5400
Cdd:cd00828    83 ALADAGITDPYevHPSEVGVVVGSgmgglRFLRRGGKLDARAVNPYVSpkWMLSPNTVAGWVNILLLSShGPIKTPVGAC 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5401 STALVAVANAVKSIQSGSMDYALVGAASiAEVSGALSGFDDQK---KTMFSKSGVCRPFDKDSEGIVRGSGVGCFVLKRY 5477
Cdd:cd00828   163 ATALEALDLAVEAIRSGKADIVVVGGVE-DPLEEGLSGFANMGalsTAEEEPEEMSRPFDETRDGFVEAEGAGVLVLERA 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5478 SQALLDNDNVHFVIKDFAINNDGHSRaSFMAPNPaGQLKCMTDVLARFtNKEKERISFVECHATGTTLGDTIEMNSLRTA 5557
Cdd:cd00828   242 ELALARGAPIYGRVAGTASTTDGAGR-SVPAGGK-GIARAIRTALAKA-GLSLDDLDVISAHGTSTPANDVAESRAIAEV 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5558 YS-FKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSEFRDGMGQFFTVNGKKSTISQNSLISIDSFGI 5636
Cdd:cd00828   319 AGaLGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLKVRAALVNAFGF 398

                  ....*....
gi 392926054 5637 GGTNVHMVI 5645
Cdd:cd00828   399 GGSNAALVL 407
PRK05691 PRK05691
peptide synthase; Validated
7100-7481 1.33e-24

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 115.65  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7100 YSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGG-VLISSehsTTItdql 7178
Cdd:PRK05691 3873 YVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGArVEIVP---NAI---- 3945
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7179 qkcqyAFLPAAVFNGFTDKTMSRLESIETLTIG------------------GETVSDVVIETAMKKFPRLRTIQIYGPTE 7240
Cdd:PRK05691 3946 -----AHDPQGLLAHVQAQGITVLESVPSLIQGmlaedrqaldglrwmlptGEAMPPELARQWLQRYPQIGLVNAYGPAE 4020
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7241 tCIWSLT------NKCKVSTLNIGSALGDS---LSNETCTICNNSVRGNVQVKGISLARGYITSA----------PHGTP 7301
Cdd:PRK05691 4021 -CSDDVAffrvdlASTRGSYLPIGSPTDNNrlyLLDEALELVPLGAVGELCVAGTGVGRGYVGDPlrtalafvphPFGAP 4099
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7302 FSDIYSTGDIVDSKLNS-LQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVLY----SNQMLIAFIVDQKSKLLH 7376
Cdd:PRK05691 4100 GERLYRTGDLARRRSDGvLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVqegvNGKHLVGYLVPHQTVLAQ 4179
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7377 DSLVKTLKNRTQ--IPDYFVQ-----INKMPLNSSGKVDKSlLLQAFEnIRKSYKREIVVMKNSLEEKVINVFSKILG-R 7448
Cdd:PRK05691 4180 GALLERIKQRLRaeLPDYMVPlhwlwLDRLPLNANGKLDRK-ALPALD-IGQLQSQAYLAPRNELEQTLATIWADVLKvE 4257
                         410       420       430
                  ....*....|....*....|....*....|...
gi 392926054 7449 NVAPTDKFESIGGNSLNAIQIAHRLAEELKIEI 7481
Cdd:PRK05691 4258 RVGVHDNFFELGGHSLLATQIASRVQKALQRNV 4290
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
5259-5640 5.45e-24

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 108.94  E-value: 5.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5259 RVAVIGWSAEFSGSSNIHEYWENLMDGICSTGNNKYLlkNPFGFDNKF------FN----LTDEDARVLDPQVRKFIQHA 5328
Cdd:PRK08722    5 RVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHF--DTTNFSTRFaglvkdFNceeyMSKKDARKMDLFIQYGIAAG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5329 YLALENSGY-VKQKHELRCGVFAGAEPSDYGRADDHDDAM-----RKL---FV----MNMnsyLASYASYCLDLKGEAVS 5395
Cdd:PRK08722   83 IQALDDSGLeVTEENAHRIGVAIGSGIGGLGLIEAGHQALvekgpRKVspfFVpstiVNM---IAGNLSIMRGLRGPNIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5396 VYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGFDDQKKTMFSK---SGVCRPFDKDSEGIVRGSGVGCF 5472
Cdd:PRK08722  160 ISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNdepQKASRPWDKDRDGFVLGDGAGMM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5473 VLKRYSQALLDNDNVHFVIKDFAINNDGHSRASfmaPNPAGQLKCMT-DVLARFTNKEKERISFVECHATGTTLGDTIEM 5551
Cdd:PRK08722  240 VLEEYEHAKARGAKIYAELVGFGMSGDAYHMTS---PSEDGSGGALAmEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5552 NSLRTAY--SFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSEFRDGMGQFFtVNGKKSTISQNSLI 5629
Cdd:PRK08722  317 KGIKRALgeAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDL-VPHTARKVESMEYA 395
                         410
                  ....*....|.
gi 392926054 5630 SIDSFGIGGTN 5640
Cdd:PRK08722  396 ICNSFGFGGTN 406
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
1885-2355 6.16e-24

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 113.18  E-value: 6.16e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1885 RLAENPIGVMAAAcRLPGGVSSPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNP--VEGGNFITQdvTQFDPSF 1962
Cdd:TIGR02813    3 RLKDMPIAIVGMA-SIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADKsyCKRGGFLPE--VDFNPME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1963 FKISKSEAELIDPQQRLLLECVQECLENSGVIETSN---VGVFVG----------------------------------- 2004
Cdd:TIGR02813   80 FGLPPNILELTDISQLLSLVVAKEVLNDAGLPDGYDrdkIGITLGvgggqkqssslnarlqypvlkkvfkasgvededse 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2005 LMEKEYQDMM---ESSSILAMLGSmaaVIAGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGV--- 2078
Cdd:TIGR02813  160 MLIKKFQDQYihwEENSFPGSLGN---VISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVctd 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2079 ----NLILNEKGQGLRTNGKMlsqhgMSLSFDSRASGYGRSDGCVVLM-LELAKPNFHYM-STIQSVNVNHGGRSVSLTA 2152
Cdd:TIGR02813  237 nspfMYMSFSKTPAFTTNEDI-----QPFDIDSKGMMIGEGIGMMALKrLEDAERDGDRIyAVIKGVGASSDGKFKSIYA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2153 PNGVAHKMLLTSVINQS---PSlAIDYWEAHGTGTPLGDPIEFNTLSSI-------LQNIIIGSVKASLGHGEASAGTCG 2222
Cdd:TIGR02813  312 PRPEGQAKALKRAYDDAgfaPH-TCGLIEAHGTGTAAGDVAEFGGLVSVfsqdndqKQHIALGSVKSQIGHTKSTAGTAG 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  2223 LLKLFLMLTYQYVPTLIHFHVLNKDINA--------GSIRLPIIGEDSELVSAGISSFGVSGTNAAAIafndnnkLEPYI 2294
Cdd:TIGR02813  391 MIKAVLALHHKVLPPTINVDQPNPKLDIenspfylnTETRPWMQREDGTPRRAGISSFGFGGTNFHMV-------LEEYS 463
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926054  2295 PIH----KY------YILPISAKNQISLdnlekqilsVIPLTDVPicNIASALANNRS-HFtirNALIVSNS 2355
Cdd:TIGR02813  464 PKHqrddQYrqravaQTLLFTAANEKAL---------VSSLKDWK--NKLSAKADDQPyAF---NALAVENT 521
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
5374-5640 1.38e-23

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 107.51  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5374 NMnsyLASYASYCLDLKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGF----------DDQK 5443
Cdd:PRK08439  139 NM---LGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFaamkalstrnDDPK 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5444 KTmfsksgvCRPFDKDSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHsraSFMAPNPAGQLKCMTdvlA 5523
Cdd:PRK08439  216 KA-------SRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDAN---HITSPAPEGPLRAMK---A 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5524 RFTNKEKERISFVECHATGTTLGDTIEMNSLRTAYSFKNKLA-IGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVN 5602
Cdd:PRK08439  283 ALEMAGNPKIDYINAHGTSTPYNDKNETAALKELFGSKEKVPpVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTIN 362
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 392926054 5603 FsEFRDGMGQFFTVNGKKSTISQNSLISiDSFGIGGTN 5640
Cdd:PRK08439  363 Q-ETPDPECDLDYIPNVARKAELNVVMS-NSFGFGGTN 398
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
4300-4628 1.74e-23

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 107.24  E-value: 1.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4300 DPEYFGIRPSEAKFIDPQQRLLLCSVAKLLDS--LLITSLTSN-TGVFIGCSANEFSHIVYAY------GYKDPRAEWSG 4370
Cdd:cd00834    54 FDPEDYLDRKELRRMDRFAQFALAAAEEALADagLDPEELDPErIGVVIGSGIGGLATIEEAYrallekGPRRVSPFFVP 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4371 GTSNSALAGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVG----TVNLV-------MHEMTTDVLQN 4439
Cdd:cd00834   134 MALPNMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGgaeaLITPLtlagfaaLRALSTRNDDP 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4440 AKMtvddfCKAFDVDANGYKRSEAVCSMLLT-----KSPNIDSVATITNYAT---GHNGTSSSlftPNGLSQLEVMQRAT 4511
Cdd:cd00834   214 EKA-----SRPFDKDRDGFVLGEGAGVLVLEslehaKARGAKIYAEILGYGAssdAYHITAPD---PDGEGAARAMRAAL 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4512 N----PLEKILEIQTHCTGTKLGDPIEINAISKLVSSACK---IGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLH 4584
Cdd:cd00834   286 AdaglSPEDIDYINAHGTSTPLNDAAESKAIKRVFGEHAKkvpVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTIN 365
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 392926054 4585 LKCPTNSIKTNkmICRFIGEDADENNsILINNFGFTGSNCSVVL 4628
Cdd:cd00834   366 LEEPDPECDLD--YVPNEAREAPIRY-ALSNSFGFGGHNASLVF 406
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4479-4586 2.46e-23

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 98.41  E-value: 2.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4479 ATITNYATGHNGTSSSLFTPNGLSQLEVMQRA-----TNPlEKILEIQTHCTGTKLGDPIEINAISKL-----VSSACKI 4548
Cdd:pfam02801    2 AVIKGSAVNHDGRHNGLTAPNGEGQARAIRRAladagVDP-EDVDYVEAHGTGTPLGDPIEAEALKRVfgsgaRKQPLAI 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 392926054  4549 GSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLK 4586
Cdd:pfam02801   81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4299-4629 5.40e-23

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 105.95  E-value: 5.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4299 WDPEYFgIRPSEAKFIDPQQRLLLCSVAKLL-DS-LLITSLTSN-TGVFIGCSAN------EFSHIVYAYGYKDPRAEWS 4369
Cdd:COG0304    54 FDPEEY-LDRKELRRMDRFTQYALAAAREALaDAgLDLDEVDPDrTGVIIGSGIGgldtleEAYRALLEKGPRRVSPFFV 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4370 GGTSNSALAGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKMT---VDD 4446
Cdd:COG0304   133 PMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALstrNDD 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4447 F---CKAFDVDANGYKRSEAVCSMLLTkSP--------NIdsVATITNYAT---GHNGTSSSlftPNGLSQLEVMQRA-- 4510
Cdd:COG0304   213 PekaSRPFDKDRDGFVLGEGAGVLVLE-ELehakargaKI--YAEVVGYGAssdAYHITAPA---PDGEGAARAMRAAlk 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4511 ---TNPlEKILEIQTHCTGTKLGDPIEINAISKLVSSACK---IGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLH 4584
Cdd:COG0304   287 dagLSP-EDIDYINAHGTSTPLGDAAETKAIKRVFGDHAYkvpVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTIN 365
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 392926054 4585 LK-----CPTNSIkTNKMIcrfigedADENNSILINNFGFTGSNCSVVLK 4629
Cdd:COG0304   366 LEnpdpeCDLDYV-PNEAR-------EAKIDYALSNSFGFGGHNASLVFK 407
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
157-396 7.99e-23

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 105.20  E-value: 7.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  157 TACSSSLVAFHLARQAIQSGETKLALVCGANH----VGSRSFHSL-----YNShmvSPNGRLAAFDRSANGFVRAESFAV 227
Cdd:PRK08439  160 TACAAGTHAIIEAVKTIMLGGADKMLVVGAESaicpVGIGGFAAMkalstRND---DPKKASRPFDKDRDGFVMGEGAGA 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  228 AVLCSKQFAEENNLLIHCECVGsaFNSDGKTPSLTAPNPISQYEVQLEALKNIDKDSVQLVTCHGTGTKLGDQVELTAIN 307
Cdd:PRK08439  237 LVLEEYESAKKRGAKIYAEIIG--FGESGDANHITSPAPEGPLRAMKAALEMAGNPKIDYINAHGTSTPYNDKNETAALK 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  308 RSFKSDIR---VMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDkSMGFVNEEMELNRVAISSYG 384
Cdd:PRK08439  315 ELFGSKEKvppVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLD-YIPNVARKAELNVVMSNSFG 393
                         250
                  ....*....|..
gi 392926054  385 FGGTNACAIIEK 396
Cdd:PRK08439  394 FGGTNGVVIFKK 405
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
5377-5645 9.24e-23

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 101.37  E-value: 9.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5377 SYLASYASYCLD-----LKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAasiaevsgalsgfddqkktmfsksg 5451
Cdd:cd00327    40 SGEFSGAAGQLAyhlgiSGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGG------------------------- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5452 vcrpfdkdSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRASfmAPNPAGQLKCMTDVLARFTNKEKE 5531
Cdd:cd00327    95 --------SEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVP--AVSGEGLARAARKALEGAGLTPSD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5532 rISFVECHATGTTLGDTIEMNSLRTAYSfKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVnfSEFRDGMg 5611
Cdd:cd00327   165 -IDYVEAHGTGTPIGDAVELALGLDPDG-VRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTP--REPRTVL- 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 392926054 5612 qfftvngkkstisqnslisIDSFGIGGTNVHMVI 5645
Cdd:cd00327   240 -------------------LLGFGLGGTNAAVVL 254
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
6990-7409 1.47e-22

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 105.43  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLAEKieniSKDIQKQLqiaKATSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPR- 7065
Cdd:cd12114     4 TAVICGDGTLTYGELAER----ARRVAGAL---KAAGVRPGDLVAVTLPKGpeqVVAVLGILAAGAAYVPVDIDQPAARr 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7066 -QLFVKSKVSFTL---ENCFSCNLKLRNFNSRTQFGS---------------IYSIFTSGSTGVPKGVLMAEQSVSSFMT 7126
Cdd:cd12114    77 eAILADAGARLVLtdgPDAQLDVAVFDVLILDLDALAapappppvdvapddlAYVIFTSGSTGTPKGVMISHRAALNTIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7127 SASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGG-VLISSEHSTTITDQLQK--CQYA-----FLPAaVFNGFTD-- 7196
Cdd:cd12114   157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGAtLVLPDEARRRDPAHWAEliERHGvtlwnSVPA-LLEMLLDvl 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7197 -KTMSRLESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSltNKCKVSTLNIGSA---LGDSLSNETCTI 7272
Cdd:cd12114   236 eAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWS--IYHPIDEVPPDWRsipYGRPLANQRYRV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7273 CNNS-------VRGNVQVKGISLARGYI-----TSA---PHGTPfSDIYSTGDIVDSKLN-SLQYIGRMDSQVKCKGVRI 7336
Cdd:cd12114   314 LDPRgrdcpdwVPGELWIGGRGVALGYLgdpelTAArfvTHPDG-ERLYRTGDLGRYRPDgTLEFLGRRDGQVKVRGYRI 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7337 NISEIEKELILCLGLLQIVVLYSNQM----LIAFIVDQK------SKLLHDSLVKTLKNrTQIPDYFVQINKMPLNSSGK 7406
Cdd:cd12114   393 ELGEIEAALQAHPGVARAVVVVLGDPggkrLAAFVVPDNdgtpiaPDALRAFLAQTLPA-YMIPSRVIALEALPLTANGK 471

                  ...
gi 392926054 7407 VDK 7409
Cdd:cd12114   472 VDR 474
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
5375-5646 3.03e-22

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 103.57  E-value: 3.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5375 MNSYLASYASYCLDLKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAA----SIAEV-----SGALSG--FDDQK 5443
Cdd:PRK07103  142 MDTDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGAlmdlSYWECqalrsLGAMGSdrFADEP 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5444 KTmfsksgVCRPFDKDSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRAsfmAPNPAGQLKCMTDVLA 5523
Cdd:PRK07103  222 EA------ACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGP---DPSLEGEMRVIRAALR 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5524 RfTNKEKERISFVECHATGTTLGDTIEMNSLRTAYSfkNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNF 5603
Cdd:PRK07103  293 R-AGLGPEDIDYVNPHGTGSPLGDETELAALFASGL--AHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNL 369
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 392926054 5604 SEFRDGMGQFftVNGKKSTISQNSLISIdSFGIGGTNVHMVIE 5646
Cdd:PRK07103  370 DEPIDERFRW--VGSTAESARIRYALSL-SFGFGGINTALVLE 409
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
5315-5641 3.52e-22

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 103.54  E-value: 3.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5315 RVLDPQ----VRKFIQHAYLA----LENSGYVKQKHE--LRCGVFAGaepSDYGRADDHDDAMRKL-------------- 5370
Cdd:PRK06333   69 RYLDPKdqrkMDRFILFAMAAakeaLAQAGWDPDTLEdrERTATIIG---SGVGGFPAIAEAVRTLdsrgprrlspftip 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5371 -FVMNMNsylASYASYCLDLKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGA--ASIAEVS-------GALS-GF 5439
Cdd:PRK06333  146 sFLTNMA---AGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGteAAIDRVSlagfaaaRALStRF 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5440 DDqkktmfSKSGVCRPFDKDSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRASfMAPNPAGQLKCMT 5519
Cdd:PRK06333  223 ND------APEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTA-GPEDGEGARRAML 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5520 DVLaRFTNKEKERISFVECHATGTTLGDTIEMNSLRTAYSFKNKLAIGSCKANIGHAY-AASGLAALVKcAKMLQTGIIP 5598
Cdd:PRK06333  296 IAL-RQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVSGLAVSSTKSATGHLLgAAGGVEAIFT-ILALRDQIAP 373
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 392926054 5599 PQVNFSEFRDGMGQFFTVNGKKSTISQNSLISiDSFGIGGTNV 5641
Cdd:PRK06333  374 PTLNLENPDPAAEGLDVVANKARPMDMDYALS-NGFGFGGVNA 415
AMP-binding pfam00501
AMP-binding enzyme;
6997-7332 5.97e-22

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 102.78  E-value: 5.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6997 NTVSYSDLAEKIENISKdiqkQLQIAKatsVREDELVGLDCKNS---YFALLACVFLGLPYAPIDPTWPEPRQLFV---- 7069
Cdd:pfam00501   20 RRLTYRELDERANRLAA----GLRALG---VGKGDRVAILLPNSpewVVAFLACLKAGAVYVPLNPRLPAEELAYIleds 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7070 KSKVSFTLENCFSCNLK------------------------LRNFNSRTQFGSIYS------------IFTSGSTGVPKG 7113
Cdd:pfam00501   93 GAKVLITDDALKLEELLealgklevvklvlvldrdpvlkeePLPEEAKPADVPPPPppppdpddlayiIYTSGTTGKPKG 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7114 VLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQV----FDVSVS-NIIGSVLNGG--VLISSEHSTTITDQLQ-----KC 7181
Cdd:pfam00501  173 VMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTlplfHDFGLSlGLLGPLLAGAtvVLPPGFPALDPAALLElieryKV 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7182 QYAFLPAAVFNGFTDK---TMSRLESIETLTIGGETVSDVVIETAMKKFPRlRTIQIYGPTETCIWSLTN----KCKVST 7254
Cdd:pfam00501  253 TVLYGVPTLLNMLLEAgapKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVTTPlpldEDLRSL 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7255 LNIGSALGDS----LSNETCTICNNSVRGNVQVKGISLARGYitsapHGTP--------FSDIYSTGDIV----DSklnS 7318
Cdd:pfam00501  332 GSVGRPLPGTevkiVDDETGEPVPPGEPGELCVRGPGVMKGY-----LNDPeltaeafdEDGWYRTGDLGrrdeDG---Y 403
                          410
                   ....*....|....
gi 392926054  7319 LQYIGRMDSQVKCK 7332
Cdd:pfam00501  404 LEIVGRKKDQIKLG 417
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
5259-5644 1.37e-21

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 101.79  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5259 RVAVIGWSAEFSGSSNIHEYWENLMDGICSTGN----NKYLLKNPFGFDNKFFNLTD----EDARVLDpqvrKFIQHAYL 5330
Cdd:PRK07314    3 RVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPithfDTSDLAVKIAGEVKDFNPDDymsrKEARRMD----RFIQYGIA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5331 ----ALENSGY-VKQKHELRCGVFAGAEPSDYGRADDHDDAM-----RK---LFV-MNMNSYLASYASYCLDLKGEAVSV 5396
Cdd:PRK07314   79 aakqAVEDAGLeITEENADRIGVIIGSGIGGLETIEEQHITLlekgpRRvspFFVpMAIINMAAGHVSIRYGAKGPNHSI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5397 YSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGF----------DDQKKTmfsksgvCRPFDKDSEGIVRG 5466
Cdd:PRK07314  159 VTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFaaaralstrnDDPERA-------SRPFDKDRDGFVMG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5467 SGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSrasfM-APNPAGQ--LKCMTDVLARfTNKEKERISFVECHATGT 5543
Cdd:PRK07314  232 EGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYH----MtAPAPDGEgaARAMKLALKD-AGINPEDIDYINAHGTST 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5544 TLGDTIEMNSLRTAYSFKN-KLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSEFRDGMGQFFTVN-GKKS 5621
Cdd:PRK07314  307 PAGDKAETQAIKRVFGEHAyKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNeARER 386
                         410       420
                  ....*....|....*....|...
gi 392926054 5622 TIsqNSLISiDSFGIGGTNVHMV 5644
Cdd:PRK07314  387 KI--DYALS-NSFGFGGTNASLV 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
129-398 1.65e-21

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 101.40  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  129 MATGNsASVMCGrityflnSRGAAVGIETACSSSLVAFHLARQAIQSGETKlALVCGanhvGSRSfhslynshMVSPNGr 208
Cdd:PRK07314  140 MAAGH-VSIRYG-------AKGPNHSIVTACATGAHAIGDAARLIAYGDAD-VMVAG----GAEA--------AITPLG- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  209 LAAF--------------------DRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNP-- 266
Cdd:PRK07314  198 IAGFaaaralstrnddperasrpfDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAY--HMTAPAPdg 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  267 ISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTAINRSF---KSDIRVMSPKSSMGHGEGAAGLIGVLQSLYS 341
Cdd:PRK07314  276 EGAARAMKLALKDagINPEDIDYINAHGTSTPAGDKAETQAIKRVFgehAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLA 355
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054  342 MQHGIIPNQLHLELPSEDLGEDksmgFV-NE--EMELNrVAIS-SYGFGGTNACAIIEKPE 398
Cdd:PRK07314  356 IRDQVIPPTINLDNPDEECDLD----YVpNEarERKID-YALSnSFGFGGTNASLVFKRYE 411
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
5251-5640 1.86e-21

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 102.75  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5251 VSNKEDDT---RVAVIGWSAEFSGSSNIHEYWENLMDGI----------CSTGNNKyllknpFGFDNKFFNLTDEDARVL 5317
Cdd:PLN02787  119 ETKKKPLTkqrRVVVTGMGVVSPLGHDPDVFYNNLLEGVsgiseierfdCSQFPTR------IAGEIKSFSTDGWVAPKL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5318 DPQVRKFIqhAYL------ALENSG----YVKQKHELRCGVFAGaepSDYGRADDHDDAMRKLFV--MNMNSYLASYAS- 5384
Cdd:PLN02787  193 SKRMDKFM--LYLltagkkALADGGitedVMKELDKTKCGVLIG---SAMGGMKVFNDAIEALRIsyRKMNPFCVPFATt 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5385 ------YCLDL--KGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGF----------DDQKKTm 5446
Cdd:PLN02787  268 nmgsamLAMDLgwMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFvacralsqrnDDPTKA- 346
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5447 fsksgvCRPFDKDSEGIVRGSGVGCFVLKRYSQALLDNDNVH--FVIKDFAINndghsrASFMA---PNPAGQLKCMTDV 5521
Cdd:PLN02787  347 ------SRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYaeFLGGSFTCD------AYHMTephPEGAGVILCIEKA 414
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5522 LARfTNKEKERISFVECHATGTTLGDTIEMNSLRTAYSFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQV 5601
Cdd:PLN02787  415 LAQ-SGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNI 493
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 392926054 5602 NFSEFRDGMGQFFTVNGKKSTISQNSLISiDSFGIGGTN 5640
Cdd:PLN02787  494 NLENPESGVDTKVLVGPKKERLDIKVALS-NSFGFGGHN 531
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
7100-7412 3.19e-21

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 101.90  E-value: 3.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7100 YSIFTSGSTGVPKGVLMAEQSVSSF---MTSASkqcMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEHstTITD 7176
Cdd:PRK04813  147 YIIFTSGTTGKPKGVQISHDNLVSFtnwMLEDF---ALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPK--DMTA 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7177 QLqKCQYAFLPAAVFN----------------GFTDKTMSRLesiETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTE 7240
Cdd:PRK04813  222 NF-KQLFETLPQLPINvwvstpsfadmclldpSFNEEHLPNL---THFLFCGEELPHKTAKKLLERFPSATIYNTYGPTE 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7241 TCIwSLT---------NKCKvsTLNIGSALGDS---LSNETCTICNNSVRGNVQVKGISLARGYITSaPHGTP--FSDI- 7305
Cdd:PRK04813  298 ATV-AVTsieitdemlDQYK--RLPIGYAKPDSpllIIDEEGTKLPDGEQGEIVISGPSVSKGYLNN-PEKTAeaFFTFd 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7306 ----YSTGDIVDSKLNSLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVLYSN-----QMLIAFIVDQKSKLLH 7376
Cdd:PRK04813  374 gqpaYHTGDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNkdhkvQYLIAYVVPKEEDFER 453
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 392926054 7377 D-SLVKTLKNRTQ--IPDY-----FVQINKMPLNSSGKVD-KSLL 7412
Cdd:PRK04813  454 EfELTKAIKKELKerLMEYmiprkFIYRDSLPLTPNGKIDrKALI 498
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
5389-5644 4.50e-21

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 100.64  E-value: 4.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5389 LKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGA--ASIAEVSgaLSGFDDQK--KTMFSKS--GVCRPFDKDSEG 5462
Cdd:PLN02836  173 FQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGteSSIDALS--IAGFSRSRalSTKFNSCptEASRPFDCDRDG 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5463 IVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSrasFMAPNP--AGQLKCMTDVLARFTNKEKErISFVECHA 5540
Cdd:PLN02836  251 FVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHH---ITQPHEdgRGAVLAMTRALQQSGLHPNQ-VDYVNAHA 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5541 TGTTLGDTIEMNSLRTAY---SFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSE----FRDGmgqF 5613
Cdd:PLN02836  327 TSTPLGDAVEARAIKTVFsehATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERpdpiFDDG---F 403
                         250       260       270
                  ....*....|....*....|....*....|.
gi 392926054 5614 FTVNGKKSTISQNSLisIDSFGIGGTNVHMV 5644
Cdd:PLN02836  404 VPLTASKAMLIRAAL--SNSFGFGGTNASLL 432
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
6558-6980 5.33e-21

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 100.49  E-value: 5.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6558 DAIPLTNSQTQMFMLRQIDT-TSKYNLifKITISYETKFVWEFLKYSLHSLIAYQPSYRTVF--KSGNSPYQYIcsLTES 6634
Cdd:pfam00668    3 DEYPLSPAQKRMWFLEKLEPhSSAYNM--PAVLKLTGELDPERLEKALQELINRHDALRTVFirQENGEPVQVI--LEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6635 FHDF-----------DKRCNLNNAISHEPNHLFEIGKSTPLR---VRVAEDcdnsRIHIVFNQHHILTDGWSMTVLSDTV 6700
Cdd:pfam00668   79 PFELeiidisdlsesEEEEAIEAFIQRDLQSPFDLEKGPLFRaglFRIAEN----RHHLLLSMHHIIVDGVSLGILLRDL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6701 SSLYAAYRGETSFPSKTKQTISQVAMGTKS---SGDIKEALEYYQNT-----YHTIIPYDSETgNTSPSYV--RISKLIP 6770
Cdd:pfam00668  155 ADLYQQLLKGEPLPLPPKTPYKDYAEWLQQylqSEDYQKDAAYWLEQlegelPVLQLPKDYAR-PADRSFKgdRLSFTLD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6771 SKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRN-ADNSELIGYFMNnalfktSLPFEI-----L 6844
Cdd:pfam00668  234 EDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPsPDIERMVGMFVN------TLPLRIdpkggK 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6845 RLEEILNIVLNSLEKSRSFATIPFYQMVEQNR--------KLNEISLFF-NFRQKLDYPTVSMFGAKCEIEHLSLNNAFD 6915
Cdd:pfam00668  308 TFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRlprdlsrhPLFDPMFSFqNYLGQDSQEEEFQLSELDLSVSSVIEEEAK 387
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054  6916 FSFTIDETPTGSLITVDFD--KSKYLDTTVHMFANIFLKKLNNLRNmNTTIPIRRTDFPSTLFQKGL 6980
Cdd:pfam00668  388 YDLSLTASERGGGLTIKIDynTSLFDEETIERFAEHFKELLEQAIA-HPSQPLSELDLLSDAEKQKL 453
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
3206-3425 5.89e-21

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 100.71  E-value: 5.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTA---KALR-EFEHWKSKVHTIAADINDKEKLIRELTKLNVG--ITG 3279
Cdd:cd08952   234 LVTGGTGALGAHVARWLARRGAEHLVLTSRRGPDApgaAELVaELTALGARVTVAACDVADRDALAALLAALPAGhpLTA 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3280 IIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHfnYKIENFIMMSSFTAACGNEGQLNYGVSNAYLEYQVQR 3359
Cdd:cd08952   314 VVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHLDELTRD--RDLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAER 391
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054 3360 RRRQGKSGCAIQWGNWIDTGMATDEnVRKFLANLGFLGQHNKDALKYLRAcILTKPE-LIMVANIDW 3425
Cdd:cd08952   392 RRARGLPATSVAWGPWAGGGMAAGA-AAERLRRRGLRPMDPELALAALRR-ALDHDEtAVVVADVDW 456
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
5379-5644 8.21e-21

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 99.36  E-value: 8.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5379 LASYASYCL----DLKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASiaEVSGALSGFDDQKKTMFSK----- 5449
Cdd:PRK07967  137 MASTVSACLatpfKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGE--ELDWEMSCLFDAMGALSTKyndtp 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5450 SGVCRPFDKDSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSrasFMAPNPAGQLKCMTDVLARFTNKe 5529
Cdd:PRK07967  215 EKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYD---MVAPSGEGAVRCMQMALATVDTP- 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5530 kerISFVECHATGTTLGDTIEMNSLRTAysFKNKL-AIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSEFRD 5608
Cdd:PRK07967  291 ---IDYINTHGTSTPVGDVKELGAIREV--FGDKSpAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDP 365
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 392926054 5609 gmgQFFTVNGKKSTISQNSLISI--DSFGIGGTNVHMV 5644
Cdd:PRK07967  366 ---QAAGMPIVTETTDNAELTTVmsNSFGFGGTNATLV 400
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
5367-5644 1.43e-20

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 98.65  E-value: 1.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5367 MRKLFVMNMNSYLASYASYCLDL----KGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGFDDQ 5442
Cdd:PRK07910  134 LRAVSPLAVQMYMPNGPAAAVGLerhaKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQM 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5443 KKTMFSKS----GVCRPFDKDSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHsraSFMAPNPAGQL--K 5516
Cdd:PRK07910  214 RIVMSTNNddpaGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGF---HMVAPDPNGERagH 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5517 CMTDV--LARFTNKEkerISFVECHATGTTLGDTIEMNSLRTAYSfKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQT 5594
Cdd:PRK07910  291 AMTRAieLAGLTPGD---IDHVNAHATGTSVGDVAEGKAINNALG-GHRPAVYAPKSALGHSVGAVGAVESILTVLALRD 366
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 392926054 5595 GIIPPQVNFsEFRDGMGQFFTVNGKKSTISQNSLISiDSFGIGGTNVHMV 5644
Cdd:PRK07910  367 GVIPPTLNL-ENLDPEIDLDVVAGEPRPGNYRYAIN-NSFGFGGHNVALA 414
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
5399-5641 2.48e-20

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 97.43  E-value: 2.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5399 ACSTALVAVANAVKSIQSGSMDYALVGA--ASIAEVSgaLSGFddQKKTMFSKSGvCRPFDKDSEGIVRGSGVGCFVLKR 5476
Cdd:PRK05952  145 ACATGLWAIAQGVELIQTGQCQRVIAGAveAPITPLT--LAGF--QQMGALAKTG-AYPFDRQREGLVLGEGGAILVLES 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5477 YSQALLDNDNVHFVIKDFAINNDGHSRASfMAPNPAGQLKCMTDVLARfTNKEKERISFVECHATGTTLGDTIEMNSLRT 5556
Cdd:PRK05952  220 AELAQKRGAKIYGQILGFGLTCDAYHMSA-PEPDGKSAIAAIQQCLAR-SGLTPEDIDYIHAHGTATRLNDQREANLIQA 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5557 AysFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNF--SEFrdgmgQFFTVNGKKSTISQNSLISidSF 5634
Cdd:PRK05952  298 L--FPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLqePEF-----DLNFVRQAQQSPLQNVLCL--SF 368

                  ....*..
gi 392926054 5635 GIGGTNV 5641
Cdd:PRK05952  369 GFGGQNA 375
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
142-393 2.61e-20

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 98.15  E-value: 2.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  142 ITYFL-NSRGAAVGIE-----------TACSSSLVAFHLARQAIQSGETKLAlVCGA-----NHVG------SRSFHSLY 198
Cdd:PRK06333  144 IPSFLtNMAAGHVSIRygfkgplgapvTACAAGVQAIGDAARLIRSGEADVA-VCGGteaaiDRVSlagfaaARALSTRF 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  199 NShmvSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPISQ--YEVQLEA 276
Cdd:PRK06333  223 ND---APEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAY--HMTAGPEDGEgaRRAMLIA 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  277 LK--NIDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSD--IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLH 352
Cdd:PRK06333  298 LRqaGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVsgLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLN 377
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 392926054  353 LELPSEDLGEDKSMGFVNEEMELnRVAIS-SYGFGGTNACAI 393
Cdd:PRK06333  378 LENPDPAAEGLDVVANKARPMDM-DYALSnGFGFGGVNASIL 418
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
843-1201 5.09e-20

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 96.84  E-value: 5.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  843 KELWDTLLTSRltTGkISDIRKKQCEGDAGLEVGLLKqdismFDNSFFAIAKDEAEFLDPQHRLLLNAAYNALEKSGL-- 920
Cdd:cd00834    19 EEFWEALLAGR--SG-IRPITRFDASGFPSRIAGEVP-----DFDPEDYLDRKELRRMDRFAQFALAAAEEALADAGLdp 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  921 -------------TSIPDADLFLAisahsEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVA 987
Cdd:cd00834    91 eeldperigvvigSGIGGLATIEE-----AYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASGA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  988 TALEMAVKSIREGRKFAIVA--TSQLIQSSKW--LYSLKTLldhhSTNS---------FSVDGSGFCRSDGVGVIILKTA 1054
Cdd:cd00834   166 HAIGDAARLIRLGRADVVIAggAEALITPLTLagFAALRAL----STRNddpekasrpFDKDRDGFVLGEGAGVLVLESL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1055 EkgdSAV---IKI--------SSAKSHHcgavMT-P------VVSSISQLLEEAG----SFSYVEGHGTATSAGDSAESM 1112
Cdd:cd00834   242 E---HAKargAKIyaeilgygASSDAYH----ITaPdpdgegAARAMRAALADAGlspeDIDYINAHGTSTPLNDAAESK 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1113 AYQKLGSE----LIMSSVKAQFGHCEVASGLIQLmkVSSIG--KHGIIPsivhnilPSEHIRN-NENIRLPFV---AEEK 1182
Cdd:cd00834   315 AIKRVFGEhakkVPVSSTKSMTGHLLGAAGAVEA--IATLLalRDGVLP-------PTINLEEpDPECDLDYVpneAREA 385
                         410
                  ....*....|....*....
gi 392926054 1183 QIDRSAIVSFGITGTKTVV 1201
Cdd:cd00834   386 PIRYALSNSFGFGGHNASL 404
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
136-396 1.07e-19

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 95.84  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  136 SVMCGRITYFLNSRGAAVGIETACSSSL---------VAFHLARQAIQSGETKLALVCGANHVGSRSFHSLYNShmvSPN 206
Cdd:PRK08722  141 NMIAGNLSIMRGLRGPNIAISTACTTGLhnighaarmIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRND---EPQ 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  207 GRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGsaFNSDGKTPSLTAPNPI-SQYEVQLEAL---KNIDK 282
Cdd:PRK08722  218 KASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVG--FGMSGDAYHMTSPSEDgSGGALAMEAAmrdAGVTG 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  283 DSVQLVTCHGTGTKLGDQVELTAINRSF----KSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSE 358
Cdd:PRK08722  296 EQIGYVNAHGTSTPAGDVAEIKGIKRALgeagSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEE 375
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 392926054  359 DLGEDKSMGFVNEEMELNRVAISSYGFGGTNACAIIEK 396
Cdd:PRK08722  376 GLDIDLVPHTARKVESMEYAICNSFGFGGTNGSLIFKK 413
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
81-394 2.34e-19

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 91.74  E-value: 2.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   81 QQRMLMQGVIKGLENAGITlemaSEARVAVYTAawcydykdllppdQYMATGNSASVMCGRITYFLNSRGAAVGIETACS 160
Cdd:cd00327     7 ASELGFEAAEQAIADAGLS----KGPIVGVIVG-------------TTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  161 SSLVAFHLARQAIQSGETKLALVCGANHvgsrsfhslynshmvspngrlaafdrsangFVRAESFAVAVLCSKQFAEENN 240
Cdd:cd00327    70 TGLTALALAVQQVQNGKADIVLAGGSEE------------------------------FVFGDGAAAAVVESEEHALRRG 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  241 LLIHCECVGSAFNSDGKT----PSLTAPNPISQyevqlEALK--NIDKDSVQLVTCHGTGTKLGDQVELTAINRSFK-SD 313
Cdd:cd00327   120 AHPQAEIVSTAATFDGASmvpaVSGEGLARAAR-----KALEgaGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGvRS 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  314 IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQlhlelpsedlgedksmgfvneEMELNRVAISSYGFGGTNACAI 393
Cdd:cd00327   195 PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------------PREPRTVLLLGFGLGGTNAAVV 253

                  .
gi 392926054  394 I 394
Cdd:cd00327   254 L 254
FabD COG0331
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...
5800-6021 2.47e-19

Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440100 [Multi-domain]  Cd Length: 306  Bit Score: 92.88  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5800 IHATQFAQIAIFVQCMAIFKAIKN-VFNPTCLIGHSVGEYAAAVISGALKTEEALKLLIKRSELIGK---TEKARMLMVW 5875
Cdd:COG0331    55 LNLTENTQPAILAASVAAYRALEEeGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEavpAGPGGMAAVL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5876 NYE--------KQLPSHVHVS-AIIDANTKCVV-GPVETIDNLEKYFINNHIKyRNIETK-HG-FHSKMFHCISKEFEFF 5943
Cdd:COG0331   135 GLDdeevealcAEAAQGEVVEiANYNSPGQIVIsGEKEAVEAAAELAKEAGAK-RAVPLPvSGpFHTPLMAPAAEKLAEA 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5944 CESFATKVPLIPMISSITG------SEIKifdsKYCTMHLTNPVNLELVVDHIMKLDIDIIVEVGPTGVLSNLLAKRNSK 6017
Cdd:COG0331   214 LAAVTFADPKIPVVSNVDAapvtdpEEIR----ELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRIDPG 289

                  ....
gi 392926054 6018 IVVV 6021
Cdd:COG0331   290 VEVL 293
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
7100-7412 3.02e-19

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 95.42  E-value: 3.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7100 YSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSEH--------- 7170
Cdd:cd17646   142 YVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPgghrdpayl 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7171 STTITDQLQKCQYaFLPA--AVFNGftDKTMSRLESIETLTIGGETVSdvvIETAmKKFPRLRTIQI---YGPTETCIWS 7245
Cdd:cd17646   222 AALIREHGVTTCH-FVPSmlRVFLA--EPAAGSCASLRRVFCSGEALP---PELA-ARFLALPGAELhnlYGPTEAAIDV 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7246 LTNKCKVSTLNIGSALGDSLSNETCTICNNSVR-------GNVQVKGISLARGY-----ITSA---PHgtPF---SDIYS 7307
Cdd:cd17646   295 THWPVRGPAETPSVPIGRPVPNTRLYVLDDALRpvpvgvpGELYLGGVQLARGYlgrpaLTAErfvPD--PFgpgSRMYR 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7308 TGDIVDSKLN-SLQYIGRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL-----YSNQMLIAFIVDQKSKL------L 7375
Cdd:cd17646   373 TGDLARWRPDgALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVaraapAGAARLVGYVVPAAGAAgpdtaaL 452
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 392926054 7376 HDSLVKTLKnRTQIPDYFVQINKMPLNSSGKVDKSLL 7412
Cdd:cd17646   453 RAHLAERLP-EYMVPAAFVVLDALPLTANGKLDRAAL 488
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
892-1201 3.85e-19

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 94.01  E-value: 3.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  892 IAKDEAEFLDPQHRLLLNAAYNALEKSGLTsIPDAD-----LFLAISAHS------EYRALAEKHINELDERLWMGTVHS 960
Cdd:COG0304    60 LDRKELRRMDRFTQYALAAAREALADAGLD-LDEVDpdrtgVIIGSGIGGldtleeAYRALLEKGPRRVSPFFVPMMMPN 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  961 MVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIV-ATSQLIQSSKWL--YSLKTLldhhSTNS---- 1032
Cdd:COG0304   139 MAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRaDVMIAgGAEAAITPLGLAgfDALGAL----STRNddpe 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1033 -----FSVDGSGFCRSDGVGVIILKTAEkgdSAV---IKI--------SSAKSHHcgavMT-------PVVSSISQLLEE 1089
Cdd:COG0304   215 kasrpFDKDRDGFVLGEGAGVLVLEELE---HAKargAKIyaevvgygASSDAYH----ITapapdgeGAARAMRAALKD 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1090 AG----SFSYVEGHGTATSAGDSAESMAYQKL----GSELIMSSVKAQFGHCEVASGLIQLmkVSSIG--KHGIIPsivh 1159
Cdd:COG0304   288 AGlspeDIDYINAHGTSTPLGDAAETKAIKRVfgdhAYKVPVSSTKSMTGHLLGAAGAIEA--IASVLalRDGVIP---- 361
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 392926054 1160 nilPSEHIRN-NENIRLPFV---AEEKQIDRSAIVSFGITGTKTVV 1201
Cdd:COG0304   362 ---PTINLENpDPECDLDYVpneAREAKIDYALSNSFGFGGHNASL 404
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
212-390 5.54e-19

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 93.19  E-value: 5.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  212 FDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPisQYEVQLEALK------NIDKDSV 285
Cdd:PRK05952  199 FDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAY--HMSAPEP--DGKSAIAAIQqclarsGLTPEDI 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  286 QLVTCHGTGTKLGDQVELTAINRSFKSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLgedks 365
Cdd:PRK05952  275 DYIHAHGTATRLNDQREANLIQALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDL----- 349
                         170       180
                  ....*....|....*....|....*..
gi 392926054  366 mGFVNE--EMELNRVAISSYGFGGTNA 390
Cdd:PRK05952  350 -NFVRQaqQSPLQNVLCLSFGFGGQNA 375
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
1903-2282 1.14e-18

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 92.60  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1903 GVSSP-----SELWELLKIGKNASSRIPATRVPTRNTLISGSkygnpveggnfitqdVTQFDPSFFkISKSEAELIDPQQ 1977
Cdd:cd00834     9 GAVTPlgngvEEFWEALLAGRSGIRPITRFDASGFPSRIAGE---------------VPDFDPEDY-LDRKELRRMDRFA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1978 RLLLECVQECLENSGVIETS----NVGVFVG-------LMEKEYQDMMESSS-------ILAMLGSMAA-VIAGRvnyiF 2038
Cdd:cd00834    73 QFALAAAEEALADAGLDPEEldpeRIGVVIGsgigglaTIEEAYRALLEKGPrrvspffVPMALPNMAAgQVAIR----L 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2039 GCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKG----QGLRTngkmLSQHG-----MSLSFDSRA 2109
Cdd:cd00834   149 GLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTlagfAALRA----LSTRNddpekASRPFDKDR 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2110 SGYGRSDGCVVLMLE--------LAKPnfhymstiqsvnvnHG---GRSVS-----LTAPNGVAHKMLLtsVINQ----- 2168
Cdd:cd00834   225 DGFVLGEGAGVLVLEslehakarGAKI--------------YAeilGYGASsdayhITAPDPDGEGAAR--AMRAalada 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2169 --SPSlAIDYWEAHGTGTPLGDPIEFNTLSSIL----QNIIIGSVKASLGHGEASAG------TCgllklfLMLTYQYVP 2236
Cdd:cd00834   289 glSPE-DIDYINAHGTSTPLNDAAESKAIKRVFgehaKKVPVSSTKSMTGHLLGAAGaveaiaTL------LALRDGVLP 361
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 392926054 2237 TLIHFHVLNKDINagsirLPIIGEDSE--LVSAGIS-SFGVSGTNAAAI 2282
Cdd:cd00834   362 PTINLEEPDPECD-----LDYVPNEAReaPIRYALSnSFGFGGHNASLV 405
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
127-389 1.38e-18

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 92.49  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  127 QYMATGNSASVMCgrityflnSRGAAVGIET---ACSSSLVAFHLARQAIQSGETKLAlVCG-------ANHVGS----R 192
Cdd:PRK07910  144 MYMPNGPAAAVGL--------ERHAKAGVITpvsACASGSEAIAQAWRQIVLGEADIA-ICGgvetrieAVPIAGfaqmR 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  193 SFHSLYNShmvSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPISQ--- 269
Cdd:PRK07910  215 IVMSTNND---DPAGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGF--HMVAPDPNGErag 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  270 ----YEVQLEALKNIDkdsVQLVTCHGTGTKLGDQVELTAINRSFKSD-IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQH 344
Cdd:PRK07910  290 hamtRAIELAGLTPGD---IDHVNAHATGTSVGDVAEGKAINNALGGHrPAVYAPKSALGHSVGAVGAVESILTVLALRD 366
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392926054  345 GIIPNQLHLEL--PSEDL----GEDKSMGFvneemelnRVAIS-SYGFGGTN 389
Cdd:PRK07910  367 GVIPPTLNLENldPEIDLdvvaGEPRPGNY--------RYAINnSFGFGGHN 410
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
4315-4628 5.07e-18

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 90.58  E-value: 5.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4315 DPQQRLLLCSVAKLLDSLLITSLT----SNTGVFIGC---SANEFSHIVYAYGYKDPRAE---WSGgtSNSALAGRIA-H 4383
Cdd:cd00828    70 DRTTLLALVATEEALADAGITDPYevhpSEVGVVVGSgmgGLRFLRRGGKLDARAVNPYVspkWML--SPNTVAGWVNiL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4384 WLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTD-----VLQNAKMTVDDFCKAFDVDANGY 4458
Cdd:cd00828   148 LLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGfanmgALSTAEEEPEEMSRPFDETRDGF 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4459 KRSEAvCSMLLTKS---------PNIDSVATITNYATGHNGTSSSLFTPNGLSQLEVMQRATNPLEKILEIQTHCTGTKL 4529
Cdd:cd00828   228 VEAEG-AGVLVLERaelalargaPIYGRVAGTASTTDGAGRSVPAGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPA 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4530 GDPIEINAISKLVSSACK---IGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLKCPTNSIKTNkmicRFIGEDA 4606
Cdd:cd00828   307 NDVAESRAIAEVAGALGAplpVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHL----SVVGLSR 382
                         330       340
                  ....*....|....*....|....*
gi 392926054 4607 DENNSI---LINNFGFTGSNCSVVL 4628
Cdd:cd00828   383 DLNLKVraaLVNAFGFGGSNAALVL 407
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
146-394 5.30e-18

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 90.29  E-value: 5.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  146 LNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGANHVgSRS----FHSLynsHMVSPnGRLAAFDRSANGFVR 221
Cdd:PRK09185  147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSL-CRLtlngFNSL---ESLSP-QPCRPFSANRDGINI 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  222 AESFAVAVLcSKQFAEENNLLIHCEcvgsafNSDGKTPSltAPNP--------ISQyevqleALK--NIDKDSVQLVTCH 291
Cdd:PRK09185  222 GEAAAFFLL-EREDDAAVALLGVGE------SSDAHHMS--APHPeglgailaMQQ------ALAdaGLAPADIGYINLH 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  292 GTGTKLGDQVELTAINRSFKSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDksmGFVNE 371
Cdd:PRK09185  287 GTATPLNDAMESRAVAAVFGDGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPL---YLVEN 363
                         250       260
                  ....*....|....*....|....*
gi 392926054  372 EMELN-RVAIS-SYGFGGTNACAII 394
Cdd:PRK09185  364 AQALAiRYVLSnSFAFGGNNCSLIF 388
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
148-394 1.15e-17

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 89.69  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  148 SRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGANhvGSRSFHSLYNSHMVS--------PNGRLAAFDRSANGF 219
Cdd:PRK06501  164 TRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATD--GSVSAEALIRFSLLSalstqndpPEKASKPFSKDRDGF 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  220 VRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDG--KTPSLTAPNPIsqyevqLEALKN------IDKDSVQLVTCH 291
Cdd:PRK06501  242 VMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSfhRTRSSPDGSPA------IGAIRAaladagLTPEQIDYINAH 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  292 GTGTKLGDQVELTAINRSFK---SDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDkSMGF 368
Cdd:PRK06501  316 GTSTPENDKMEYLGLSAVFGerlASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLD-VVPN 394
                         250       260
                  ....*....|....*....|....*.
gi 392926054  369 VNEEMELNRVAISSYGFGGTNACAII 394
Cdd:PRK06501  395 VARDARVTAVLSNSFGFGGQNASLVL 420
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
4342-4628 2.02e-17

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 88.75  E-value: 2.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4342 GVFIGCS-----ANEFshivyAYGYKDPR-----AEWSGGTSN-SALAGRIAHWLKLKGPVVTLDTACSSSFYALSAACD 4410
Cdd:PRK09185   98 GVVLGTStsgilEGEL-----AYRRRDPAhgalpADYHYAQQElGSLADFLRAYLGLSGPAYTISTACSSSAKVFASARR 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4411 ALRTGQCEYAIVGTVnlvmhemttDVLqnAKMTVDDF----------CKAFDVDANGYKRSEAVCSMLLTKSPNiDSVAT 4480
Cdd:PRK09185  173 LLEAGLCDAAIVGGV---------DSL--CRLTLNGFnsleslspqpCRPFSANRDGINIGEAAAFFLLEREDD-AAVAL 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4481 ItnyatGHnGTSS-----SLFTPNGLSQLEVMQRATN-----PlEKILEIQTHCTGTKLGDPIEINAISKLVSSACKIGS 4550
Cdd:PRK09185  241 L-----GV-GESSdahhmSAPHPEGLGAILAMQQALAdaglaP-ADIGYINLHGTATPLNDAMESRAVAAVFGDGVPCSS 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4551 VKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLK-----CPTNSIKTNkmicrfigEDADENNSILINNFGFTGSNCS 4625
Cdd:PRK09185  314 TKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGqpdpaLPPLYLVEN--------AQALAIRYVLSNSFAFGGNNCS 385

                  ...
gi 392926054 4626 VVL 4628
Cdd:PRK09185  386 LIF 388
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
7527-7737 2.05e-17

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 91.30  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7527 IYLVHAIGGTIYPYYSFLQIFPKDISLYGIEF----DLKYPSNDLRELAHFYAEEIAAHAGNKRIFVMGHSMGGIMSREI 7602
Cdd:COG3319   604 LFCVHPAGGNVLCYRPLARALGPDRPVYGLQApgldGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEM 683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7603 VAELKIWGYDIPFVMLFDSWV--LRTNELDIENIKQFITYVFSGLP-----------DSEHRINRAIKLA---------- 7659
Cdd:COG3319   684 ARQLEAQGEEVALLVLLDSYApgALARLDEAELLAALLRDLARGVDlpldaeelralDPEERLARLLERLreaglpagld 763
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7660 ---------------QLLREYKTSVSDTKLYLFkskqlgdaafkkavRSDLNEELSRSMTCNGFDELSLQPVETYLIDGD 7724
Cdd:COG3319   764 aerlrrllrvfranlRALRRYRPRPYDGPVLLF--------------RAEEDPPGRADDPALGWRPLVAGGLEVHDVPGD 829
                         250
                  ....*....|...
gi 392926054 7725 HESCLKAENLKKV 7737
Cdd:COG3319   830 HFSMLREPHVAEL 842
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
151-390 3.32e-17

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 88.70  E-value: 3.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  151 AAVgieTACSSSLVAFHLARQAIQSGETKLaLVCGANH--------VG---SRSFHSLYNShmvSPNGRLAAFDRSANGF 219
Cdd:PLN02836  179 AAV---TACATGAHSIGDAFRMIQFGDADV-MVAGGTEssidalsiAGfsrSRALSTKFNS---CPTEASRPFDCDRDGF 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  220 VRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPISQYEV--QLEALKN--IDKDSVQLVTCHGTGT 295
Cdd:PLN02836  252 VIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAH--HITQPHEDGRGAVlaMTRALQQsgLHPNQVDYVNAHATST 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  296 KLGDQVELTAINRSFKSD-----IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPsEDLGEDKSMGFVN 370
Cdd:PLN02836  330 PLGDAVEARAIKTVFSEHatsggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERP-DPIFDDGFVPLTA 408
                         250       260
                  ....*....|....*....|.
gi 392926054  371 EEMELNRVAIS-SYGFGGTNA 390
Cdd:PLN02836  409 SKAMLIRAALSnSFGFGGTNA 429
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
1902-2282 3.59e-17

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 88.23  E-value: 3.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1902 GGVSS----PSELWELLKIGKNASSRIPATRVPTRNTLISGSkygnpveggnfitqdVTQFDPSFFkISKSEAELIDPQQ 1977
Cdd:COG0304     9 GAVSPlgngVEEFWEALLAGRSGIRPITRFDASGLPVRIAGE---------------VKDFDPEEY-LDRKELRRMDRFT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1978 RLLLECVQECLENSGV----IETSNVGVFVG-------LMEKEYQDMME-------SSSILAMLGSMAAviaGRVNYIFG 2039
Cdd:COG0304    73 QYALAAAREALADAGLdldeVDPDRTGVIIGsgiggldTLEEAYRALLEkgprrvsPFFVPMMMPNMAA---GHVSIRFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2040 CYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQ-----HGMSLSFDSRASGYGR 2114
Cdd:COG0304   150 LKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrnddpEKASRPFDKDRDGFVL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2115 SDGCVVLMLE------------LAKpnfhymstIQSVNVNHGGRSVSLTAPNGVAhkmlLTSVINQ-------SPSlAID 2175
Cdd:COG0304   230 GEGAGVLVLEelehakargakiYAE--------VVGYGASSDAYHITAPAPDGEG----AARAMRAalkdaglSPE-DID 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2176 YWEAHGTGTPLGDPIEFNTLSSIL----QNIIIGSVKASLGHgeaSAGTCGLLKL---FLMLTYQYVPTLIHFHvlNKDI 2248
Cdd:COG0304   297 YINAHGTSTPLGDAAETKAIKRVFgdhaYKVPVSSTKSMTGH---LLGAAGAIEAiasVLALRDGVIPPTINLE--NPDP 371
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 392926054 2249 NagsIRLPIIGEDS-EL-VSAGIS-SFGVSGTNAAAI 2282
Cdd:COG0304   372 E---CDLDYVPNEArEAkIDYALSnSFGFGGHNASLV 405
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
60-399 4.65e-17

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 88.88  E-value: 4.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   60 IEYFDDQYFGT---GESEAICMD----PQ--QRM------LMQGVIKGLENAGITLEMASE---ARVAVYTA-------- 113
Cdd:PLN02787  163 IERFDCSQFPTriaGEIKSFSTDgwvaPKlsKRMdkfmlyLLTAGKKALADGGITEDVMKEldkTKCGVLIGsamggmkv 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  114 ------AWCYDYKDLLPPDQYMATGNSASVMcgrITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN 187
Cdd:PLN02787  243 fndaieALRISYRKMNPFCVPFATTNMGSAM---LAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSD 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  188 ----------HVGSRSFhSLYNShmvSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGK 257
Cdd:PLN02787  320 aaiipiglggFVACRAL-SQRND---DPTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAY 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  258 tpSLTAPNP-----ISQYEVQLeALKNIDKDSVQLVTCHGTGTKLGDQVELTAINRSF--KSDIRVMSPKSSMGHGEGAA 330
Cdd:PLN02787  396 --HMTEPHPegagvILCIEKAL-AQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFgqNPELRVNSTKSMIGHLLGAA 472
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  331 GLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEMELnRVAIS-SYGFGGTNAcAIIEKPEK 399
Cdd:PLN02787  473 GAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDI-KVALSnSFGFGGHNS-SILFAPYK 540
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
3206-3409 5.06e-17

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 88.09  E-value: 5.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGK-FIANNGAENVILISRRQPTAK---ALR-EFEHWKSKVHTIAADINDKEKLIRELTKLNVG--IT 3278
Cdd:cd08956   197 LITGGTGTLGALLARhLVTEHGVRHLLLVSRRGPDAPgaaELVaELAALGAEVTVAACDVADRAALAALLAAVPADhpLT 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3279 GIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFNYKIenFIMMSSFTAACGNEGQLNYGVSNAYLEYQVQ 3358
Cdd:cd08956   277 AVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWHLHELTRDLDLAA--FVLFSSAAGVLGSPGQANYAAANAFLDALAQ 354
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392926054 3359 RRRRQGKSGCAIQWGNWIDTGMAT---DENVRKFLANLGFLGQHNKDALKYLRA 3409
Cdd:cd08956   355 HRRARGLPATSLAWGLWAQASGMTahlSDADLARLARGGLRPLSAEEGLALFDA 408
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
5388-5645 5.12e-17

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 87.74  E-value: 5.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5388 DLKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASiaEVSGALSG-FDdqkkTMFSKSG-------VCRPFDKD 5459
Cdd:PRK09116  152 GLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAE--ELCPTEAAvFD----TLFATSTrndapelTPRPFDAN 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5460 SEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGhsrASFMAPNPAGQLKCMTDVLaRFTNKEKERISFVECH 5539
Cdd:PRK09116  226 RDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDG---AHVTQPQAETMQIAMELAL-KDAGLAPEDIGYVNAH 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5540 ATGTTLGDTIEmnSLRTAYSFKNKLAIGSCKANIGHAYAASG-LAALVKCaKMLQTGIIPPQVNFSEFRDGMGQFFTVNG 5618
Cdd:PRK09116  302 GTATDRGDIAE--SQATAAVFGARMPISSLKSYFGHTLGACGaLEAWMSI-EMMNEGWFAPTLNLTQVDPACGALDYIMG 378
                         250       260
                  ....*....|....*....|....*..
gi 392926054 5619 KKSTISQNSLISiDSFGIGGTNVHMVI 5645
Cdd:PRK09116  379 EAREIDTEYVMS-NNFAFGGINTSLIF 404
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
6560-6954 6.24e-17

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 87.46  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6560 IPLTNSQTQMFMLRQIDTTSKynlIFKITISYETK--FVWEFLKYSLHSLIAYQPSYRTVFKSGN-SPYQYICSLTESF- 6635
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPS---AFNVAIEMFLTgsLDLARLKQALDAVMERHDVLRTRFCEEAgRYEQVVLDKTVRFr 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6636 -------HDFDKRCNLN---NAISHEPnhlFEIGKSTPLR---VRVAEDcdnsRIHIVFNQHHILTDGWSMTVLSDTVSS 6702
Cdd:cd19066    79 ieiidlrNLADPEARLLeliDQIQQTI---YDLERGPLVRvalFRLADE----RDVLVVAIHHIIVDGGSFQILFEDISS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6703 LY-AAYRGETSFPSKTKQTISQVAMGTK--SSGDIKEALEYYQNTYHTI-----IPYDSETGnTSPSY--VRISKLIPSK 6772
Cdd:cd19066   152 VYdAAERQKPTLPPPVGSYADYAAWLEKqlESEAAQADLAYWTSYLHGLppplpLPKAKRPS-QVASYevLTLEFFLRSE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6773 IWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LIGYFMNNALF--KTSLPFEilrLEEI 6849
Cdd:cd19066   231 ETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEdTIGLFLNLLPLriDTSPDAT---FPEL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6850 LNIVLNSLEKSRSFATIPFYQMVEQ--------NRKLNEISL-FFNFRQKLDYPTVSMFGAkcEIEHLSLNNAFDFSFTI 6920
Cdd:cd19066   308 LKRTKEQSREAIEHQRVPFIELVRHlgvvpeapKHPLFEPVFtFKNNQQQLGKTGGFIFTT--PVYTSSEGTVFDLDLEA 385
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 392926054 6921 DETPTGSL-ITVDFDKSKYLDTTVHMFANIFLKKL 6954
Cdd:cd19066   386 SEDPDGDLlLRLEYSRGVYDERTIDRFAERYMTAL 420
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
6560-6957 1.30e-16

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 86.55  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6560 IPLTNSQTQMFMLRQIDTTSK-YNLIFKITISyeTKFVWEFLKYSLHSLIAYQPSYRTVFKS-GNSPYQYICSLTESFHD 6637
Cdd:cd19538     2 IPLSFAQRRLWFLHQLEGPSAtYNIPLVIKLK--GKLDVQALQQALYDVVERHESLRTVFPEeDGVPYQLILEEDEATPK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6638 FD-KRCN---LNNAISHEPNHLFEIGKSTPLRVRVAEDCDNSRIhIVFNQHHILTDGWSMTVLSDTVSSLYAAY-RGET- 6711
Cdd:cd19538    80 LEiKEVDeeeLESEINEAVRYPFDLSEEPPFRATLFELGENEHV-LLLLLHHIAADGWSLAPLTRDLSKAYRARcKGEAp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6712 SFPSKTKQ----TISQVAMGTKSSGD---IKEALEYYQNTYHTI-----IPYDSETGNTSpSYV--RISKLIPSKIWQKL 6777
Cdd:cd19538   159 ELAPLPVQyadyALWQQELLGDESDPdslIARQLAYWKKQLAGLpdeieLPTDYPRPAES-SYEggTLTFEIDSELHQQL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6778 VGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LIGYFMN----------NALF--------KTS 6838
Cdd:cd19538   238 LQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEdLVGFFVNtlvlrtdtsgNPSFrellervkETN 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6839 L--------PFEilRLEEILNivlnsleKSRSFATIPFYQMVeqnrklneislfFNFrQKLDYPTVSMFGAKCEIEHLSL 6910
Cdd:cd19538   318 LeayehqdiPFE--RLVEALN-------PTRSRSRHPLFQIM------------LAL-QNTPQPSLDLPGLEAKLELRTV 375
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392926054 6911 NNA-FDFSFTI-----DETPTGSLITVDFDKSKYLDTTVHMFANIFLKKLNNL 6957
Cdd:cd19538   376 GSAkFDLTFELreqynDGTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESA 428
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
5371-5646 5.32e-16

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 83.62  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5371 FVMNMnsyLASYASYCLDLKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAASIAEVSGALSGFDDQK--KTMFS 5448
Cdd:PRK14691   65 FLVNL---AAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARalSTHFN 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5449 KS--GVCRPFDKDSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDGHSRASfMAPNPAGQLKCMTDVLaRFT 5526
Cdd:PRK14691  142 STpeKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTS-GAEDGDGAYRAMKIAL-RQA 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5527 NKEKERISFVECHATGTTLGDTIEMNSLRTAYSFKNKLAIGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFSEF 5606
Cdd:PRK14691  220 GITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENP 299
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392926054 5607 RDGMGQFFTVNGKKSTISQNSLISiDSFGIGGTNVHMVIE 5646
Cdd:PRK14691  300 DPAAKGLNIIAGNAQPHDMTYALS-NGFGFAGVNASILLK 338
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
4991-5131 7.38e-16

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 83.59  E-value: 7.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4991 VFHLAGIVNNSLHENVKRDSLDEMVSIKLQGAKNLmkcCDET-----SHFVFSSSIANVLGSYGQSNYAFSNGLVTSFLE 5065
Cdd:cd05274   233 VIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNL---HELTpdlplDFFVLFSSVAALLGGAGQAAYAAANAFLDALAA 309
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 5066 TSST---KSTIIHWGPWKDVGMLAqpeRREIVKQIESNGWKLLPNQDAISVFYTQFMETHEQIIVFDGD 5131
Cdd:cd05274   310 QRRRrglPATSVQWGAWAGGGMAA---AAALRARLARSGLGPLAPAEALEALEALLASDAPQAVVASVD 375
PLN02752 PLN02752
[acyl-carrier protein] S-malonyltransferase
3643-3925 1.31e-15

[acyl-carrier protein] S-malonyltransferase


Pssm-ID: 215401 [Multi-domain]  Cd Length: 343  Bit Score: 82.50  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3643 SSKCVLMLTGQGSQYPMMGRQLVENyeifrTTLQSCLKKCDEYLQGDvsLWEILFNTDHYKLlQLTKHMQPIMFCFGYAT 3722
Cdd:PLN02752   37 KPTTAFLFPGQGAQAVGMGKEAAEV-----PAAKALFDKASEILGYD--LLDVCVNGPKEKL-DSTVVSQPAIYVASLAA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3723 AQLWLSLGIVP------DYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIA-----------GLG--ALLAVQR 3783
Cdd:PLN02752  109 VEKLRARDGGQavidsvDVCAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAAdagpsgmvsviGLDsdKVQELCA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3784 EIADEVLRKFKVSVATINSPKQVVFAGTKSVLDAALAFVKGQG-KQATYVNQQYPFHSNLIqETHLVSLRQCLADIKFSA 3862
Cdd:PLN02752  189 AANEEVGEDDVVQIANYLCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFM-EPAVDALEAALAAVEIRT 267
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054 3863 GRTPLVSNVTGQIintFSEAYIVKHT-----VSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:PLN02752  268 PRIPVISNVDAQP---HSDPATIKKIlarqvTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGIVKRV 332
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
867-1206 1.40e-15

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 83.24  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  867 CEGDAGLEvgllkqDISMFDNSFFA--IAK-----DEAEFLDPQH--------RLLLNAAYNALEKSGLT-SIPDADLFl 930
Cdd:PRK08439   27 CNGECGIK------KITLFDASDFPvqIAGeitdfDPTEVMDPKEvkkadrfiQLGLKAAREAMKDAGFLpEELDAERF- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  931 AISAHSEYRALA--EKHINELDER--------LWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREG 1000
Cdd:PRK08439  100 GVSSASGIGGLPniEKNSIICFEKgprkispfFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1001 ---RKFAIVATSQL----IQSSKWLYSLKTLLDH--HSTNSFSVDGSGFCRSDGVGVIILKTAEKGDSAVIKI------- 1064
Cdd:PRK08439  180 gadKMLVVGAESAIcpvgIGGFAAMKALSTRNDDpkKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIyaeiigf 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1065 -SSAKSHHcgaVMTPVV----SSISQLLEEAGS--FSYVEGHGTATSAGDSAESMAYQKL--GSELI--MSSVKAQFGHC 1133
Cdd:PRK08439  260 gESGDANH---ITSPAPegplRAMKAALEMAGNpkIDYINAHGTSTPYNDKNETAALKELfgSKEKVppVSSTKGQIGHC 336
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054 1134 EVASGLIQlmKVSSIG--KHGIIPSIVHNILPsehirnNENIRL---PFVAEEKQIDRSAIVSFGITGTKTVVTTERV 1206
Cdd:PRK08439  337 LGAAGAIE--AVISIMamRDGILPPTINQETP------DPECDLdyiPNVARKAELNVVMSNSFGFGGTNGVVIFKKV 406
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
1976-2282 3.12e-15

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 79.41  E-value: 3.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1976 QQRLLLECVQECLENSGVIETSNVGVFVGLmekeyqdmmesssiLAMLGSMAAViAGRVNYIFG-CYGPSVTIDTACSSS 2054
Cdd:cd00327     7 ASELGFEAAEQAIADAGLSKGPIVGVIVGT--------------TGGSGEFSGA-AGQLAYHLGiSGGPAYSVNQACATG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2055 LVALEMAINALLDNRCSKVIVAGVNLIlnekgqglrtngkmlsqhgmslsfdsrasgyGRSDGCVVLML----ELAKPNF 2130
Cdd:cd00327    72 LTALALAVQQVQNGKADIVLAGGSEEF-------------------------------VFGDGAAAAVVeseeHALRRGA 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2131 HYMSTIQSVNVNHGGRS----VSLTAPNGVAHKMLltSVINQSPSlAIDYWEAHGTGTPLGDPIEFNTLSS--ILQNIII 2204
Cdd:cd00327   121 HPQAEIVSTAATFDGASmvpaVSGEGLARAARKAL--EGAGLTPS-DIDYVEAHGTGTPIGDAVELALGLDpdGVRSPAV 197
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054 2205 GSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLihfhvlnkdinagsirlpiigeDSELVSAGISSFGVSGTNAAAI 2282
Cdd:cd00327   198 SATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----------------------PREPRTVLLLGFGLGGTNAAVV 253
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
4991-5114 3.22e-15

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 81.56  E-value: 3.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4991 VFHLAGIVNNSLHENVKRDSLDEMVSIKLQGAKNLMKCCDETS--HFVFSSSIANVLGSYGQSNYAFSNGLVTSFLETSS 5068
Cdd:cd08955   233 VIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPldFFVLFSSVASLLGSPGQANYAAANAFLDALAHYRR 312
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 392926054 5069 TK---STIIHWGPWKDVGMLAQPERREivkQIESNGWKLLPNQDAISVF 5114
Cdd:cd08955   313 ARglpALSINWGPWAEVGMAASLARQA---RLEARGVGAISPAAGLQAL 358
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
129-399 3.93e-15

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 81.64  E-value: 3.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  129 MATGNSASVMcgriTYFlNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGA-----------NHVGSRSfhSL 197
Cdd:PRK07967  137 MASTVSACLA----TPF-KIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGeeldwemsclfDAMGALS--TK 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  198 YNShmvSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPISQYEVQLEAL 277
Cdd:PRK07967  210 YND---TPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGY--DMVAPSGEGAVRCMQMAL 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  278 KNIDKDsVQLVTCHGTGTKLGDQVELTAINRSFKSDIRVMSPKSSM-GHGEGAAGLIGVLQSLYSMQHGIIPNQLHLElp 356
Cdd:PRK07967  285 ATVDTP-IDYINTHGTSTPVGDVKELGAIREVFGDKSPAISATKSLtGHSLGAAGVQEAIYSLLMMEHGFIAPSANIE-- 361
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 392926054  357 seDLGED-KSMGFVNEEME---LNRVAISSYGFGGTNACAIIEKPEK 399
Cdd:PRK07967  362 --ELDPQaAGMPIVTETTDnaeLTTVMSNSFGFGGTNATLVFRRYKG 406
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
950-1197 4.26e-15

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 84.29  E-value: 4.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   950 DERLWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVATSQLIQSSKWLYSLKTLLDHHS 1029
Cdd:TIGR02813  173 EENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFT 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1030 TNS----FSVDGSGFCRSDGVGVIILK---TAEK-GDS--AVIK-ISSAKSHHCGAVMTP----VVSSISQLLEEAG--- 1091
Cdd:TIGR02813  253 TNEdiqpFDIDSKGMMIGEGIGMMALKrleDAERdGDRiyAVIKgVGASSDGKFKSIYAPrpegQAKALKRAYDDAGfap 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1092 -SFSYVEGHGTATSAGDSAESMAYQKLGSE-------LIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVH---- 1159
Cdd:TIGR02813  333 hTCGLIEAHGTGTAAGDVAEFGGLVSVFSQdndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINvdqp 412
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 392926054  1160 ----NILPSEHIRNNENirLPFVAEEKQIDRSA-IVSFGITGT 1197
Cdd:TIGR02813  413 npklDIENSPFYLNTET--RPWMQREDGTPRRAgISSFGFGGT 453
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
1083-1159 4.79e-15

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 74.91  E-value: 4.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1083 ISQLLEEAG----SFSYVEGHGTATSAGDSAESMAYQKL------GSELIMSSVKAQFGHCEVASGLIQLMKVSSIGKHG 1152
Cdd:pfam02801   30 IRRALADAGvdpeDVDYVEAHGTGTPLGDPIEAEALKRVfgsgarKQPLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHG 109

                   ....*..
gi 392926054  1153 IIPSIVH 1159
Cdd:pfam02801  110 VIPPTLN 116
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
6562-6789 4.95e-15

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 78.54  E-value: 4.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6562 LTNSQTQMFMLRQidTTSKYNLIFKITIsyETKFVWEFLKYSLHSLIAYQPSYRTVFKSGNS-PYQYI---CSLTESFHD 6637
Cdd:COG4908     1 LSPAQKRFLFLEP--GSNAYNIPAVLRL--EGPLDVEALERALRELVRRHPALRTRFVEEDGePVQRIdpdADLPLEVVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6638 F------DKRCNLNNAISHEPNHLFEIGKSTPLRVRVAEdCDNSRIHIVFNQHHILTDGWSMTVLSDTVSSLYAAYRG-- 6709
Cdd:COG4908    77 LsalpepEREAELEELVAEEASRPFDLARGPLLRAALIR-LGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEge 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6710 ETSFPSKTKQTISQVA--MGTKSSGDIKEALEYYQNTY-----HTIIPYD-SETGNTSPSYVRISKLIPSKIWQKLVGLS 6781
Cdd:COG4908   156 PPPLPELPIQYADYAAwqRAWLQSEALEKQLEYWRQQLagappVLELPTDrPRPAVQTFRGATLSFTLPAELTEALKALA 235

                  ....*...
gi 392926054 6782 KLYNTTMY 6789
Cdd:COG4908   236 KAHGATVN 243
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
142-394 6.81e-15

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 81.19  E-value: 6.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  142 ITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGANHV---GSRSFHSLY-----NSHmvsPNGRLAAFD 213
Cdd:PRK09116  147 VGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELcptEAAVFDTLFatstrNDA---PELTPRPFD 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  214 RSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPIS-QYEVQLeALK--NIDKDSVQLVTC 290
Cdd:PRK09116  224 ANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGA--HVTQPQAETmQIAMEL-ALKdaGLAPEDIGYVNA 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  291 HGTGTKLGDQVELTAINRSFKSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGE-DKSMGFV 369
Cdd:PRK09116  301 HGTATDRGDIAESQATAAVFGARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGAlDYIMGEA 380
                         250       260
                  ....*....|....*....|....*
gi 392926054  370 nEEMELNRVAISSYGFGGTNACAII 394
Cdd:PRK09116  381 -REIDTEYVMSNNFAFGGINTSLIF 404
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
3203-3381 7.05e-15

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 78.37  E-value: 7.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3203 GNWLITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALR-EFEHWKSKVHTIAADINDKE---KLIRELTKLNVGIT 3278
Cdd:COG0300     6 KTVLITGASSGIGRALARALAARGA-RVVLVARDAERLEALAaELRAAGARVEVVALDVTDPDavaALAEAVLARFGPID 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3279 GIIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN----FIMMSSFTAACGNEGQLNYGVSNAYL 3353
Cdd:COG0300    85 VLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGpVRLTRALLPLM---RARgrgrIVNVSSVAGLRGLPGMAAYAASKAAL 161
                         170       180       190
                  ....*....|....*....|....*....|..
gi 392926054 3354 E-YQVQRRRRQGKSG---CAIQWGnWIDTGMA 3381
Cdd:COG0300   162 EgFSESLRAELAPTGvrvTAVCPG-PVDTPFT 192
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
899-1159 1.90e-14

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 79.79  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  899 FLDPQHRLLLNAAYNALEKSGLTsipDADLF----LAISAHS---EYRALAekHINELDERLWMGTV-------HSMVAG 964
Cdd:cd00828    68 IVDRTTLLALVATEEALADAGIT---DPYEVhpseVGVVVGSgmgGLRFLR--RGGKLDARAVNPYVspkwmlsPNTVAG 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  965 RLAV-LMGIRGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQ--SSKWL-----YSLKTLLDHHSTNSFSV 1035
Cdd:cd00828   143 WVNIlLLSSHGPIKTPVGACATALEALDLAVEAIRSGKaDIVVVGGVEDPLeeGLSGFanmgaLSTAEEEPEEMSRPFDE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1036 DGSGFCRSDGVGVIILKT---AEKGDSAVIKISSAKSHHC-GAVM------TPVVSSISQLLEEAGSF----SYVEGHGT 1101
Cdd:cd00828   223 TRDGFVEAEGAGVLVLERaelALARGAPIYGRVAGTASTTdGAGRsvpaggKGIARAIRTALAKAGLSlddlDVISAHGT 302
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926054 1102 ATSAGDSAES----MAYQKLGSELIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVH 1159
Cdd:cd00828   303 STPANDVAESraiaEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTAN 364
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
883-1199 2.62e-14

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 79.35  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  883 SMFDNSFFAIAKDEAEFLdpqhRLLLNAAYNALEKSGLTSIPDAD-------LFLAISA----HSEYRALAEKHINELDE 951
Cdd:PTZ00050   61 SEFDPSDFAPTKRESRAT----HFAMAAAREALADAKLDILSEKDqerigvnIGSGIGSladlTDEMKTLYEKGHSRVSP 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  952 RLWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVA-------TSQLIQSSKWLYSLKTL 1024
Cdd:PTZ00050  137 YFIPKILGNMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICggteasiTPVSFAGFSRMRALCTK 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1025 L-DHHSTNS--FSVDGSGFCRSDGVGVIILKTAEKGDSAVIKI--------SSAKSHHcgaVMTP------VVSSISQLL 1087
Cdd:PTZ00050  217 YnDDPQRASrpFDKDRAGFVMGEGAGILVLEELEHALRRGAKIyaeirgygSSSDAHH---ITAPhpdgrgARRCMENAL 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1088 EEAGSFS-----YVEGHGTATSAGDSAESMAYQKL-----GSELIMSSVKAQFGHCEVASGLIQ-LMKVSSIgKHGIIPS 1156
Cdd:PTZ00050  294 KDGANINindvdYVNAHATSTPIGDKIELKAIKKVfgdsgAPKLYVSSTKGGLGHLLGAAGAVEsIVTILSL-YEQIIPP 372
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 392926054 1157 IVHNILPSEHIRNNENIRLpfVAEEKQIDRSAI-VSFGITGTKT 1199
Cdd:PTZ00050  373 TINLENPDAECDLNLVQGK--TAHPLQSIDAVLsTSFGFGGVNT 414
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
903-1197 3.54e-14

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 78.06  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  903 QHRLLLNAAYNALEKSGLTSIPDADLFLAISAHS--------EYRALAEKHINELDERLWMgtvHSMVAGRLAVLMGIRG 974
Cdd:cd00825    11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTgggsprfqVFGADAMRAVGPYVVTKAM---FPGASGQIATPLGIHG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  975 RAMIVDTTCSSVATALEMAVKSIR--EGRKFAIVATSQLIqsskWLYSL------KTLLDHHSTNSFSVDGSGFCRSDGV 1046
Cdd:cd00825    88 PAYDVSAACAGSLHALSLAADAVQngKQDIVLAGGSEELA----APMDCefdamgALSTPEKASRTFDAAADGFVFGDGA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1047 GVIILK----TAEKGDSAVIKISSAKSHHCGAVM-------TPVVSSISQLLEEAG----SFSYVEGHGTATSAGDSAES 1111
Cdd:cd00825   164 GALVVEelehALARGAHIYAEIVGTAATIDGAGMgafapsaEGLARAAKEALAVAGltvwDIDYLVAHGTGTPIGDVKEL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1112 MAYQKL--GSELIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPsivhnilPSEHIRNNENIRLPFVAEE--KQIDRS 1187
Cdd:cd00825   244 KLLRSEfgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIP-------PSIHIEELDEAGLNIVTETtpRELRTA 316
                         330
                  ....*....|
gi 392926054 1188 AIVSFGITGT 1197
Cdd:cd00825   317 LLNGFGLGGT 326
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
5390-5645 3.84e-14

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 78.90  E-value: 3.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5390 KGEAVSVYSACSTALVAVANAVKSIQSGSMDYAL-------VGAASIAEVS--GALSGFDD--QKKTmfsksgvcRPFDK 5458
Cdd:PRK06501  165 RGLPISLSTACASGATAIQLGVEAIRRGETDRALciatdgsVSAEALIRFSllSALSTQNDppEKAS--------KPFSK 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5459 DSEGIVRGSGVGCFVLKRYSQALLDNDNVHFVIKDFAINNDG-H-SRASfmaPNPAGQLKCMTDVLARfTNKEKERISFV 5536
Cdd:PRK06501  237 DRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSfHrTRSS---PDGSPAIGAIRAALAD-AGLTPEQIDYI 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5537 ECHATGTTLGDTIEMNSLRTAysFKNKLA---IGSCKANIGHAYAASGLAALVKCAKMLQTGIIPPQVNFsEFRDGMGQF 5613
Cdd:PRK06501  313 NAHGTSTPENDKMEYLGLSAV--FGERLAsipVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINY-DNPDPAIPL 389
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392926054 5614 FTVNGKKSTISQNSLISiDSFGIGGTNVHMVI 5645
Cdd:PRK06501  390 DVVPNVARDARVTAVLS-NSFGFGGQNASLVL 420
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
6561-6951 3.96e-14

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 78.65  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6561 PLTNSQTQM-FMLRQIDTTSKYNlifkITISYE-------TKfvwefLKYSLHSLIAYQPSYRTVF---KSGNSPYQYIc 6629
Cdd:cd19532     3 PMSFGQSRFwFLQQYLEDPTTFN----VTFSYRltgpldvAR-----LERAVRAVGQRHEALRTCFftdPEDGEPMQGV- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6630 sLTESFHDFDKRcnlnnAISHEP----------NHLFEIGKSTPLRVRVAEDCDNSrIHIVFNQHHILTDGWSMTVLsdt 6699
Cdd:cd19532    73 -LASSPLRLEHV-----QISDEAeveeeferlkNHVYDLESGETMRIVLLSLSPTE-HYLIFGYHHIAMDGVSFQIF--- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6700 VSSLYAAYRGETSfPSKTKQ----TISQVAMgtKSSGDIKEALEYYQNTYHTIIP------------------YDSETgn 6757
Cdd:cd19532   143 LRDLERAYNGQPL-LPPPLQyldfAARQRQD--YESGALDEDLAYWKSEFSTLPEplpllpfakvksrppltrYDTHT-- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6758 tspSYVRISKLIPSKIWQklvgLSKLYNTTMYNLALSVFcdAV---RsFTGQADILLAYAISGRN-ADNSELIGYFMN-- 6831
Cdd:cd19532   218 ---AERRLDAALAARIKE----ASRKLRVTPFHFYLAAL--QVllaR-LLDVDDICIGIADANRTdEDFMETIGFFLNll 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6832 ------------------------NALFKTSLPFEILrLEEiLNIvlnslekSRSFATIPFYQmveqnrklneisLFFNF 6887
Cdd:cd19532   288 plrfrrdpsqtfadvlketrdkayAALAHSRVPFDVL-LDE-LGV-------PRSATHSPLFQ------------VFINY 346
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054 6888 RQKldyPTVSMFGAKCEIEHLSL---NNAFDFSFTIDETPTGS-LITVDFDKSKYLDTTVHMFANIFL 6951
Cdd:cd19532   347 RQG---VAESRPFGDCELEGEEFedaRTPYDLSLDIIDNPDGDcLLTLKVQSSLYSEEDAELLLDSYV 411
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
4991-5081 4.13e-14

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 74.06  E-value: 4.13e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   4991 VFHLAGIVNNSLHENVKRDSLDEMVSIKLQGAKNLMKCCDET--SHFVFSSSIANVLGSYGQSNYAFSNglvtSFLE--- 5065
Cdd:smart00822   85 VIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLplDFFVLFSSIAGVLGSPGQANYAAAN----AFLDala 160
                            90       100
                    ....*....|....*....|
gi 392926054   5066 ----TSSTKSTIIHWGPWKD 5081
Cdd:smart00822  161 eyrrARGLPALSIAWGAWAE 180
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
4991-5131 4.61e-14

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 78.95  E-value: 4.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4991 VFHLAGIVNNSLHENVKRDSLDEMVSIKLQGAKNLMKCC--DETSHFVFSSSIANVLGSYGQSNYAFSNglvtSFLETSS 5068
Cdd:cd08953   292 VIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALadEPLDFFVLFSSVSAFFGGAGQADYAAAN----AFLDAFA 367
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926054 5069 ---------TKSTIIHWGPWKDVGMLAQPERREIVKQIesnGWKLLPNQDAISVFYtQFMETHE-QIIVFDGD 5131
Cdd:cd08953   368 aylrqrgpqGRVLSINWPAWREGGMAADLGARELLARA---GLLPIEPEEGLQALE-QALSSDLpQVLVSPGD 436
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
3206-3398 5.71e-14

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 75.59  E-value: 5.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:COG1028    10 LVTGGSSGIGRAIARALAAEGA-RVVITDRDAEALEAAaAELRAAGGRALAVAADVTDEAaveALVAAAVAAFGRLDILV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN----FIMMSSFTAACGNEGQLNYGVSNAYLEYQ 3356
Cdd:COG1028    89 NNAGITPPGPLEELTEEDWDRVLDVNLKGpFLLTRAALPHM---RERgggrIVNISSIAGLRGSPGQAAYAASKAAVVGL 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392926054 3357 VqrR---RRQGKSG---CAIQWGnWIDTGM----ATDENVRKFLAN---LGFLGQ 3398
Cdd:COG1028   166 T--RslaLELAPRGirvNAVAPG-PIDTPMtralLGAEEVREALAAripLGRLGT 217
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
3206-3351 6.00e-14

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 75.40  E-value: 6.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGIIH 3282
Cdd:cd05233     2 LVTGASSGIGRAIARRLAREGA-KVVLADRNEEALAELAAIEALGGNAVAVQADVSDEEdveALVEEALEEFGRLDILVN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926054 3283 SAGVLKDSKIERQNKESFNQVFtpKAN---GFHVLEEIEKHFnyKIENF---IMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:cd05233    81 NAGIARPGPLEELTDEDWDRVL--DVNltgVFLLTRAALPHM--KKQGGgriVNISSVAGLRPLPGQAAYAASKA 151
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
6565-6957 7.87e-14

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 77.73  E-value: 7.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6565 SQTQMFMLRQIdttskynliFKITISYETKFVWEF--------LKYSLHSLIAYQPSYRTVF--------------KSGN 6622
Cdd:cd19542     5 TPMQEGMLLSQ---------LRSPGLYFNHFVFDLdssvdverLRNAWRQLVQRHDILRTVFvessaegtflqvvlKSLD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6623 SPYQYICSLTESFHDFDKRCNLNNAISHEPNHLFEIGKSTPLRVRVaedcdnsRIHIvfnqHHILTDGWSMTVLsdtVSS 6702
Cdd:cd19542    76 PPIEEVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYL-------VLRI----SHALYDGVSLPII---LRD 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6703 LYAAYRGETSFPSKT-KQTISQVAmgtksSGDIKEALEYYQNTYHTIIPYD--SETGNTsPSYVRISKliPSKIWQKLVG 6779
Cdd:cd19542   142 LAAAYNGQLLPPAPPfSDYISYLQ-----SQSQEESLQYWRKYLQGASPCAfpSLSPKR-PAERSLSS--TRRSLAKLEA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6780 LSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNA--DNSE-LIGYFMNnalfktSLPFeILRLEEILNI--VL 6854
Cdd:cd19542   214 FCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLpvPGIDdIVGPCIN------TLPV-RVKLDPDWTVldLL 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6855 NSL----EKSRSFATIPFYQMVEQNRKLNEISLF---FNFRQKLDYPTVSMFGAKCeIEHLSLNNAFDFSFTID-ETPTG 6926
Cdd:cd19542   287 RQLqqqyLRSLPHQHLSLREIQRALGLWPSGTLFntlVSYQNFEASPESELSGSSV-FELSAAEDPTEYPVAVEvEPSGD 365
                         410       420       430
                  ....*....|....*....|....*....|..
gi 392926054 6927 SL-ITVDFDKSKYLDTTVHMFANIFLKKLNNL 6957
Cdd:cd19542   366 SLkVSLAYSTSVLSEEQAEELLEQFDDILEAL 397
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
4335-4629 2.41e-13

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 75.54  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4335 TSLTSNTGVFIGCSANEFSHIVYAYGYKDPRA--EWSGGTSNSAL----AGRIAHWLKLKGPVVTLDTACSSSFYALSAA 4408
Cdd:PRK14691   22 TEKQERTATIIGAGIGGFPAIAHAVRTSDSRGpkRLSPFTVPSFLvnlaAGHVSIKHHFKGPIGAPVTACAAGVQAIGDA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4409 CDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKMTVDDF-------CKAFDVDANGYKRSEAVCSMLLTK-----SPNID 4476
Cdd:PRK14691  102 VRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHFnstpekaSRPFDTARDGFVMGEGAGLLIIEElehalARGAK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4477 SVATITNYATGHNGTSSSLFTPNGLSQLEVM-----QRATNPlEKILEIQTHCTGTKLGDPIEINAISKLV--SSACKIG 4549
Cdd:PRK14691  182 PLAEIVGYGTSADAYHMTSGAEDGDGAYRAMkialrQAGITP-EQVQHLNAHATSTPVGDLGEINAIKHLFgeSNALAIT 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4550 SVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLKCPTNSIKTNKMICRfiGEDADENNSILINNFGFTGSNCSVVLK 4629
Cdd:PRK14691  261 STKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAG--NAQPHDMTYALSNGFGFAGVNASILLK 338
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
1901-2280 2.47e-13

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 76.27  E-value: 2.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1901 PGGVSsPSELWELLKIGKNASSRI---PATRVPTRNTLISGSKY--GNPVEGGNFITQDVtqFDPSFFKISKSEAELIdp 1975
Cdd:PTZ00050    4 PLGVG-AESTWEALIAGKSGIRKLtefPKFLPDCIPEQKALENLvaAMPCQIAAEVDQSE--FDPSDFAPTKRESRAT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1976 qqRLLLECVQECLENSGVIETSN-----VGVFVGLMEKEYQDMMESSS--------------ILAMLGSMAAviaGRVNY 2036
Cdd:PTZ00050   79 --HFAMAAAREALADAKLDILSEkdqerIGVNIGSGIGSLADLTDEMKtlyekghsrvspyfIPKILGNMAA---GLVAI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2037 IFGCYGPSVTIDTACSSSLVALEMAINALLDNRcSKVIVAG--------VNLILNEKGQGLRTNGKMLSQHGmSLSFDSR 2108
Cdd:PTZ00050  154 KHKLKGPSGSAVTACATGAHCIGEAFRWIKYGE-ADIMICGgteasitpVSFAGFSRMRALCTKYNDDPQRA-SRPFDKD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2109 ASGYGRSDGCVVLMLE----LAKPNFHYMSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS---PSLAIDYWEAHG 2181
Cdd:PTZ00050  232 RAGFVMGEGAGILVLEelehALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGaniNINDVDYVNAHA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2182 TGTPLGDPIEFNTLSSIL-----QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKD----INAGS 2252
Cdd:PTZ00050  312 TSTPIGDKIELKAIKKVFgdsgaPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAEcdlnLVQGK 391
                         410       420
                  ....*....|....*....|....*...
gi 392926054 2253 IRLPIIGEDSELVsagiSSFGVSGTNAA 2280
Cdd:PTZ00050  392 TAHPLQSIDAVLS----TSFGFGGVNTA 415
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
4378-4629 5.21e-13

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 75.50  E-value: 5.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4378 AGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVG-------TVNLV----MHEMTTDVLQNAKMTvdd 4446
Cdd:PTZ00050  148 AGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGgteasitPVSFAgfsrMRALCTKYNDDPQRA--- 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4447 fCKAFDVDANGYKRSEAVCSMLL-----TKSPNIDSVATITNYatghnGTSSSLF-----TPNGLSQLEVMQRATN---- 4512
Cdd:PTZ00050  225 -SRPFDKDRAGFVMGEGAGILVLeelehALRRGAKIYAEIRGY-----GSSSDAHhitapHPDGRGARRCMENALKdgan 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4513 -PLEKILEIQTHCTGTKLGDPIEINAISKLV----SSACKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYR--VAQLHL 4585
Cdd:PTZ00050  299 iNINDVDYVNAHATSTPIGDKIELKAIKKVFgdsgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIppTINLEN 378
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 392926054 4586 KCPT--NSIKTNKMICRFIGEDAdennsILINNFGFTGSNCSVVLK 4629
Cdd:PTZ00050  379 PDAEcdLNLVQGKTAHPLQSIDA-----VLSTSFGFGGVNTALLFT 419
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
144-396 2.26e-12

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 72.45  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  144 YFLNSRGAAVgieTACSSSLVAFHLARQAIQSGETKLALVCGANHV----------GSRSFHSLYNShmvSPNGRLAAFD 213
Cdd:PRK14691   79 HFKGPIGAPV---TACAAGVQAIGDAVRMIRNNEADVALCGGAEAVidtvslagfaAARALSTHFNS---TPEKASRPFD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  214 RSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCH 291
Cdd:PRK14691  153 TARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQagITPEQVQHLNAH 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  292 GTGTKLGDQVELTAINRSF--KSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFV 369
Cdd:PRK14691  233 ATSTPVGDLGEINAIKHLFgeSNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGN 312
                         250       260
                  ....*....|....*....|....*..
gi 392926054  370 NEEMELNRVAISSYGFGGTNACAIIEK 396
Cdd:PRK14691  313 AQPHDMTYALSNGFGFAGVNASILLKR 339
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
5351-5645 5.80e-12

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 71.80  E-value: 5.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5351 GAEPSDYGRAddhddamrklfVMNMNSyLASYASYCLDLKGEAVSVYSACSTALVAVANAVKSIQSGSMDYALVGAA-SI 5429
Cdd:PRK09185  123 GALPADYHYA-----------QQELGS-LADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVdSL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5430 AEVSgaLSGFDDQKKTmfsKSGVCRPFDKDSEGIVRGSGVGCFVLKRYSQA---LLdndnvhfvikdfainndGH---SR 5503
Cdd:PRK09185  191 CRLT--LNGFNSLESL---SPQPCRPFSANRDGINIGEAAAFFLLEREDDAavaLL-----------------GVgesSD 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5504 ASFM-APNPAGQ--LKCMTDVLARfTNKEKERISFVECHATGTTLGDTIE---MNSLrtaysFKNKLAIGSCKANIGHAY 5577
Cdd:PRK09185  249 AHHMsAPHPEGLgaILAMQQALAD-AGLAPADIGYINLHGTATPLNDAMEsraVAAV-----FGDGVPCSSTKGLTGHTL 322
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 5578 AASGLAALVKCAKMLQTGIIPPQVNFSEFRDGMG-QFFTVNGKKSTISqnsLISIDSFGIGGTNVHMVI 5645
Cdd:PRK09185  323 GAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPpLYLVENAQALAIR---YVLSNSFAFGGNNCSLIF 388
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
5803-6010 7.69e-12

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272922 [Multi-domain]  Cd Length: 290  Bit Score: 70.19  E-value: 7.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5803 TQFAQIAIFVQCMAIFKAIKN--VFNPTCLIGHSVGEYAAAVISGALKTEEALKLLIKRSELIGK--TEKARMLMV---W 5875
Cdd:TIGR00128   58 TQYTQPALYVVSAILYLKLKEqgGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEavPEGGGAMAAvigL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5876 NYE--KQLPSHVHVSAIIDANTKC---VV--GPVETIDNLEKYFINNHIKyRNI--ETKHGFHSKMFHCISKEFEFFCES 5946
Cdd:TIGR00128  138 DEEqlAQACEEATENDVDLANFNSpgqVVisGTKDGVEAAAALFKEMGAK-RAVplEVSGAFHSRFMKPAAEKFAETLEA 216
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5947 FATKVPLIPMISSIT------GSEIKifdsKYCTMHLTNPVNLELVVDHIMKLDIDIIVEVGPTGVLSNL 6010
Cdd:TIGR00128  217 CQFNDPTVPVISNVDakpytnGDRIK----EKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGL 282
PRK12316 PRK12316
peptide synthase; Provisional
6470-6829 1.46e-11

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 72.68  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6470 TSCEFVIAEIWKETLGISILNDANpNFFSLGGDSLSALQVVWKVQKKTDRiVDVNDLFDNPTLQEFTKFVK-----NLTT 6544
Cdd:PRK12316 3555 NELERRLAAIWADVLKLEQVGLTD-NFFELGGDSIISLQVVSRARQAGIR-FTPKDLFQHQTIQGLARVARvgggvAVDQ 3632
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6545 EKFAGNTndkisydaiPLTNSQTQMFMLrQIDTTSKYN--LIFKITISYETKFvwefLKYSLHSLIAYQPSYRTVFKSGN 6622
Cdd:PRK12316 3633 GPVSGET---------LLLPIQQQFFEE-PVPERHHWNqsLLLKPREALDAAA----LEAALQALVEHHDALRLRFVEDA 3698
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6623 SPYQYICSLTESFHDFDKRCNLNNA-----ISHEPNHLFEIGKSTPLRVRVAEDCDNSRiHIVFNQHHILTDGWSMTVLS 6697
Cdd:PRK12316 3699 GGWTAEHLPVELGGALLWRAELDDAeelerLGEEAQRSLDLADGPLLRALLATLADGSQ-RLLLVIHHLVVDGVSWRILL 3777
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6698 DTVSSLYAAY-RGE-TSFPSKTKQTISQVA--MGTKSSGDIKEALEYYQNTYHTI---IPYDSETGNTSPSYVR--ISKL 6768
Cdd:PRK12316 3778 EDLQQAYQQLlQGEaPRLPAKTSSFKAWAErlQEHARGEALKAELAYWQEQLQGVsseLPCDHPQGALQNRHAAsvQTRL 3857
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054 6769 IPSKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGR-----NADNSELIGYF 6829
Cdd:PRK12316 3858 DRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGRedlfaDIDLSRTVGWF 3923
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
6560-6957 1.85e-11

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 70.49  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6560 IPLTNSQTQMFMLRQIDT-TSKYN--LIFKITISYETkfvwEFLKYSLHSLIAYQPSYRTVFK--SGNSPYQYICSLT-- 6632
Cdd:cd19539     2 IPLSFAQERLWFIDQGEDgGPAYNipGAWRLTGPLDV----EALREALRDVVARHEALRTLLVrdDGGVPRQEILPPGpa 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6633 ------ESFHDFDKRCNLNNAISHEPNHLFEIGKSTPLRVRVAEDcDNSRIHIVFNQHHILTDGWSMTVLSDTVSSLYAA 6706
Cdd:cd19539    78 plevrdLSDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRF-DPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6707 YR-GETSFPSKTKQTISQVAM--GTKSSGD-IKEALEYYQNTYH--------TIIPYDSETGNTSPSYVRIsklIPSKIW 6774
Cdd:cd19539   157 RRkGPAAPLPELRQQYKEYAAwqREALAAPrAAELLDFWRRRLRgaeptalpTDRPRPAGFPYPGADLRFE---LDAELV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6775 QKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNSE-LIGYFMNNALFKTSLPfEILRLEEILNIV 6853
Cdd:cd19539   234 AALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFEsTVGFFVNLLPLRVDVS-DCATFRDLIARV 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6854 LNSLEKSRSFATIPFYQMVEQNRKLNEIS---LF---FNFRQKLD----------YPTVSMF--GAKceiehlslnnaFD 6915
Cdd:cd19539   313 RKALVDAQRHQELPFQQLVAELPVDRDAGrhpLVqivFQVTNAPAgelelagglsYTEGSDIpdGAK-----------FD 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 392926054 6916 FSFTIDETPTGSLITVDFDKSKYLDTTVHMFANIFLKKLNNL 6957
Cdd:cd19539   382 LNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQL 423
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
1544-1759 3.71e-11

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


Pssm-ID: 434191  Cd Length: 296  Bit Score: 68.17  E-value: 3.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1544 HVVDSKIVLPGATSIRL----VHQLNGKPT-VELSNIDFLN--KITPSEAPSV---VKIEEQDGLEKLVF---------- 1603
Cdd:pfam14765   33 HRVGGTVVLPGAGYLEMaleaARQLFGGSGaVALRDVSILKalVLPEDDPVEVqtsLTPEEDGADSWWEFeifsragggw 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1604 -------------GETDAISFKLTELQNFNPIPNERLNAEVHHtdnIYERFANSHLTYRNEFQMVDSLKY--TMGKGEVR 1668
Cdd:pfam14765  113 ewtlhatgtvrlaPGEPAAPVDLESLPARCAQPADPRSVSSAE---FYERLAARGLFYGPAFQGLRRIWRgdGEALAEAR 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  1669 FVSMKDLD--------ILIDGTLQAIVGCYFFENTNDNSPFVPFTIDQLSILNGDISQKQLHAVLKYDSSGN-FINGDAT 1739
Cdd:pfam14765  190 LPEAAAGGespyllhpALLDAALQLLGAALPAEAEHADQAYLPVGIERLRIYRSLPPGEPLWVHARLERRGGrTIVGDLT 269
                          250       260
                   ....*....|....*....|
gi 392926054  1740 VYDALGNIILHISNVTFKRL 1759
Cdd:pfam14765  270 LVDEDGRVVARIEGLRLRRV 289
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
889-1155 4.31e-11

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 69.27  E-value: 4.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  889 FFAIAKDEAEFldPQHRLLLNAAynaleksGLTSIPDADLFLAISAHSEYRALAEkhineldeRLWMGTVhsmvAGRLAV 968
Cdd:PRK06501  102 FLAAPPVELEW--PARFALAAAV-------GDNDAPSYDRLLRAARGGRFDALHE--------RFQFGSI----ADRLAD 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  969 LMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFA--IVAT------SQLIQSSkWLYSLKTLLD--HHSTNSFSVDGS 1038
Cdd:PRK06501  161 RFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRalCIATdgsvsaEALIRFS-LLSALSTQNDppEKASKPFSKDRD 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1039 GFCRSDGVGVIILKTAEkgdSAV---IKI--------SSAKSHHC------GAvmtPVVSSISQLLEEAG----SFSYVE 1097
Cdd:PRK06501  240 GFVMAEGAGALVLESLE---SAVargAKIlgivagcgEKADSFHRtrsspdGS---PAIGAIRAALADAGltpeQIDYIN 313
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926054 1098 GHGTATSAGDSAESMAYQKLGSELI----MSSVKAQFGHCEVASGLIQlmKVSSIG--KHGIIP 1155
Cdd:PRK06501  314 AHGTSTPENDKMEYLGLSAVFGERLasipVSSNKSMIGHTLTAAGAVE--AVFSLLtiQTGRLP 375
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3354 8.72e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 66.05  E-value: 8.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKEKLIR---ELTKLNVGITGII 3281
Cdd:PRK12825   10 LVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELvEAVEALGRRAQAVQADVTDKAALEAavaAAVERFGRIDILV 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEE-----IEKHFNyKIenfIMMSSFTAACGNEGQLNYGVSNAYLE 3354
Cdd:PRK12825   90 NNAGIFEDKPLADMSDDEWDEVIDVNLSGvFHLLRAvvppmRKQRGG-RI---VNISSVAGLPGWPGRSNYAAAKAGLV 164
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2943-3024 1.00e-10

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 61.50  E-value: 1.00e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   2943 ATVDRTEIRRKVSLAVFDLATETL---SAEDLQ-SKGFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDELS 3018
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLghaAAEAIDpDRPFRDLGLDSLMAVELRNRLEAAT--GLRLPATLVFDHPTPAALA 79

                    ....*.
gi 392926054   3019 DHIVRK 3024
Cdd:smart00823   80 EHLAAE 85
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
3206-3351 1.08e-10

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 65.95  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGIIH 3282
Cdd:PRK05653    9 LVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAavrALIEAAVEAFGALDILVN 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926054 3283 SAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN----FIMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:PRK05653   89 NAGITRDALLPRMSEEDWDRVIDVNLTGtFNVVRAALPPM---IKArygrIVNISSVSGVTGNPGQTNYSAAKA 159
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
4346-4628 1.25e-10

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 65.93  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4346 GCSANEFSHIVYAYGYKDPRAewsggtsnSALAGRIAHWLKLK-GPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGT 4424
Cdd:cd00327    23 GLSKGPIVGVIVGTTGGSGEF--------SGAAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4425 VNLVmhemttdvlqnakmtvddfckafdVDANGykrseavCSMLLTKS------PNIDSVATITNYATGHNGtSSSLFTP 4498
Cdd:cd00327    95 SEEF------------------------VFGDG-------AAAAVVESeehalrRGAHPQAEIVSTAATFDG-ASMVPAV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4499 NGLSQLEVMQRATNPL----EKILEIQTHCTGTKLGDPIEINAI-SKLVSSACKIGSVKSNIGHTEGSSGLVSLCSSLMS 4573
Cdd:cd00327   143 SGEGLARAARKALEGAgltpSDIDYVEAHGTGTPIGDAVELALGlDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLM 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392926054 4574 FRSkyrvaqlhlkcptnsiktnkmicRFIGEDADENNSILINNFGFTGSNCSVVL 4628
Cdd:cd00327   223 LEH-----------------------EFIPPTPREPRTVLLLGFGLGGTNAAVVL 254
Acyl_transf_1 pfam00698
Acyl transferase domain;
5802-6007 1.44e-10

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 66.73  E-value: 1.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5802 ATQFAQIAIFVQCMAIFKAIKNV-FNPTCLIGHSVGEYAAAVISGALKTEEALKLLIKRSELIGKTEKAR-MLMVWNYEK 5879
Cdd:pfam00698   58 GTQFVQPALFAMQIALAALLQSYgVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGgMAAVELSAE 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  5880 QL----PSHVHVSAIIDANTKCVVGPVETIDNLEKYFINNHIKYRNIETKHGFHSKMFHCISKEFEFFCESFATKVPLIP 5955
Cdd:pfam00698  138 EVeqrwPDDVVGAVVNSPRSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVP 217
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392926054  5956 MISSITGSEI--KIFDSKYCTMHLTNPVNLELVVDHIMKLDIDIIVEVGPTGVL 6007
Cdd:pfam00698  218 FISSTSIDPSdqRTLSAEYWVRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLL 271
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
7102-7412 1.73e-10

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 66.59  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7102 IFTSGSTGVPKGVLM-AEQSVSSFMtsASKQCM-FRSNIRVLDSVKqVFDVS-VSNIIGSVLNGGVLISSEHSTTITDQL 7178
Cdd:cd17630     6 ILTSGSTGTPKAVVHtAANLLASAA--GLHSRLgFGGGDSWLLSLP-LYHVGgLAILVRSLLAGAELVLLERNQALAEDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7179 --QKCQYAFL-PAAVFNGFTDK-TMSRLESIETLTIGGETVSDVVIETAMKKfpRLRTIQIYGPTET----CIWSLTNKC 7250
Cdd:cd17630    83 apPGVTHVSLvPTQLQRLLDSGqGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTETasqvATKRPDGFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7251 KVStlnIGSALGDSlsnETCTicnnSVRGNVQVKGISLARGYITSAPHGTPFSD-IYSTGDIVDSKLNS-LQYIGRMDSQ 7328
Cdd:cd17630   161 RGG---VGVLLPGR---ELRI----VEDGEIWVGGASLAMGYLRGQLVPEFNEDgWFTTKDLGELHADGrLTVLGRADNM 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7329 VKCKGVRINISEIEKELILCLGLLQIVVLYS-----NQMLIAFIVdQKSKLLHDSLVKTLKN---RTQIPDYFVQINKMP 7400
Cdd:cd17630   231 IISGGENIQPEEIEAALAAHPAVRDAFVVGVpdeelGQRPVAVIV-GRGPADPAELRAWLKDklaRFKLPKRIYPVPELP 309
                         330
                  ....*....|..
gi 392926054 7401 LNSSGKVDKSLL 7412
Cdd:cd17630   310 RTGGGKVDRRAL 321
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2946-3026 3.11e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 59.87  E-value: 3.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2946 DRTEIRRKVS--LA-VFDLATETLSAED-LqskgFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDELSDHI 3021
Cdd:COG0236     2 PREELEERLAeiIAeVLGVDPEEITPDDsF----FEDLGLDSLDAVELIAALEEEF--GIELPDTELFEYPTVADLADYL 75

                  ....*
gi 392926054 3022 VRKKS 3026
Cdd:COG0236    76 EEKLA 80
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
4448-4628 3.56e-10

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 66.21  E-value: 3.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4448 CKAFDVDANGYKRSEAvCSMLLTKSP------NIDSVATITNYATGHNGTSSSLftPNGLSQLEVMQ----RATNPLEKI 4517
Cdd:PRK07103  225 CRPFDQDRDGFIYGEA-CGAVVLESAesarrrGARPYAKLLGWSMRLDANRGPD--PSLEGEMRVIRaalrRAGLGPEDI 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4518 LEIQTHCTGTKLGDPIEINAISKLVSSACKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLKCPTNSiktnkm 4597
Cdd:PRK07103  302 DYVNPHGTGSPLGDETELAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPIDE------ 375
                         170       180       190
                  ....*....|....*....|....*....|...
gi 392926054 4598 ICRFIGEDAD--ENNSILINNFGFTGSNCSVVL 4628
Cdd:PRK07103  376 RFRWVGSTAEsaRIRYALSLSFGFGGINTALVL 408
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
6237-6393 4.46e-10

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 66.24  E-value: 4.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6237 LVFGANGFIGSIVFR-LLQEMGMNVIPISRASIP-----------------------SCDITNIKDVQNVFKSLG--FKK 6290
Cdd:cd08953   209 LVTGGAGGIGRALARaLARRYGARLVLLGRSPLPpeeewkaqtlaalealgarvlyiSADVTDAAAVRRLLEKVRerYGA 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6291 FSVVINCVGVETSA---KMNKTSLEQeiVLSPKTFGSVNILKCLEEFsiEVDKLVNFSSLSSVVPLLGNFDYASANCF-- 6365
Cdd:cd08953   289 IDGVIHAAGVLRDAllaQKTAEDFEA--VLAPKVDGLLNLAQALADE--PLDFFVLFSSVSAFFGGAGQADYAAANAFld 364
                         170       180       190
                  ....*....|....*....|....*....|
gi 392926054 6366 --VEALTKQGskYIKQFLTLSLPPLEGSRM 6393
Cdd:cd08953   365 afAAYLRQRG--PQGRVLSINWPAWREGGM 392
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
4991-5089 7.02e-10

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 65.55  E-value: 7.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4991 VFHLAGIVNNSLHENVKrDSLDEMVSI-KLQGAKNL----MKCCDETSHFVFSSSIANVLGSYGQSNYAFSNGLVTSFLE 5065
Cdd:cd08954   305 IFHLAFVLIDKVLEIDT-ESLFISVNKaKVMGAINLhnqsIKRCWKLDYFVLFSSVSSIRGSAGQCNYVCANSVLDSLSR 383
                          90       100
                  ....*....|....*....|....*..
gi 392926054 5066 ---TSSTKSTIIHWGPWKDVGMLAQPE 5089
Cdd:cd08954   384 yrkSIGLPSIAINWGAIGDVGFVSRNE 410
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
6475-6534 7.92e-10

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 57.96  E-value: 7.92e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054  6475 VIAEIWKETLGISILN-DANPNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQE 6534
Cdd:pfam00550    2 RLRELLAEVLGVPAEEiDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
1949-2282 8.17e-10

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 65.41  E-value: 8.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1949 NFITQD---VTQFDPSFFkISKSEAELIDPQQRLLLECVQECLENSGVIET----SNVGVFVG-------LMEKEYQDMM 2014
Cdd:PRK08722   45 NFSTRFaglVKDFNCEEY-MSKKDARKMDLFIQYGIAAGIQALDDSGLEVTeenaHRIGVAIGsgigglgLIEAGHQALV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2015 ESS----SILAMLGSMAAVIAGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLR 2090
Cdd:PRK08722  124 EKGprkvSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGF 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2091 TNGKMLSQ-----HGMSLSFDSRASGYGRSDGCVVLMLELAKPNFHYMSTIQSVNVNHG--GRSVSLTAP--NGVAHKML 2161
Cdd:PRK08722  204 GAAKALSTrndepQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGmsGDAYHMTSPseDGSGGALA 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2162 LTSVINQSPSLA--IDYWEAHGTGTPLGDPIEFNTLSSIL-----QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQY 2234
Cdd:PRK08722  284 MEAAMRDAGVTGeqIGYVNAHGTSTPAGDVAEIKGIKRALgeagsKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQI 363
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392926054 2235 VPTLIHF----HVLNKDINAGSIRlpiigEDSELVSAGISSFGVSGTNAAAI 2282
Cdd:PRK08722  364 VPPTINLddpeEGLDIDLVPHTAR-----KVESMEYAICNSFGFGGTNGSLI 410
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
4388-4628 9.54e-10

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 64.69  E-value: 9.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4388 KGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQnaKMTV--DDFCKAFDVDANGYKRSE--A 4463
Cdd:PRK05952  136 QGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQ--QMGAlaKTGAYPFDRQREGLVLGEggA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4464 VC---SMLLTKSPNIDSVATITNYATGHNGTSSSLFTPNGLSQLEVMQ----RATNPLEKILEIQTHCTGTKLGDPIEIN 4536
Cdd:PRK05952  214 ILvleSAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQqclaRSGLTPEDIDYIHAHGTATRLNDQREAN 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4537 AISKLVSSACKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKyrvaQLHlkcPTNSIKTNKMICRFIGEDADEN-NSILIN 4615
Cdd:PRK05952  294 LIQALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQ----QLP---PCVGLQEPEFDLNFVRQAQQSPlQNVLCL 366
                         250
                  ....*....|...
gi 392926054 4616 NFGFTGSNCSVVL 4628
Cdd:PRK05952  367 SFGFGGQNAAIAL 379
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
6995-7407 9.92e-10

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 65.31  E-value: 9.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6995 STNTVSYSDLAEKIENISKDIQKQLqiakatsVREDELVGLDCKNS--YFAL-LACVFLGLPYAPIDPTWPEP---RQL- 7067
Cdd:cd05911     7 TGKELTYAQLRTLSRRLAAGLRKLG-------LKKGDVVGIISPNStyYPPVfLGCLFAGGIFSAANPIYTADelaHQLk 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7068 FVKSKVSFTLENCFScnlKLRN-------------FNSRTQF-GSIYSI---------------------------FTSG 7106
Cdd:cd05911    80 ISKPKVIFTDPDGLE---KVKEaakelgpkdkiivLDDKPDGvLSIEDLlsptlgeededlppplkdgkddtaailYSSG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7107 STGVPKGVLMAEQSVSS--FMTSASKQCMFRSNIRVLdSVKQVFDVS-VSNIIGSVLNGG-VLISSEHS-----TTItdQ 7177
Cdd:cd05911   157 TTGLPKGVCLSHRNLIAnlSQVQTFLYGNDGSNDVIL-GFLPLYHIYgLFTTLASLLNGAtVIIMPKFDselflDLI--E 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7178 LQKCQYAFLPAAVFNGF---TDKTMSRLESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLTNkcKVST 7254
Cdd:cd05911   234 KYKITFLYLVPPIAAALaksPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVN--PDGD 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7255 LNIGSAlGDSLSN--------ETCTICNNSVRGNVQVKGISLARGYI--TSAPHGTPFSD-IYSTGDIVDSKLNSLQYI- 7322
Cdd:cd05911   312 DKPGSV-GRLLPNveakivddDGKDSLGPNEPGEICVRGPQVMKGYYnnPEATKETFDEDgWLHTGDIGYFDEDGYLYIv 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7323 GRMDSQVKCKGVRINISEIEkELILCL-GLLQIVVL-----YSNQMLIAFIVDQKSKLL-HDSLVKTLKnrTQIPDY--- 7392
Cdd:cd05911   391 DRKKELIKYKGFQVAPAELE-AVLLEHpGVADAAVIgipdeVSGELPRAYVVRKPGEKLtEKEVKDYVA--KKVASYkql 467
                         490       500
                  ....*....|....*....|
gi 392926054 7393 -----FVQinKMPLNSSGKV 7407
Cdd:cd05911   468 rggvvFVD--EIPKSASGKI 485
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
6214-6369 1.15e-09

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 61.42  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6214 LCKHGFRTTEIPSRLHPVSRGHAlvfganGFIgsivfRLLQEMGMNVIPISrasipsCDITNIKDVQNVFKSLGFKKFSV 6293
Cdd:pfam08659   20 LAERGARHLVLLSRSAAPRPDAQ------ALI-----AELEARGVEVVVVA------CDVSDPDAVAALLAEIKAEGPPI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  6294 --VINCVGVETSAKMNKTSLEQ-EIVLSPKTFGSVNILKCLEEfsIEVDKLVNFSSLSSvvpLLGNF---DYASANCFVE 6367
Cdd:pfam08659   83 rgVIHAAGVLRDALLENMTDEDwRRVLAPKVTGTWNLHEATPD--EPLDFFVLFSSIAG---LLGSPgqaNYAAANAFLD 157

                   ..
gi 392926054  6368 AL 6369
Cdd:pfam08659  158 AL 159
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7102-7408 2.02e-09

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 64.38  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7102 IFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLI---SSEHSTTITDQL 7178
Cdd:cd05922   123 LYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVltnDGVLDDAFWEDL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7179 QK---CQYAFLP--AAVFNGFTDKTMSrLESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETciwsltnKCKVS 7253
Cdd:cd05922   203 REhgaTGLAGVPstYAMLTRLGFDPAK-LPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEA-------TRRMT 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7254 TL----------NIGSALGD---SLSNETCTICNNSVRGNVQVKGISLARGYITSAPH---GTPFSDIYSTGDIVDSKLN 7317
Cdd:cd05922   275 YLpperilekpgSIGLAIPGgefEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYrrkEGRGGGVLHTGDLARRDED 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7318 SLQYI-GRMDSQVKCKGVRINISEIEKEL--------ILCLGL-------LQIVVLYSNQMLIAFIVDQKSKLLHdslvk 7381
Cdd:cd05922   355 GFLFIvGRRDRMIKLFGNRISPTEIEAAArsigliieAAAVGLpdplgekLALFVTAPDKIDPKDVLRSLAERLP----- 429
                         330       340
                  ....*....|....*....|....*..
gi 392926054 7382 tlknRTQIPDYFVQINKMPLNSSGKVD 7408
Cdd:cd05922   430 ----PYKVPATVRVVDELPLTASGKVD 452
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
3994-4216 4.11e-09

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


Pssm-ID: 434191  Cd Length: 296  Bit Score: 62.00  E-value: 4.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3994 DEFELLEGHQLNGKIVVAGA-Y---------QLFKIDQLVKLKaagmelmlkNVKFLKPWYIEDNREYQIQ--------- 4054
Cdd:pfam14765   25 ADLPWLRDHRVGGTVVLPGAgYlemaleaarQLFGGSGAVALR---------DVSILKALVLPEDDPVEVQtsltpeedg 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4055 -----------WNSDMTiELIVNSVIVCSLEVEPQNSVLKLETI------SENEKPFEVHDFYETLFRNGLQYDSGFRRI 4117
Cdd:pfam14765   96 adswwefeifsRAGGGW-EWTLHATGTVRLAPGEPAAPVDLESLparcaqPADPRSVSSAEFYERLAARGLFYGPAFQGL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4118 ESARRSDKRCFSQIKSS----PFAWP------LIDSAMHSITASVVP--RRPDCYFLPVAMGSVTMKDTNSFTLPnLHAQ 4185
Cdd:pfam14765  175 RRIWRGDGEALAEARLPeaaaGGESPyllhpaLLDAALQLLGAALPAeaEHADQAYLPVGIERLRIYRSLPPGEP-LWVH 253
                          250       260       270
                   ....*....|....*....|....*....|..
gi 392926054  4186 TVITSETDKFIQVNVALLAGD-TPICEVRNMT 4216
Cdd:pfam14765  254 ARLERRGGRTIVGDLTLVDEDgRVVARIEGLR 285
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
3206-3351 4.98e-09

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 60.64  E-value: 4.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAK-ALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:cd05333     4 LVTGASRGIGRAIALRLAAEGA-KVAVTDRSEEAAAeTVEEIKALGGNAAALEADVSDREaveALVEKVEAEFGPVDILV 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926054 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN----FIMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:cd05333    83 NNAGITRDNLLMRMSEEDWDAVINVNLTGvFNVTQAVIRAM---IKRrsgrIINISSVVGLIGNPGQANYAASKA 154
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
864-1197 6.60e-09

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 62.33  E-value: 6.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  864 KKQCEGDAGLeVGLLKQDISMFDNSFFAIAKD----------EAEFLDPQHRLLLNAAYNALEKSGLTSIPD--ADLFLA 931
Cdd:PRK08722   26 KALLAGQSGI-VNIEHFDTTNFSTRFAGLVKDfnceeymskkDARKMDLFIQYGIAAGIQALDDSGLEVTEEnaHRIGVA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  932 ISA--------HSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKF 1003
Cdd:PRK08722  105 IGSgigglgliEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDAD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1004 AIVATSQLIQSSKW-------LYSLKTLLD--HHSTNSFSVDGSGFCRSDGVGVIILKTAEKGDSAVIKI--------SS 1066
Cdd:PRK08722  185 AMVAGGAEKASTPLgmagfgaAKALSTRNDepQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIyaelvgfgMS 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1067 AKSHHcgavMTPVVS-------SISQLLEEAG----SFSYVEGHGTATSAGDSAESMAYQK-LGSE----LIMSSVKAQF 1130
Cdd:PRK08722  265 GDAYH----MTSPSEdgsggalAMEAAMRDAGvtgeQIGYVNAHGTSTPAGDVAEIKGIKRaLGEAgskqVLVSSTKSMT 340
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926054 1131 GHCEVASGLIQ-LMKVSSIGKHGIIPSIvhNILPSEhirnnENIRLPFVAEE----KQIDRSAIVSFGITGT 1197
Cdd:PRK08722  341 GHLLGAAGSVEaIITVMSLVDQIVPPTI--NLDDPE-----EGLDIDLVPHTarkvESMEYAICNSFGFGGT 405
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
3206-3381 7.94e-09

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 59.07  E-value: 7.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRqptakalrefehwkskvhtiaaDIndkeklireltklnvgitgIIHSAG 3285
Cdd:cd02266     2 LVTGGSGGIGGAIARWLASRGSPKVLVVSRR----------------------DV-------------------VVHNAA 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3286 VLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFNYKIE-NFIMMSSFTAACGNEGQLNYGVSNAYLEYQVQRRRRQ 3363
Cdd:cd02266    41 ILDDGRLIDLTGSRIERAIRANVVGtRRLLEAARELMKAKRLgRFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASE 120
                         170       180
                  ....*....|....*....|..
gi 392926054 3364 GKSG----CAIQWGNWIDTGMA 3381
Cdd:cd02266   121 GWGNglpaTAVACGTWAGSGMA 142
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
6600-6926 8.82e-09

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 61.99  E-value: 8.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6600 LKYSLHSLIAYQPSYRTVFKSGN-SPYQYI---CSLTESFHDFDKRCN------LNNAISHEPNHLFEIGKSTPLRV--- 6666
Cdd:cd19531    41 LERALNELVARHEALRTTFVEVDgEPVQVIlppLPLPLPVVDLSGLPEaereaeAQRLAREEARRPFDLARGPLLRAtll 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6667 RVAEDCdnsriHI-VFNQHHILTDGWSMTVLSDTVSSLYAAYRGETSfPSKTKQTIsQVA---------MgtkSSGDIKE 6736
Cdd:cd19531   121 RLGEDE-----HVlLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRP-SPLPPLPI-QYAdyavwqrewL---QGEVLER 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6737 ALEYYQNTYHTII-----PYD-------SETGNTspsyVRISklIPSKIWQKLVGLSKLYNTTMYNLALSVFcdAV---R 6801
Cdd:cd19531   191 QLAYWREQLAGAPpvlelPTDrprpavqSFRGAR----VRFT--LPAELTAALRALARREGATLFMTLLAAF--QVllhR 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6802 sFTGQADILLAYAISGRN-ADNSELIGYFMNnalfktSLPfeiLRLEeilnivlnsLEKSRSFAT--------------- 6865
Cdd:cd19531   263 -YSGQDDIVVGTPVAGRNrAELEGLIGFFVN------TLV---LRTD---------LSGDPTFREllarvretaleayah 323
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6866 --IPFYQMVEQ---NRKLNEISLF---FNFrQKLDYPTVSMFGAKCEIEHLSLNNA-FDFSFTIDETPTG 6926
Cdd:cd19531   324 qdLPFEKLVEAlqpERDLSRSPLFqvmFVL-QNAPAAALELPGLTVEPLEVDSGTAkFDLTLSLTETDGG 392
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2790-2867 9.93e-09

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 55.72  E-value: 9.93e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054   2790 AAKTLQMAVRHKVCLAVGDVIESGLDIDESqlstgFSELGIDSLATVDLLNRLNQKYfpEIELTTSDLFDNPSIIDLS 2867
Cdd:smart00823    9 RRRLLLDLVREQVAAVLGHAAAEAIDPDRP-----FRDLGLDSLMAVELRNRLEAAT--GLRLPATLVFDHPTPAALA 79
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
7102-7408 1.88e-08

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 61.19  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7102 IFTSGSTGVPKGVLMAEQSVSSfmtsaskqcmfrsNIrvlDSVKQVFDVSVSNIIGSVL--------NGGVLI------- 7166
Cdd:cd05909   153 LFTSGSEGLPKGVVLSHKNLLA-------------NV---EQITAIFDPNPEDVVFGALpffhsfglTGCLWLpllsgik 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7167 -----SSEHSTTITDQLQKCQYAFLPAA--VFNGFTD-KTMSRLESIETLTIGGETVSDVVIETAMKKFpRLRTIQIYGP 7238
Cdd:cd05909   217 vvfhpNPLDYKKIPELIYDKKATILLGTptFLRGYARaAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGT 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7239 TETC-IWSLTNKC---KVSTLNIGSALGDSL--SNETCTICNNSVRGNVQVKGISLARGYITS-APHGTPFSD-IYSTGD 7310
Cdd:cd05909   296 TECSpVISVNTPQspnKEGTVGRPLPGMEVKivSVETHEEVPIGEGGLLLVRGPNVMLGYLNEpELTSFAFGDgWYDTGD 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7311 IVdsKLNSLQYI---GRMDSQVKCKGVRINISEIEkELILCLGLLQIVVLYSNqmliafIVDQKS----KLLH------- 7376
Cdd:cd05909   376 IG--KIDGEGFLtitGRLSRFAKIAGEMVSLEAIE-DILSEILPEDNEVAVVS------VPDGRKgekiVLLTtttdtdp 446
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 392926054 7377 DSLVKTLKN----RTQIPDYFVQINKMPLNSSGKVD 7408
Cdd:cd05909   447 SSLNDILKNagisNLAKPSYIHQVEEIPLLGTGKPD 482
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
3206-3304 2.31e-08

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 58.01  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQ-PTAKALREFEHWKSKVHTIAADINDK-------EKLIRELTKLNVgi 3277
Cdd:pfam00106    4 LVTGASSGIGRAIAKRLAKEGA-KVVLVDRSEeKLEAVAKELGALGGKALFIQGDVTDRaqvkalvEQAVERLGRLDI-- 80
                           90       100
                   ....*....|....*....|....*..
gi 392926054  3278 tgIIHSAGVLKDSKIERQNKESFNQVF 3304
Cdd:pfam00106   81 --LVNNAGITGLGPFSELSDEDWERVI 105
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
1951-2282 3.37e-08

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 60.13  E-value: 3.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1951 ITQDVTQFDPSFFkISKSEAELIDPQQRLLLECVQECLENS------------GVIETSNVGvfvGL--MEKEYQDMMES 2016
Cdd:PRK08439   48 IAGEITDFDPTEV-MDPKEVKKADRFIQLGLKAAREAMKDAgflpeeldaerfGVSSASGIG---GLpnIEKNSIICFEK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2017 -----------SSILAMLGsmaaviaGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEK 2085
Cdd:PRK08439  124 gprkispffipSALVNMLG-------GFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2086 GQGLRTNGKMLS------QHGmSLSFDSRASGYGRSDGCVVLMLE-----LAKPNFHYMSTI---QSVNVNHggrsVSLT 2151
Cdd:PRK08439  197 GIGGFAAMKALStrnddpKKA-SRPFDKDRDGFVMGEGAGALVLEeyesaKKRGAKIYAEIIgfgESGDANH----ITSP 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2152 APNGVAHKMllTSVINQSPSLAIDYWEAHGTGTPLGDPIEFNTLSSIL---QNI-IIGSVKASLGHGEASAGTCGLLKLF 2227
Cdd:PRK08439  272 APEGPLRAM--KAALEMAGNPKIDYINAHGTSTPYNDKNETAALKELFgskEKVpPVSSTKGQIGHCLGAAGAIEAVISI 349
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392926054 2228 LMLTYQYVPTLIHFhvLNKDINAGSIRLPIIGEDSELVSAGISSFGVSGTNAAAI 2282
Cdd:PRK08439  350 MAMRDGILPPTINQ--ETPDPECDLDYIPNVARKAELNVVMSNSFGFGGTNGVVI 402
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
2005-2231 3.79e-08

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 60.04  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2005 LMEKEYQDMMESSSILAMLGSMAAVIAGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVnliLNE 2084
Cdd:PRK07103  121 LVHETYRDRPAFLRPSYGLSFMDTDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGA---LMD 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2085 KG----QGLRTNGKMLSQHGMSL------SFDSRASG--YGRSDGCVVLmlELAKP----NFHYMSTIQSVNVNHGGRSV 2148
Cdd:PRK07103  198 LSywecQALRSLGAMGSDRFADEpeaacrPFDQDRDGfiYGEACGAVVL--ESAESarrrGARPYAKLLGWSMRLDANRG 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2149 SLTAPNGVAHkmlltsVINQSPSLA------IDYWEAHGTGTPLGDPIEFNTL-SSILQNIIIGSVKASLGHGEASAGTC 2221
Cdd:PRK07103  276 PDPSLEGEMR------VIRAALRRAglgpedIDYVNPHGTGSPLGDETELAALfASGLAHAWINATKSLTGHGLSAAGIV 349
                         250
                  ....*....|
gi 392926054 2222 GLLKLFLMLT 2231
Cdd:PRK07103  350 ELIATLLQMR 359
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
4377-4629 4.08e-08

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 59.75  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4377 LAGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQ-------------CEYAIVGTVNlvMHEMTTdvlQNakmt 4443
Cdd:PRK08439  141 LGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGadkmlvvgaesaiCPVGIGGFAA--MKALST---RN---- 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4444 vDDFCKA---FDVDANGYKRSEAVCSMLL-TKSPNIDSVATItnYAT----GHNGTSSSLFTPNGLSQLEVMQRA----T 4511
Cdd:PRK08439  212 -DDPKKAsrpFDKDRDGFVMGEGAGALVLeEYESAKKRGAKI--YAEiigfGESGDANHITSPAPEGPLRAMKAAlemaG 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4512 NPleKILEIQTHCTGTKLGDPIEINAISKLVSSACK---IGSVKSNIGHTEGSSGLVSLCSSLMSFRSKyrvaqlhLKCP 4588
Cdd:PRK08439  289 NP--KIDYINAHGTSTPYNDKNETAALKELFGSKEKvppVSSTKGQIGHCLGAAGAIEAVISIMAMRDG-------ILPP 359
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 392926054 4589 TNSIKTNKMICrfigeDAD---------ENNSILINNFGFTGSNCSVVLK 4629
Cdd:PRK08439  360 TINQETPDPEC-----DLDyipnvarkaELNVVMSNSFGFGGTNGVVIFK 404
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2800-2863 4.16e-08

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 53.34  E-value: 4.16e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926054  2800 HKVCLAVGDVIesGLDIDESQLSTGFSELGIDSLATVDLLNRLNQKYfpEIELTTSDLFDNPSI 2863
Cdd:pfam00550    1 ERLRELLAEVL--GVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEF--GVEIPPSDLFEHPTL 60
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
3206-3351 4.21e-08

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 58.11  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPT----AKALREfEHwKSKVHTIAADINDK---EKLIRELTKLNVGIT 3278
Cdd:cd05352    12 IVTGGSRGIGLAIARALAEAGA-DVAIIYNSAPRaeekAEELAK-KY-GVKTKAYKCDVSSQesvEKTFKQIQKDFGKID 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054 3279 GIIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFNYKIE-NFIMMSSFTAACGNEGQLN--YGVSNA 3351
Cdd:cd05352    89 ILIANAGITVHKPALDYTYEQWNKVIDVNLNGvFNCAQAAAKIFKKQGKgSLIITASMSGTIVNRPQPQaaYNASKA 165
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1806-1857 5.17e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 53.79  E-value: 5.17e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 392926054   1806 DIDNTTGFFDLGLTSIQAVKLRNAIKSNYP-NASSTCVFDYPSIDLLSGYLST 1857
Cdd:smart00823   32 AIDPDRPFRDLGLDSLMAVELRNRLEAATGlRLPATLVFDHPTPAALAEHLAA 84
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
961-1197 5.22e-08

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 59.42  E-value: 5.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  961 MVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVA------TSQL----IQSSKwlySLKTLLDHHST 1030
Cdd:PRK07314  140 MAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAggaeaaITPLgiagFAAAR---ALSTRNDDPER 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1031 NS--FSVDGSGFCRSDGVGVIILKTAE--KGDSAviKI--------SSAKSHHcgavMT-PV------VSSISQLLEEAG 1091
Cdd:PRK07314  217 ASrpFDKDRDGFVMGEGAGILVLEELEhaKARGA--KIyaevvgygMTGDAYH----MTaPApdgegaARAMKLALKDAG 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1092 ----SFSYVEGHGTATSAGDSAESMAYQKL----GSELIMSSVKAQFGHCEVASGLIQ-LMKVSSIgKHGIIPsivhnil 1162
Cdd:PRK07314  291 inpeDIDYINAHGTSTPAGDKAETQAIKRVfgehAYKVAVSSTKSMTGHLLGAAGAVEaIFSVLAI-RDQVIP------- 362
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 392926054 1163 PSEHIRN-NENIRLPFV---AEEKQIDRSAIVSFGITGT 1197
Cdd:PRK07314  363 PTINLDNpDEECDLDYVpneARERKIDYALSNSFGFGGT 401
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
7023-7414 6.06e-08

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 59.28  E-value: 6.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7023 KATSVREDELVGLDCKNS---YFALLACVFLGLPYAPIDptwpepRQLfVKSKVSFTLENcfscnlklrnfnSRTQFGSI 7099
Cdd:cd05912    19 AALGVRKGDRVALLSKNSiemILLIHALWLLGAEAVLLN------TRL-TPNELAFQLKD------------SDVKLDDI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7100 YSI-FTSGSTGVPKGVLmaeQSVSSFMTSA----------SKQC---------------MFRS-----NIRVLDSvkqvF 7148
Cdd:cd05912    80 ATImYTSGTTGKPKGVQ---QTFGNHWWSAigsalnlgltEDDNwlcalplfhisglsiLMRSviygmTVYLVDK----F 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7149 DVSvsNIIGSVLNGGVLISSEHSTTITDQLQKcqyafLPaavfNGFTdktmsrlESIETLTIGGETVSDVVIETAMKK-F 7227
Cdd:cd05912   153 DAE--QVLHLINSGKVTIISVVPTMLQRLLEI-----LG----EGYP-------NNLRCILLGGGPAPKPLLEQCKEKgI 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7228 PrlrTIQIYGPTETCIWSLTNKCKVSTLNIGSAlGDSLSNETCTICNNSVR----GNVQVKGISLARGYITSAP-HGTPF 7302
Cdd:cd05912   215 P---VYQSYGMTETCSQIVTLSPEDALNKIGSA-GKPLFPVELKIEDDGQPpyevGEILLKGPNVTKGYLNRPDaTEESF 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7303 SDIY-STGDIVDSKLNSLQYI-GRMDSQVKCKGVRINISEIEKELILCLGLLQIVVLYS-----NQMLIAFIVDQKsKLL 7375
Cdd:cd05912   291 ENGWfKTGDIGYLDEEGFLYVlDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIpddkwGQVPVAFVVSER-PIS 369
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 392926054 7376 HDSLVKTLKNRT---QIPDYFVQINKMPLNSSGKVDKSLLLQ 7414
Cdd:cd05912   370 EEELIAYCSEKLakyKVPKKIYFVDELPRTASGKLLRHELKQ 411
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
6476-6542 7.76e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 52.93  E-value: 7.76e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 6476 IAEIWKETLGISILN-DANPNFFS-LGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEFTKFVKNL 6542
Cdd:COG0236    10 LAEIIAEVLGVDPEEiTPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2808-2875 7.99e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 52.93  E-value: 7.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054 2808 DVIESGLDIDESQLSTG---FSELGIDSLATVDLLNRLNQKYfpEIELTTSDLFDNPSIIDLSIMIEQLLN 2875
Cdd:COG0236    12 EIIAEVLGVDPEEITPDdsfFEDLGLDSLDAVELIAALEEEF--GIELPDTELFEYPTVADLADYLEEKLA 80
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
7043-7412 8.20e-08

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 58.93  E-value: 8.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7043 ALLACVFLGLPYAPIDPTWPEPRQLFV----KSKVSFTLEncfscnlKLRNFNSRTQFGSI-YSIFTSGSTGVPKGVLma 7117
Cdd:cd05903    42 LYLACLRIGAVTNPILPFFREHELAFIlrraKAKVFVVPE-------RFRQFDPAAMPDAVaLLLFTSGTTGEPKGVM-- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7118 eQSVSSFMTSAskqCMFRSNIRVLDSVKQVFDVSVSNIIGSVlnGGVLISS-EHSTTITDQL------------QKCQYA 7184
Cdd:cd05903   113 -HSHNTLSASI---RQYAERLGLGPGDVFLVASPMAHQTGFV--YGFTLPLlLGAPVVLQDIwdpdkalalmreHGVTFM 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7185 FLPAAVFNGFT---DKTMSRLESIETLTIGGETVSDVVIETAMKKFpRLRTIQIYGPTETCiwSLTNKCKvSTLNIGSAL 7261
Cdd:cd05903   187 MGATPFLTDLLnavEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECP--GAVTSIT-PAPEDRRLY 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7262 GDS---------LSNETCTICNNSVRGNVQVKGISLARGYiTSAPHGTPFSDI---YSTGDIVDskLNSLQYI---GRMD 7326
Cdd:cd05903   263 TDGrplpgveikVVDDTGATLAPGVEGELLSRGPSVFLGY-LDRPDLTADAAPegwFRTGDLAR--LDEDGYLritGRSK 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7327 SQVKCKGVRINISEIEKELILCLGLLQI-VVLYSNQML----IAFIVDQKSKLLH-DSLVKTLKN----RTQIPDYFVQI 7396
Cdd:cd05903   340 DIIIRGGENIPVLEVEDLLLGHPGVIEAaVVALPDERLgeraCAVVVTKSGALLTfDELVAYLDRqgvaKQYWPERLVHV 419
                         410
                  ....*....|....*.
gi 392926054 7397 NKMPLNSSGKVDKSLL 7412
Cdd:cd05903   420 DDLPRTPSGKVQKFRL 435
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
3206-3286 8.26e-08

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 57.26  E-value: 8.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISR-----RQPTAKALREFEHWKSKVHTIAADINDK---EKLIRELTKLNVGI 3277
Cdd:cd08939     5 LITGGSSGIGKALAKELVKEGA-NVIIVARsesklEEAVEEIEAEANASGQKVSYISADLSDYeevEQAFAQAVEKGGPP 83

                  ....*....
gi 392926054 3278 TGIIHSAGV 3286
Cdd:cd08939    84 DLVVNCAGI 92
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
903-1155 8.41e-08

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 57.45  E-value: 8.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  903 QHRLLLNAAYNALEKSGLTSIPDADLFLAISAhseyralaekhinelderlwMGTVHSMVAGRLAVLMGIR-GRAMIVDT 981
Cdd:cd00327     7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTG--------------------GSGEFSGAAGQLAYHLGISgGPAYSVNQ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  982 TCSSVATALEMAVKSIREGRKFAIVAtsqliqsskwlyslktlldhhstnsfsVDGSGFCRSDGVGVIILKT----AEKG 1057
Cdd:cd00327    67 ACATGLTALALAVQQVQNGKADIVLA---------------------------GGSEEFVFGDGAAAAVVESeehaLRRG 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1058 DSAVIKISSAKSHHCGAVMTPVVS------SISQLLEEAG----SFSYVEGHGTATSAGDSAESMAYQKL--GSELIMSS 1125
Cdd:cd00327   120 AHPQAEIVSTAATFDGASMVPAVSgeglarAARKALEGAGltpsDIDYVEAHGTGTPIGDAVELALGLDPdgVRSPAVSA 199
                         250       260       270
                  ....*....|....*....|....*....|
gi 392926054 1126 VKAQFGHCEVASGLIQLMKVSSIGKHGIIP 1155
Cdd:cd00327   200 TLIMTGHPLGAAGLAILDELLLMLEHEFIP 229
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
7099-7409 8.42e-08

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 58.19  E-value: 8.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7099 IYSIFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQVFDVSVSNIIGSVLNGGVLISSehSTTITDQL 7178
Cdd:cd17633     3 FYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQ--RKFNPKSW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7179 QK--CQYAflpaaVFNGFTDKTMSRL--------ESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIwsLTN 7248
Cdd:cd17633    81 IRkiNQYN-----ATVIYLVPTMLQAlartlepeSKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF--ITY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7249 KCKVSTLNIGSAlGDSLSNETCTICN--NSVRGNVQVKGISLARGYIT---SAPHGTpfsdiYSTGDIVDSKLNSLQYI- 7322
Cdd:cd17633   154 NFNQESRPPNSV-GRPFPNVEIEIRNadGGEIGKIFVKSEMVFSGYVRggfSNPDGW-----MSVGDIGYVDEEGYLYLv 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7323 GRMDSQVKCKGVRINISEIEKELILCLGLLQIVVL-----YSNQMLIAFIVDQK--SKLLHDSLVKTLKnRTQIPDYFVQ 7395
Cdd:cd17633   228 GRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVgipdaRFGEIAVALYSGDKltYKQLKRFLKQKLS-RYEIPKKIIF 306
                         330
                  ....*....|....
gi 392926054 7396 INKMPLNSSGKVDK 7409
Cdd:cd17633   307 VDSLPYTSSGKIAR 320
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
3485-3549 1.00e-07

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 52.55  E-value: 1.00e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054 3485 IKEKVSSILMCSPTKLKNNKNIM-DMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLEKLAAHI 3549
Cdd:COG0236    10 LAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
7207-7418 1.01e-07

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 58.85  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7207 TLTIGGETVSDVVIETAmkKFPRLRTIQIYGPTETCiwsltnkCKVSTL--------NIGSalGDSLSNETCTICNNSVr 7278
Cdd:PRK07445  234 TILLGGAPAWPSLLEQA--RQLQLRLAPTYGMTETA-------SQIATLkpddflagNNSS--GQVLPHAQITIPANQT- 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7279 GNVQVKGISLARGYItsaPHGTPFSDIYSTGDI--VDSKlNSLQYIGRMDSQVKCKGVRINISEIEKeLILCLGLLQ-IV 7355
Cdd:PRK07445  302 GNITIQAQSLALGYY---PQILDSQGIFETDDLgyLDAQ-GYLHILGRNSQKIITGGENVYPAEVEA-AILATGLVQdVC 376
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054 7356 VL-----YSNQMLIAFIVDQKSKLLHDSLVKTLKN---RTQIPDYFVQINKMPLNSSGKVDKSLLLQAFEN 7418
Cdd:PRK07445  377 VLglpdpHWGEVVTAIYVPKDPSISLEELKTAIKDqlsPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQ 447
PRK12467 PRK12467
peptide synthase; Provisional
6467-6539 1.06e-07

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 59.79  E-value: 1.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926054 6467 PKStSCEFVIAEIWKETLGISILNdANPNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEFTKFV 6539
Cdd:PRK12467 3602 PRS-EVEQQLAAIWADVLGVEQVG-VTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS 3672
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
6265-6369 1.31e-07

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 55.18  E-value: 1.31e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   6265 RASIPSCDITNIKDVQNVFKSLGFKKFSV--VINCVGVETSAKMNKTSLEQ-EIVLSPKTFGSVNILKCLEEfsIEVDKL 6341
Cdd:smart00822   54 RVTVVACDVADRDALAAVLAAIPAVEGPLtgVIHAAGVLDDGVLASLTPERfAAVLAPKAAGAWNLHELTAD--LPLDFF 131
                            90       100
                    ....*....|....*....|....*...
gi 392926054   6342 VNFSSLSSVVPLLGNFDYASANCFVEAL 6369
Cdd:smart00822  132 VLFSSIAGVLGSPGQANYAAANAFLDAL 159
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
6236-6371 1.33e-07

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 55.67  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6236 ALVFGANGFIGSIVFRLLQEMGMNVIPISRAS-IPSCDITNIKDVQNVFKSLGfkKFSVVINCVGVETSAKMNKTSLEQ- 6313
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSgDYQVDITDEASIKALFEKVG--HFDAIVSTAGDAEFAPLAELTDADf 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926054 6314 EIVLSPKTFGSVNILKCLEEF-----SIEVdklvnFSSLSSVVPLLGNFDYASANCFVEALTK 6371
Cdd:cd11731    79 QRGLNSKLLGQINLVRHGLPYlndggSITL-----TSGILAQRPIPGGAAAATVNGALEGFVR 136
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
7436-7493 1.52e-07

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 51.80  E-value: 1.52e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054  7436 EKVINVFSKILGRN---VAPTDKFESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLK 7493
Cdd:pfam00550    1 ERLRELLAEVLGVPaeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
3485-3543 1.90e-07

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 51.41  E-value: 1.90e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054  3485 IKEKVSSILMCSPTKLKNNKNIMDMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLE 3543
Cdd:pfam00550    3 LRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
3201-3286 1.97e-07

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 55.94  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3201 ITGNW-LITGGLSGIGLEIGK-FIAnNGAEnVILISRRQPT-AKALREFEHwkskVHTIAADINDKE-------KLIREL 3270
Cdd:COG3967     3 LTGNTiLITGGTSGIGLALAKrLHA-RGNT-VIITGRREEKlEEAAAANPG----LHTIVLDVADPAsiaalaeQVTAEF 76
                          90
                  ....*....|....*.
gi 392926054 3271 TKLNVgitgIIHSAGV 3286
Cdd:COG3967    77 PDLNV----LINNAGI 88
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
3206-3304 2.11e-07

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 56.14  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGK-FIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAAD---INDKEKLIRELTKLNVGITGII 3281
Cdd:cd05367     3 ILTGASRGIGRALAEeLLKRGSPSVVVLLARSEEPLQELKEELRPGLRVTTVKADlsdAAGVEQLLEAIRKLDGERDLLI 82
                          90       100
                  ....*....|....*....|....
gi 392926054 3282 HSAGVLKD-SKIERQNKESFNQVF 3304
Cdd:cd05367    83 NNAGSLGPvSKIEFIDLDELQKYF 106
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
4378-4628 2.52e-07

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 57.49  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4378 AGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVnlvmhEMTTDVLqnakmTVDDFCKA------- 4450
Cdd:PLN02836  164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGT-----ESSIDAL-----SIAGFSRSralstkf 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4451 ----------FDVDANGYKRSEAVCSMLL-----TKSPNIDSVATITNYAT---GHNGTSSSlftPNGLSQLEVMQRATN 4512
Cdd:PLN02836  234 nscpteasrpFDCDRDGFVIGEGAGVLVLeelehAKRRGAKIYAEVRGYGMsgdAHHITQPH---EDGRGAVLAMTRALQ 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4513 P----LEKILEIQTHCTGTKLGDPIEINAISKL-----VSSACKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQL 4583
Cdd:PLN02836  311 QsglhPNQVDYVNAHATSTPLGDAVEARAIKTVfsehaTSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTL 390
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392926054 4584 HLKCPTNSIKTNKMICrfIGEDADENNSILINNFGFTGSNCSVVL 4628
Cdd:PLN02836  391 NLERPDPIFDDGFVPL--TASKAMLIRAALSNSFGFGGTNASLLF 433
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
2020-2280 2.55e-07

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 56.98  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2020 LAMLGSMAAVIAGRvnyIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVN-----LILnekgQGLRTNGk 2094
Cdd:PRK05952  118 LDTLPHQAAIAAAR---QIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEapitpLTL----AGFQQMG- 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2095 MLSQHGmSLSFDSRASGYGRSDGCVVLMLELAkpnfhymSTIQSVNVNHGGR--SVSLTAPngvAHKMLLTSVINQSPSL 2172
Cdd:PRK05952  190 ALAKTG-AYPFDRQREGLVLGEGGAILVLESA-------ELAQKRGAKIYGQilGFGLTCD---AYHMSAPEPDGKSAIA 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2173 A--------------IDYWEAHGTGTPLGDPIEFNTLSSIL-QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPT 2237
Cdd:PRK05952  259 AiqqclarsgltpedIDYIHAHGTATRLNDQREANLIQALFpHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPP 338
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 392926054 2238 LIHFHVLNKDINAgsIRLPiigEDSELVSAGISSFGVSGTNAA 2280
Cdd:PRK05952  339 CVGLQEPEFDLNF--VRQA---QQSPLQNVLCLSFGFGGQNAA 376
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
961-1199 2.58e-07

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 57.49  E-value: 2.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  961 MVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVA--TSQLIQS--------SKWLYSLKTLLDHHST 1030
Cdd:PLN02836  162 MAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAggTESSIDAlsiagfsrSRALSTKFNSCPTEAS 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1031 NSFSVDGSGFCRSDGVGVIILKTAEKGDSAVIKIS--------SAKSHHC--------GAVMtpvvsSISQLLEEAG--- 1091
Cdd:PLN02836  242 RPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYaevrgygmSGDAHHItqphedgrGAVL-----AMTRALQQSGlhp 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1092 -SFSYVEGHGTATSAGDSAESMAYQKLGSE------LIMSSVKAQFGHCEVASGLIQ-LMKVSSIgKHGIIPSIVHNILP 1163
Cdd:PLN02836  317 nQVDYVNAHATSTPLGDAVEARAIKTVFSEhatsggLAFSSTKGATGHLLGAAGAVEaIFSVLAI-HHGIAPPTLNLERP 395
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392926054 1164 SEHIRNNeniRLPFVAEEKQIDRSAIV-SFGITGTKT 1199
Cdd:PLN02836  396 DPIFDDG---FVPLTASKAMLIRAALSnSFGFGGTNA 429
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
2022-2282 2.85e-07

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 57.32  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2022 MLGSMAAviaGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHG- 2100
Cdd:PRK06333  147 FLTNMAA---GHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFn 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2101 -----MSLSFDSRASGYGRSDGCVVLMLEL--------AKPNFHYMSTIQSVNVNHggrsvsLTAP----NGVAHKMLLT 2163
Cdd:PRK06333  224 dapeqASRPFDRDRDGFVMGEGAGILVIETlehalargAPPLAELVGYGTSADAYH------MTAGpedgEGARRAMLIA 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2164 svINQ---SPSlAIDYWEAHGTGTPLGDPIEFNTLSSIL---QNIIIGSVKASLGHGEASAGtcGLLKLF--LMLTYQYV 2235
Cdd:PRK06333  298 --LRQagiPPE-EVQHLNAHATSTPVGDLGEVAAIKKVFghvSGLAVSSTKSATGHLLGAAG--GVEAIFtiLALRDQIA 372
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 392926054 2236 PTLIHFHvlNKDINAGSIRLpIIGEDSEL-VSAGIS-SFGVSGTNAAAI 2282
Cdd:PRK06333  373 PPTLNLE--NPDPAAEGLDV-VANKARPMdMDYALSnGFGFGGVNASIL 418
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
4943-5081 3.03e-07

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 54.11  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4943 GGIGSAIINEL--KPKSSVIIT-RKNIASEDGKTFL-------------SSDITRLD--------ISHKFNY---VFHLA 4995
Cdd:pfam08659   10 GGLGRELARWLaeRGARHLVLLsRSAAPRPDAQALIaeleargvevvvvACDVSDPDavaallaeIKAEGPPirgVIHAA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4996 GIVNNSLHENVKRDSLDEMVSIKLQGAKNLMKCCDETS--HFVFSSSIANVLGSYGQSNYAFSNGLVTSFLETSSTK--- 5070
Cdd:pfam08659   90 GVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPldFFVLFSSIAGLLGSPGQANYAAANAFLDALAEYRRSQglp 169
                          170
                   ....*....|.
gi 392926054  5071 STIIHWGPWKD 5081
Cdd:pfam08659  170 ATSINWGPWAE 180
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
6236-6372 3.68e-07

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 54.98  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6236 ALVFGANGFIGS-IVFRLLQEmGMNVIPISR-----------------ASIPSCDITNIKDVQNVFKSLG--FKKFSVVI 6295
Cdd:cd05233     1 ALVTGASSGIGRaIARRLARE-GAKVVLADRneealaelaaiealggnAVAVQADVSDEEDVEALVEEALeeFGRLDILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6296 NCVGVETSAKMNKTSLEQ-EIVLSPKTFGSVNILK-CLEEFsIEVDK--LVNFSSLSSVVPLLGNFDYASANCFVEALTK 6371
Cdd:cd05233    80 NNAGIARPGPLEELTDEDwDRVLDVNLTGVFLLTRaALPHM-KKQGGgrIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158

                  .
gi 392926054 6372 Q 6372
Cdd:cd05233   159 S 159
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
6237-6299 3.85e-07

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 55.52  E-value: 3.85e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926054 6237 LVFGANGFIGSIVFRLLQEMGMNVIPISRasiPSCDITNIKDVQNVFKSLgfkKFSVVINCVG 6299
Cdd:COG1091     3 LVTGANGQLGRALVRLLAERGYEVVALDR---SELDITDPEAVAALLEEV---RPDVVINAAA 59
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
6559-6888 4.38e-07

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 56.69  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6559 AIPLTNSQtQMFMLRQIDTTSKYNLIFKITISYETKFVWEFLKYSLHSLIAYQPSYRTVF--KSGNSPYQYICSLTES-- 6634
Cdd:cd19536     1 MYPLSSLQ-EGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFieDGLGQPVQVVHRQAQVpv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6635 -----FHDFDKRCNLNNAISHEPNHLFEIGKSTPLRVRVAEDCDNSRIHIVFNQHHILTDGWSMTVLSDTVSSLY---AA 6706
Cdd:cd19536    80 teldlTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYnqlLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6707 YRGETSFPSK-----TKQTISQVAmgtkssgdiKEALEYYQNTY-----HTIIPYDSET---GNTSPSYVRISKLIPSKI 6773
Cdd:cd19536   160 YKPLSLPPAQpyrdfVAHERASIQ---------QAASERYWREYlagatLATLPALSEAvggGPEQDSELLVSVPLPVRS 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6774 WQklvgLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGRNADNS---ELIGYFMNNALFKTSLPFEilRLEEIL 6850
Cdd:cd19536   231 RS----LAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTgaeRLLGLFLNTLPLRVTLSEE--TVEDLL 304
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 392926054 6851 NIVLNSLEKSRSFATIPFYQMVEQNRKLNEISLFFNFR 6888
Cdd:cd19536   305 KRAQEQELESLSHEQVPLADIQRCSEGEPLFDSIVNFR 342
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3485-3552 5.34e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 50.71  E-value: 5.34e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054   3485 IKEKVSSILMCSPTKLKN-NKNIMDMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLEKLAAHIFEQ 3552
Cdd:smart00823   17 VREQVAAVLGHAAAEAIDpDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
3203-3286 7.21e-07

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 54.15  E-value: 7.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3203 GNW-LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKAL-REFEH-WKSKVHTIAADINDK----EKLIRELTKLNV 3275
Cdd:cd05356     1 GTWaVVTGATDGIGKAYAEELAKRGF-NVILISRTQEKLDAVaKEIEEkYGVETKTIAADFSAGddiyERIEKELEGLDI 79
                          90
                  ....*....|.
gi 392926054 3276 GItgIIHSAGV 3286
Cdd:cd05356    80 GI--LVNNVGI 88
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
212-394 8.32e-07

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.


Pssm-ID: 238428 [Multi-domain]  Cd Length: 399  Bit Score: 55.44  E-value: 8.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  212 FDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEAlKNIDKDSVQLVTCH 291
Cdd:cd00832   218 FDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPPGLARAIRLALAD-AGLTPEDVDVVFAD 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  292 GTGTKLGDQVELTAINRSFKSD-IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGfVN 370
Cdd:cd00832   297 AAGVPELDRAEAAALAAVFGPRgVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTG-RP 375
                         170       180
                  ....*....|....*....|....
gi 392926054  371 EEMELNRVAISSYGFGGTNACAII 394
Cdd:cd00832   376 RPAALRTALVLARGRGGFNSALVV 399
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
3206-3304 1.39e-06

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 53.45  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADIND-KEKLIRELTKLnVGITGI---I 3281
Cdd:cd05325     2 LITGASRGIGLELVRQLLARGNNTVIATCRDPSAATELAALGASHSRLHILELDVTDeIAESAEAVAER-LGDAGLdvlI 80
                          90       100
                  ....*....|....*....|....
gi 392926054 3282 HSAGVL-KDSKIERQNKESFNQVF 3304
Cdd:cd05325    81 NNAGILhSYGPASEVDSEDLLEVF 104
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
1907-2284 1.72e-06

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 54.79  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1907 PSELWELLKIGKNASSRIP---ATRVPTRntlISGSkygnpveggnfitqdVTQFDPSFFkISKSEAELIDPQQRLLLEC 1983
Cdd:PRK07314   19 VESTWKNLLAGKSGIGPIThfdTSDLAVK---IAGE---------------VKDFNPDDY-MSRKEARRMDRFIQYGIAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1984 VQECLENSG-VIETSN---VGVFVG-------LMEKEYQDMMESS----SILAMLGSMAAVIAGRVNYIFGCYGPSVTID 2048
Cdd:PRK07314   80 AKQAVEDAGlEITEENadrIGVIIGsgiggleTIEEQHITLLEKGprrvSPFFVPMAIINMAAGHVSIRYGAKGPNHSIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2049 TACSSSLVALEMA--INALLDnrcSKVIVAG-VNLILNEKGQGLRTNGKMLSQ-----HGMSLSFDSRASGYGRSDGCVV 2120
Cdd:PRK07314  160 TACATGAHAIGDAarLIAYGD---ADVMVAGgAEAAITPLGIAGFAAARALSTrnddpERASRPFDKDRDGFVMGEGAGI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2121 LMLEL--------AKPnfhY-------MStiqsvnvnhgGRSVSLTAPN----GVAHKM---LLTSVINQSpslAIDYWE 2178
Cdd:PRK07314  237 LVLEElehakargAKI---YaevvgygMT----------GDAYHMTAPApdgeGAARAMklaLKDAGINPE---DIDYIN 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2179 AHGTGTPLGDPIEFNTLSSIL----QNIIIGSVKASLGHGEASAGtcGLLKLF--LMLTYQYVPTLIHFHVLNKDINAGS 2252
Cdd:PRK07314  301 AHGTSTPAGDKAETQAIKRVFgehaYKVAVSSTKSMTGHLLGAAG--AVEAIFsvLAIRDQVIPPTINLDNPDEECDLDY 378
                         410       420       430
                  ....*....|....*....|....*....|..
gi 392926054 2253 IrlPIIGEDSELVSAGISSFGVSGTNaAAIAF 2284
Cdd:PRK07314  379 V--PNEARERKIDYALSNSFGFGGTN-ASLVF 407
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
69-201 2.33e-06

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.


Pssm-ID: 238425 [Multi-domain]  Cd Length: 375  Bit Score: 54.19  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054   69 GTGES---EAICMDPQQrMLMQGVIKGLENAGITLEMAsEARVAVYTAAWcydykdllppdqyMATGNSASVMCgriTYF 145
Cdd:cd00829     2 GVGMTpfgRRSDRSPLE-LAAEAARAALDDAGLEPADI-DAVVVGNAAGG-------------RFQSFPGALIA---EYL 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054  146 LNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGANHVGSRSFHSLYNSH 201
Cdd:cd00829    64 GLLGKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGR 119
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
3206-3351 2.36e-06

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 52.89  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVIL--ISRRQPTAKALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGI 3280
Cdd:PRK05557    9 LVTGASRGIGRAIAERLAAQGA-NVVInyASSEAGAEALVAEIGALGGKALAVQGDVSDAEsveRAVDEAKAEFGGVDIL 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054 3281 IHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHF----NYKIenfIMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:PRK05557   88 VNNAGITRDNLLMRMKEEDWDRVIDTNLTGvFNLTKAVARPMmkqrSGRI---INISSVVGLMGNPGQANYAASKA 160
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
6989-7114 2.42e-06

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 54.49  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6989 EPALLLSTNTVSYSDLAEKIENISKDIQKQLqiakatsVREDELVGLDCKNSY---FALLACVFLGLPYAPIDPTWPEPR 7065
Cdd:PRK09029   19 AIALRLNDEVLTWQQLCARIDQLAAGFAQQG-------VVEGSGVALRGKNSPetlLAYLALLQCGARVLPLNPQLPQPL 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926054 7066 Q------------LFVKSKVSFTLENCFSCNLKLRNFNSRTQFGSIYS-IFTSGSTGVPKGV 7114
Cdd:PRK09029   92 LeellpsltldfaLVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATmTLTSGSTGLPKAA 153
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
3206-3358 2.77e-06

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 52.75  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAK-ALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:cd05347     9 LVTGASRGIGFGIASGLAEAGA-NIVINSRNEEKAEeAQQLIEKEGVEATAFTCDVSDEEaikAAVEAIEEDFGKIDILV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHF----NYKIEN---------FIMMSSFTAACGNEGQLNYG 3347
Cdd:cd05347    88 NNAGIIRRHPAEEFPEAEWRDVIDVNLNGvFFVSQAVARHMikqgHGKIINicsllselgGPPVPAYAASKGGVAGLTKA 167
                         170
                  ....*....|.
gi 392926054 3348 VSNAYLEYQVQ 3358
Cdd:cd05347   168 LATEWARHGIQ 178
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
4991-5088 3.23e-06

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 54.10  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4991 VFHLAGIVNNSLHENVKRDSLDEMVSIKLQGAKNLmkcCDET-----SHFVFSSSIANVLGSYGQSNYAFSN-------- 5057
Cdd:cd08952   314 VVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHL---DELTrdrdlDAFVLFSSIAGVWGSGGQGAYAAANayldalae 390
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 392926054 5058 -----GLVTsfleTSstkstiIHWGPWKDVGMLAQP 5088
Cdd:cd08952   391 rrrarGLPA----TS------VAWGPWAGGGMAAGA 416
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
4991-5114 3.83e-06

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 53.81  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4991 VFHLAGIVNNSLHENVKRDSLDEMVSIKLQGAKNLmkccDE------TSHFVFSSSIANVLGSYGQSNYAFSNglvtSFL 5064
Cdd:cd08956   278 VVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWHL----HEltrdldLAAFVLFSSAAGVLGSPGQANYAAAN----AFL 349
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926054 5065 E-------------TSstkstiIHWGPWKDVGMLAQPERREIVKQIESNGWKLLPNQDAISVF 5114
Cdd:cd08956   350 DalaqhrrarglpaTS------LAWGLWAQASGMTAHLSDADLARLARGGLRPLSAEEGLALF 406
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
730-803 4.71e-06

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 47.93  E-value: 4.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054  730 SDAEIESTVRTIVKQFLDIEEDDI----NLLETGAVDSLTSIEMVEAFGTAVNQTMPFDLLEAYPTILNIVDFLKTLV 803
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDPEEItpddSFFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
7323-7495 4.80e-06

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 53.92  E-value: 4.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7323 GRMDSQVKCKGVRINISEIEKELILCLGLLQIVVLYSN-----QMLIAFIVDQ-------KSKLLHDS------------ 7378
Cdd:TIGR03443  698 GRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRdkdeePTLVSYIVPQdksdeleEFKSEVDDeessdpvvkgli 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7379 ----LVKTLKN--RTQIPDY-----FVQINKMPLNSSGKVDK--------SLLLQAFENIRKSYKREIVvmkNSLEEKVI 7439
Cdd:TIGR03443  778 kyrkLIKDIREylKKKLPSYaiptvIVPLKKLPLNPNGKVDKpalpfpdtAQLAAVAKNRSASAADEEF---TETEREIR 854
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054  7440 NVFSKILGR---NVAPTDKFESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLKTF 7495
Cdd:TIGR03443  855 DLWLELLPNrpaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGF 913
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
4385-4628 6.13e-06

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 52.81  E-value: 6.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4385 LKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKMTV----DD---FCKAFDVDANG 4457
Cdd:PRK07910  158 RHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMstnnDDpagACRPFDKDRDG 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4458 YKRSEAVCSMLLTKSPNIDSV-ATITNYATGHNGTSSSLFT----PNGLSQLEVMQRA--TNPLEK--ILEIQTHCTGTK 4528
Cdd:PRK07910  238 FVFGEGGALMVIETEEHAKARgANILARIMGASITSDGFHMvapdPNGERAGHAMTRAieLAGLTPgdIDHVNAHATGTS 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4529 LGDPIEINAISKLV-SSACKIGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLKCPTNSIKTNKMicrfIGEDAD 4607
Cdd:PRK07910  318 VGDVAEGKAINNALgGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVV----AGEPRP 393
                         250       260
                  ....*....|....*....|..
gi 392926054 4608 ENNSILINN-FGFTGSNCSVVL 4628
Cdd:PRK07910  394 GNYRYAINNsFGFGGHNVALAF 415
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2949-3016 6.59e-06

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 47.17  E-value: 6.59e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054  2949 EIRRKVSlAVFDLATETLSAEDlqskGFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDE 3016
Cdd:pfam00550    2 RLRELLA-EVLGVPAEEIDPDT----DLFDLGLDSLLAVELIARLEEEF--GVEIPPSDLFEHPTLAE 62
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
376-431 6.77e-06

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 48.70  E-value: 6.77e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054   376 NRVAISSYGFGGTNACAIIEKPEKPSLVQKESYAESNVLFLSAKSHESLKLQIEEY 431
Cdd:pfam16197   25 GIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKALLEKL 80
PRK12316 PRK12316
peptide synthase; Provisional
6467-6535 7.20e-06

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 53.81  E-value: 7.20e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054 6467 PKSTSCEFVIAEIWKETLGISI--LNDanpNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEF 6535
Cdd:PRK12316 5068 APRSELEQQVAAIWAEVLQLERvgLDD---NFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAF 5135
PRK12826 PRK12826
SDR family oxidoreductase;
3206-3351 8.57e-06

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 51.07  E-value: 8.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADINDKEKL---IRELTKLNVGITGIIH 3282
Cdd:PRK12826   10 LVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALkaaVAAGVEDFGRLDILVA 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926054 3283 SAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnyKIENF---IMMSSFTA-ACGNEGQLNYGVSNA 3351
Cdd:PRK12826   90 NAGIFPLTPFAEMDDEQWERVIDVNLTGtFLLTQAALPAL--IRAGGgriVLTSSVAGpRVGYPGLAHYAASKA 161
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
4614-4695 1.03e-05

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 47.92  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  4614 INNFGFTGSNCSVVLK--PKNAISEhFVSSEVFYPILLSSHSAKSLQKYVQVL------CEFISnsakSLHDImmslFQK 4685
Cdd:pfam16197   29 VNSFGFGGANAHVILKsnPKPKIPP-ESPDNLPRLVLLSGRTEEAVKALLEKLenhlddAEFLS----LLNDI----HSL 99
                           90
                   ....*....|..
gi 392926054  4686 KI--HVHRQFII 4695
Cdd:pfam16197  100 PIsgHPYRGYAI 111
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
3205-3304 1.24e-05

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 50.57  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3205 WLITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALREfEHwKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:COG4221     8 ALITGASSGIGAATARALAAAGA-RVVLAARRAERLEALAA-EL-GGRALAVPLDVTDEAaveAAVAAAVAEFGRLDVLV 84
                          90       100
                  ....*....|....*....|...
gi 392926054 3282 HSAGVLKDSKIERQNKESFNQVF 3304
Cdd:COG4221    85 NNAGVALLGPLEELDPEDWDRMI 107
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
6237-6299 2.75e-05

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 49.93  E-value: 2.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926054 6237 LVFGANGFIGSIVFRLLQEMGMNVIPISRASIPSCDItNIKDVQNVFKSLGFKKFSVVINCVG 6299
Cdd:cd05254     3 LITGATGMLGRALVRLLKERGYEVIGTGRSRASLFKL-DLTDPDAVEEAIRDYKPDVIINCAA 64
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
7102-7409 3.07e-05

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 50.34  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7102 IFTSGSTGVPKGVLMAEQSVSSFMTSASKQCMFRSNIRVLDSVKQV-FDVSVSNIIGSVLNGGVLISSEHSTTITDQLQK 7180
Cdd:cd17635     7 IFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPAtHIGGLWWILTCLIHGGLCVTGGENTTYKSLFKI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7181 CQyafLPAAVFNGFTDKTMSRL-----------ESIETLTIGGETVSDVVIETAmKKFPRLRTIQIYGPTETciwslTNK 7249
Cdd:cd17635    87 LT---TNAVTTTCLVPTLLSKLvselksanatvPSLRLIGYGGSRAIAADVRFI-EATGLTNTAQVYGLSET-----GTA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7250 CKVST----LNIGsALGDSLSNETCTICNNSV-------RGNVQVKGISLARGYITSaPHGTP--FSDIY-STGDIVDSK 7315
Cdd:cd17635   158 LCLPTdddsIEIN-AVGRPYPGVDVYLAATDGiagpsasFGTIWIKSPANMLGYWNN-PERTAevLIDGWvNTGDLGERR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7316 LNSLQYI-GRMDSQVKCKGVRINISEIEKELILCLGLLQIVV--LYSNQM---LIAFIVdqKSKLLHDSLVKTLKNRTQ- 7388
Cdd:cd17635   236 EDGFLFItGRSSESINCGGVKIAPDEVERIAEGVSGVQECACyeISDEEFgelVGLAVV--ASAELDENAIRALKHTIRr 313
                         330       340
                  ....*....|....*....|....*..
gi 392926054 7389 ------IPDYFVQINKMPLNSSGKVDK 7409
Cdd:cd17635   314 elepyaRPSTIVIVTDIPRTQSGKVKR 340
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
7102-7409 3.17e-05

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 50.19  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7102 IFTSGSTGVPKGVLMAE-QSVSSFMT-SASKQCMFRSNIRVLDSVKQVFDVSvSNIIGSVLNGGVLISSE--HSTTITDQ 7177
Cdd:cd17638     6 MFTSGTTGRSKGVMCAHrQTLRAAAAwADCADLTEDDRYLIINPFFHTFGYK-AGIVACLLTGATVVPVAvfDVDAILEA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7178 LQKCQYAFLPAA--VFNGFTDKTMSR---LESIETLTIGGETVSDVVIETAMKKFPRLRTIQIYGPTETCIWSLtnkCKV 7252
Cdd:cd17638    85 IERERITVLPGPptLFQSLLDHPGRKkfdLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVATM---CRP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7253 --STLNIGSALGDSLSNETCTICNNsvrGNVQVKGISLARGYI--TSAPHGTPFSDIY-STGDI--VDSKLNsLQYIGRM 7325
Cdd:cd17638   162 gdDAETVATTCGRACPGFEVRIADD---GEVLVRGYNVMQGYLddPEATAEAIDADGWlHTGDVgeLDERGY-LRITDRL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7326 DSQVKCKGVRINISEIEKELILCLGLLQIVVL-----YSNQMLIAFIVDQKSKLL-HDSLVKTLKNRT---QIPDYFVQI 7396
Cdd:cd17638   238 KDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIgvpdeRMGEVGKAFVVARPGVTLtEEDVIAWCRERLanyKVPRFVRFL 317
                         330
                  ....*....|...
gi 392926054 7397 NKMPLNSSGKVDK 7409
Cdd:cd17638   318 DELPRNASGKVMK 330
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
3206-3414 3.53e-05

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 49.25  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALRE--FEHWKSKVHTIAADINDKEK---LIRELTKLNVGITGI 3280
Cdd:cd08930     6 LITGAAGLIGKAFCKALLSAGA-RLILADINAPALEQLKEelTNLYKNRVIALELDITSKESikeLIESYLEKFGRIDIL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3281 IHSAGV---LKDSKIERQNKESFNQVFTPKANGFHVL-EEIEKHF-NYKIENFIMMSSFTAACGNEgQLNYGVSNAY--L 3353
Cdd:cd08930    85 INNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCsQAFIKLFkKQGKGSIINIASIYGVIAPD-FRIYENTQMYspV 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926054 3354 EYQVqrrrrqGKSGcAIQWGNWIDTGMAtDENVR-KFLANLGFLGQHNKDALKYLRACILTK 3414
Cdd:cd08930   164 EYSV------IKAG-IIHLTKYLAKYYA-DTGIRvNAISPGGILNNQPSEFLEKYTKKCPLK 217
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
5628-5692 3.92e-05

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 46.38  E-value: 3.92e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926054  5628 LISIDSFGIGGTNVHMVIEFPARSQEVVKISSENLILydmIPISAKTEYSLDHTSEAISKYLQTD 5692
Cdd:pfam16197   26 IVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRL---VLLSGRTEEAVKALLEKLENHLDDA 87
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
6656-6831 4.13e-05

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 50.28  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6656 FEIGKSTPLR---VRVAEDcdnsRIHIVFNQHHILTDGWSMTVLSDTVSSLYAAYRGETSFPSKTKQTISQ--VAMGTKs 6730
Cdd:cd19543   108 FDLARAPLMRltlIRLGDD----RYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLPPVRPYRDyiAWLQRQ- 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6731 sgDIKEALEYYQN-----TYHTIIPYDSE-TGNTSPSYVRISKLIPSKIWQKLVGLSKLYNTTMYNLALSVFCDAVRSFT 6804
Cdd:cd19543   183 --DKEAAEAYWREylagfEEPTPLPKELPaDADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVVQGAWALLLSRYS 260
                         170       180       190
                  ....*....|....*....|....*....|
gi 392926054 6805 GQADILLAYAISGRNADNSEL---IGYFMN 6831
Cdd:cd19543   261 GRDDVVFGTTVSGRPAELPGIetmVGLFIN 290
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
963-1141 4.90e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 49.99  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  963 AGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVA--TSQLIQSSKW----LYSLKTLLDH-HSTNS-FS 1034
Cdd:PRK09116  144 AVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAggAEELCPTEAAvfdtLFATSTRNDApELTPRpFD 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1035 VDGSGFCRSDGVGVIILKTAE--KGDSAVI--KISSAKSHHCGAVMT-PVVSS----ISQLLEEAG----SFSYVEGHGT 1101
Cdd:PRK09116  224 ANRDGLVIGEGAGTLVLEELEhaKARGATIyaEIVGFGTNSDGAHVTqPQAETmqiaMELALKDAGlapeDIGYVNAHGT 303
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392926054 1102 ATSAGDSAESMAYQKL-GSELIMSSVKAQFGHCEVASGLIQ 1141
Cdd:PRK09116  304 ATDRGDIAESQATAAVfGARMPISSLKSYFGHTLGACGALE 344
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
2174-2282 5.16e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 50.01  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2174 IDYWEAHGTGTPLGDPIEFNTLSSI----LQNIIIGSVKASLGHGEASAGTC-GLLKLFLMLTYQYVPTlihfhvLNKDI 2248
Cdd:PRK06501  309 IDYINAHGTSTPENDKMEYLGLSAVfgerLASIPVSSNKSMIGHTLTAAGAVeAVFSLLTIQTGRLPPT------INYDN 382
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392926054 2249 NAGSIRLPIIGEDSE--LVSAGIS-SFGVSGTNAAAI 2282
Cdd:PRK06501  383 PDPAIPLDVVPNVARdaRVTAVLSnSFGFGGQNASLV 419
PRK12467 PRK12467
peptide synthase; Provisional
6473-6829 5.16e-05

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 50.93  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6473 EFVIAEIWKETLGISI--LNDanpNFFSLGGDSLSALQVVWKVQKKTDRIVDvNDLFDNPTLQEFTKFVKnlTTEKFAGN 6550
Cdd:PRK12467 2099 EQRLAAIWQDVLGLEQvgLHD---NFFELGGDSIISIQVVSRARQAGIRFTP-KDLFQHQTVQSLAAVAQ--EGDGTVSI 2172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6551 TNDKISYDaIPLTNSQtQMFMLRQIDTTSKYNLifKITISYETKFVWEFLKYSLHSLIAYQPSYRTVFKSGNS------- 6623
Cdd:PRK12467 2173 DQGPVTGD-LPLLPIQ-QMFFADDIPERHHWNQ--SVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGgwsamhr 2248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6624 -PYQYICSL--TESFHDFDKrcnlNNAISHEPNHLFEIGKSTPLRVRVAEDCDNS-RIHIVFnqHHILTDGWSMTVLsdt 6699
Cdd:PRK12467 2249 aPEQERRPLlwQVVVADKEE----LEALCEQAQRSLDLEEGPLLRAVLATLPDGSqRLLLVI--HHLVVDGVSWRIL--- 2319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6700 VSSLYAAYR----GET-SFPSKTK--QTISQVAMGTKSSGDIKEALEYYQNTYH---TIIPYDSETGNTSPSYVRISKLI 6769
Cdd:PRK12467 2320 LEDLQTAYRqlqgGQPvKLPAKTSafKAWAERLQTYAASAALADELGYWQAQLQgasTELPCDHPQGGLQRRHAASVTTH 2399
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054 6770 PSKIW--QKLVGLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGR-----NADNSELIGYF 6829
Cdd:PRK12467 2400 LDSEWtrRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGRedlfdEIDLTRTVGWF 2466
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
2174-2280 5.19e-05

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 50.05  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2174 IDYWEAHGTGTPLGDPIEFNTLSSILQNII--IGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDInAG 2251
Cdd:PRK07967  291 IDYINTHGTSTPVGDVKELGAIREVFGDKSpaISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQA-AG 369
                          90       100       110
                  ....*....|....*....|....*....|..
gi 392926054 2252 sirLPIIG---EDSELVSAGISSFGVSGTNAA 2280
Cdd:PRK07967  370 ---MPIVTettDNAELTTVMSNSFGFGGTNAT 398
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
4377-4629 5.26e-05

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 50.00  E-value: 5.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4377 LAGRIAHWLKLKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVNLVMHEMTTDVLQNAKMTV---DDFCKA--- 4450
Cdd:PRK08722  143 IAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALStrnDEPQKAsrp 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4451 FDVDANGYKRSEAVCSMLLTKSPNIDSV-ATItnYAT----GHNGTSSSLFTPN------GLSQLEVMQRATNPLEKILE 4519
Cdd:PRK08722  223 WDKDRDGFVLGDGAGMMVLEEYEHAKARgAKI--YAElvgfGMSGDAYHMTSPSedgsggALAMEAAMRDAGVTGEQIGY 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4520 IQTHCTGTKLGDPIEINAISKLVSSACK----IGSVKSNIGHTEGSSGLVSLCSSLMSFRSKYRVAQLHLKCPTNSIKTN 4595
Cdd:PRK08722  301 VNAHGTSTPAGDVAEIKGIKRALGEAGSkqvlVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDID 380
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392926054 4596 kmicrFIGEDADENNSI---LINNFGFTGSNCSVVLK 4629
Cdd:PRK08722  381 -----LVPHTARKVESMeyaICNSFGFGGTNGSLIFK 412
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
3204-3333 5.95e-05

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 49.21  E-value: 5.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3204 NWLITGGLSGIGLEIGKFIANNGAEnVILISRRQPTAKALREFEHwkskVHTIAADINDKEKLIRELTklnvGITGIIHS 3283
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHE-VVGLDRSPPGAANLAALPG----VEFVRGDLRDPEALAAALA----GVDAVVHL 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392926054 3284 AGVlkdSKIERQNKESFNQVFtpkANGF-HVLEEIEKHfnyKIENFIMMSS 3333
Cdd:COG0451    72 AAP---AGVGEEDPDETLEVN---VEGTlNLLEAARAA---GVKRFVYASS 113
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
6561-6831 6.12e-05

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 49.68  E-value: 6.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6561 PLTNSQTQMFMLRQIDT-TSKYNL--IFKIT--ISYETkfvwefLKYSLHSLIAYQPSYRTVFKSGN-SPYQYICSLTE- 6633
Cdd:cd19533     3 PLTSAQRGVWFAEQLDPeGSIYNLaeYLEITgpVDLAV------LERALRQVIAEAETLRLRFTEEEgEPYQWIDPYTPv 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6634 --SFHDFDKRCNLNNAISH----EPNHLFEIGKSTPLR---VRVAEDcdnsRIHIVFNQHHILTDGWSMTVLSDTVSSLY 6704
Cdd:cd19533    77 piRHIDLSGDPDPEGAAQQwmqeDLRKPLPLDNDPLFRhalFTLGDN----RHFWYQRVHHIVMDGFSFALFGQRVAEIY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6705 AAYRGETSFPSKTKQTISQVAMGTKSSGDIKEALE---YYQNTYHTIIPYDSETGNT---SPSYVRISKLIPSKIWQKLV 6778
Cdd:cd19533   153 TALLKGRPAPPAPFGSFLDLVEEEQAYRQSERFERdraFWTEQFEDLPEPVSLARRApgrSLAFLRRTAELPPELTRTLL 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392926054 6779 GLSKLYNTTMYNLALSVFCDAVRSFTGQADILLAYAISGR-NADNSELIGYFMN 6831
Cdd:cd19533   233 EAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlGAAARQTPGMVAN 286
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
3206-3323 7.33e-05

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 48.76  E-value: 7.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALRE---FEHWKSKVHTIAADIND-------KEKLIRELTKLNV 3275
Cdd:cd05327     5 VITGANSGIGKETARELAKRGA-HVIIACRNEEKGEEAAAeikKETGNAKVEVIQLDLSSlasvrqfAEEFLARFPRLDI 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 392926054 3276 gitgIIHSAGVlkdskierqnkesFNQVFTPKANGFhvleeiEKHF--NY 3323
Cdd:cd05327    84 ----LINNAGI-------------MAPPRRLTKDGF------ELQFavNY 110
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
2022-2280 7.71e-05

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 49.41  E-value: 7.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2022 MLGSMAAviaGRVNYIFGCYGPSVTIDTACSSSLVALEMAINaLLDNRCSKVIVAG--------VNLILNEKGQGLRTNG 2093
Cdd:PLN02836  158 ILINMAA---GHVSIRYGFQGPNHAAVTACATGAHSIGDAFR-MIQFGDADVMVAGgtessidaLSIAGFSRSRALSTKF 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2094 KMLSQHGmSLSFDSRASGYGRSDGCVVLMLEL---AKPNFHYM-STIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS 2169
Cdd:PLN02836  234 NSCPTEA-SRPFDCDRDGFVIGEGAGVLVLEElehAKRRGAKIyAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQS 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2170 ---PSlAIDYWEAHGTGTPLGDPIEFNTLSSIL------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIH 2240
Cdd:PLN02836  313 glhPN-QVDYVNAHATSTPLGDAVEARAIKTVFsehatsGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLN 391
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 392926054 2241 FHVLNKDINAGSIrlPIIGEDSELVSAGIS-SFGVSGTNAA 2280
Cdd:PLN02836  392 LERPDPIFDDGFV--PLTASKAMLIRAALSnSFGFGGTNAS 430
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
3206-3351 7.87e-05

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 48.46  E-value: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADIN---DKEKLIRElTKLNVGITGI- 3280
Cdd:PRK12935   10 IVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLvNELGKEGHDVYAVQADVSkveDANRLVEE-AVNHFGKVDIl 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926054 3281 IHSAGVLKDSKIERQNKESFNQVFtpKANGFHVLEEIEKHFNYKIEN----FIMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:PRK12935   89 VNNAGITRDRTFKKLNREDWERVI--DVNLSSVFNTTSAVLPYITEAeegrIISISSIIGQAGGFGQTNYSAAKA 161
PRK09072 PRK09072
SDR family oxidoreductase;
3206-3305 7.95e-05

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 48.40  E-value: 7.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALREFEHWKSKVHTIAADINDKE--KLIRELTKLNVGITGIIHS 3283
Cdd:PRK09072    9 LLTGASGGIGQALAEALAAAGA-RLLLVGRNAEKLEALAARLPYPGRHRWVVADLTSEAgrEAVLARAREMGGINVLINN 87
                          90       100
                  ....*....|....*....|..
gi 392926054 3284 AGVLKDSKIERQNKESFNQVFT 3305
Cdd:PRK09072   88 AGVNHFALLEDQDPEAIERLLA 109
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3351 8.58e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 48.03  E-value: 8.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPT-AKALREFEHWKSKVHTIAADINDKEKLIRELTKLNV---GITGII 3281
Cdd:PRK08217    9 VITGGAQGLGRAMAEYLAQKGA-KLALIDLNQEKlEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEdfgQLNGLI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3282 HSAGVL--------KDSKI-ERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN-----FIMMSSFTAAcGNEGQLNY 3346
Cdd:PRK08217   88 NNAGILrdgllvkaKDGKVtSKMSLEQFQSVIDVNLTGvFLCGREAAAKM---IESgskgvIINISSIARA-GNMGQTNY 163

                  ....*
gi 392926054 3347 GVSNA 3351
Cdd:PRK08217  164 SASKA 168
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
3206-3353 9.95e-05

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 47.71  E-value: 9.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALR-EFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:cd05350     2 LITGASSGIGRALAREFAKAGY-NVALAARRTDRLDELKaELLNPNPSVEVEILDVTDEErnqLVIAELEAELGGLDLVI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926054 3282 HSAGVLKDSKIERQNKESFNQVFTPKANGFHV-LEEIEKHFNYKIENFI-MMSSFTAACGNEGQLNYGVSNAYL 3353
Cdd:cd05350    81 INAGVGKGTSLGDLSFKAFRETIDTNLLGAAAiLEAALPQFRAKGRGHLvLISSVAALRGLPGAAAYSASKAAL 154
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
7527-7606 1.02e-04

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 45.21  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7527 IYLVHAIGGTIYPYYSFLQIFPKDislyGIE-FDLKYPSNDL------RELAHFyAEEIAAHAGNKRIFVMGHSMGGIMS 7599
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAA----GYPvYALNYPSTNGsiedsaEQLAAF-VDAVLAATGAEKVDLVGHSMGGLVA 82

                  ....*..
gi 392926054 7600 REIVAEL 7606
Cdd:COG1075    83 RYYLKRL 89
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
4387-4629 1.03e-04

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 48.83  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4387 LKGPVVTLDTACSSSFYALSAACDALRTGQCEYAIVGTVN-LVMHE-MTTDVLQnAKMTVDDFCKA----FDVDANGYKR 4460
Cdd:PRK09116  153 LKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEeLCPTEaAVFDTLF-ATSTRNDAPELtprpFDANRDGLVI 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4461 SEAVCSMLL-----TKSPNIDSVATITNYATGHNGTSSSlfTPnglsQLEVMQRATN--------PLEKILEIQTHCTGT 4527
Cdd:PRK09116  232 GEGAGTLVLeelehAKARGATIYAEIVGFGTNSDGAHVT--QP----QAETMQIAMElalkdaglAPEDIGYVNAHGTAT 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4528 KLGDPIEINAISKLVSSACKIGSVKSNIGHTEGSSG-LVSLCSSLMSFRSKYrvaqlhlkCPTNSIKTNKMIC---RFIG 4603
Cdd:PRK09116  306 DRGDIAESQATAAVFGARMPISSLKSYFGHTLGACGaLEAWMSIEMMNEGWF--------APTLNLTQVDPACgalDYIM 377
                         250       260
                  ....*....|....*....|....*...
gi 392926054 4604 EDADENNS--ILINNFGFTGSNCSVVLK 4629
Cdd:PRK09116  378 GEAREIDTeyVMSNNFAFGGINTSLIFK 405
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
5167-5235 1.12e-04

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 44.07  E-value: 1.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 5167 EEIFFEIVGItdISSKLNIP----------FMDLGIDSLCMENLRYSLNKNFDLELTVSEMFENATYQKLQTYVETLRK 5235
Cdd:COG0236     4 EELEERLAEI--IAEVLGVDpeeitpddsfFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
2031-2282 1.18e-04

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 48.57  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2031 AGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQH------GMSLS 2104
Cdd:PRK14691   71 AGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfnstpeKASRP 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2105 FDSRASGYGRSDGCVVLMLEL--------AKPNFHYMSTIQSVNVNHggrsVSLTAPNGVAHKMLLTSVINQ---SPSlA 2173
Cdd:PRK14691  151 FDTARDGFVMGEGAGLLIIEElehalargAKPLAEIVGYGTSADAYH----MTSGAEDGDGAYRAMKIALRQagiTPE-Q 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2174 IDYWEAHGTGTPLGDPIEFNTLSSIL---QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHvlNKDINA 2250
Cdd:PRK14691  226 VQHLNAHATSTPVGDLGEINAIKHLFgesNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLE--NPDPAA 303
                         250       260       270
                  ....*....|....*....|....*....|....
gi 392926054 2251 GSIRLpIIG--EDSELVSAGISSFGVSGTNAAAI 2282
Cdd:PRK14691  304 KGLNI-IAGnaQPHDMTYALSNGFGFAGVNASIL 336
PRK05691 PRK05691
peptide synthase; Validated
6473-6542 1.24e-04

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 49.40  E-value: 1.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6473 EFVIAEIWKETLGISILNdANPNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEFTKFVKNL 6542
Cdd:PRK05691 4243 EQTLATIWADVLKVERVG-VHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGL 4311
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
3206-3358 1.27e-04

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 47.75  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADINDKEKLIRELTKL--NVGITGI-IH 3282
Cdd:PRK07097   14 LITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIekEVGVIDIlVN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3283 SAGVLKDSKIERQNKESFNQVFTPKANG-F----HVLEEIEKHFNYKIENFI-MMS--------SFTAACGNEGQLNYGV 3348
Cdd:PRK07097   94 NAGIIKRIPMLEMSAEDFRQVIDIDLNApFivskAVIPSMIKKGHGKIINICsMMSelgretvsAYAAAKGGLKMLTKNI 173
                         170
                  ....*....|
gi 392926054 3349 SNAYLEYQVQ 3358
Cdd:PRK07097  174 ASEYGEANIQ 183
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
3206-3273 1.32e-04

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 47.66  E-value: 1.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALR-EF-EHWKSKVHTIAADINDKEKLIRELTKL 3273
Cdd:cd05346     4 LITGASSGIGEATARRFAKAGA-KLILTGRRAERLQELAdELgAKFPVKVLPLQLDVSDRESIEAALENL 72
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
3206-3304 1.32e-04

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 47.36  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAEnVILISRRQPTAKALREFEHwksKVHTIAADINDKEK---LIRELTKLNVGITGIIH 3282
Cdd:cd08932     4 LVTGASRGIGIEIARALARDGYR-VSLGLRNPEDLAALSASGG---DVEAVPYDARDPEDaraLVDALRDRFGRIDVLVH 79
                          90       100
                  ....*....|....*....|..
gi 392926054 3283 SAGVLKDSKIERQNKESFNQVF 3304
Cdd:cd08932    80 NAGIGRPTTLREGSDAELEAHF 101
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
6990-7123 1.43e-04

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 48.44  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6990 PALLLSTNTVSYSDLAEKIENISKDIQKQLQIAKATsvredeLVGLDCKNSY---FALLACVFLGLPYAPIDPTWPEPRQ 7066
Cdd:cd05941     3 IAIVDDGDSITYADLVARAARLANRLLALGKDLRGD------RVAFLAPPSAeyvVAQLAIWRAGGVAVPLNPSYPLAEL 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 7067 LFV--KSKVSFTLENCFScnlklrnfnsrtqfgsiysIFTSGSTGVPKGVLMAEQSVSS 7123
Cdd:cd05941    77 EYVitDSEPSLVLDPALI-------------------LYTSGTTGRPKGVVLTHANLAA 116
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
3206-3355 1.44e-04

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 47.27  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:cd05362     7 LVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVvAEIEAAGGKAIAVQADVSDPSqvaRLFDAAEKAFGGVDILV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHF--NYKIENFimMSSFTAAcgneGQLNYGV---SNAYLEY 3355
Cdd:cd05362    87 NNAGVMLKKPIAETSEEEFDRMFTVNTKGaFFVLQEAAKRLrdGGRIINI--SSSLTAA----YTPNYGAyagSKAAVEA 160
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
3206-3351 1.50e-04

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 47.45  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGaeNVILISRRQPTAKALR---EFEHWKSKVHTIAADINDKEKLIRELTKL---NVGITG 3279
Cdd:PRK12824    6 LVTGAKRGIGSAIARELLNDG--YRVIATYFSGNDCAKDwfeEYGFTEDQVRLKELDVTDTEECAEALAEIeeeEGPVDI 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054 3280 IIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHV----LEEIEKHFNYKIENfimMSSFTAACGNEGQLNYGVSNA 3351
Cdd:PRK12824   84 LVNNAGITRDSVFKRMSHQEWNDVINTNLNSvFNVtqplFAAMCEQGYGRIIN---ISSVNGLKGQFGQTNYSAAKA 157
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
3206-3289 1.69e-04

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 46.92  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAEnVILISRRQptaKALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGIIH 3282
Cdd:cd05370     9 LITGGTSGIGLALARKFLEAGNT-VIITGRRE---ERLAEAKKELPNIHTIVLDVGDAEsveALAEALLSEYPNLDILIN 84

                  ....*..
gi 392926054 3283 SAGVLKD 3289
Cdd:cd05370    85 NAGIQRP 91
PRK06198 PRK06198
short chain dehydrogenase; Provisional
3206-3333 1.73e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 47.31  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:PRK06198   10 LVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQaAELEALGAKAVFVQADLSDVEdcrRVVAAADEAFGRLDALV 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392926054 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFNYK-----IENFIMMSS 3333
Cdd:PRK06198   90 NAAGLTDRGTILDTSPELFDRHFAVNVRApFFLMQEAIKLMRRRkaegtIVNIGSMSA 147
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
6997-7368 2.11e-04

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 47.98  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6997 NTVSYSDLAEKIENISKdiqkQLQiakATSVREDELVGLDCKNSY-FAL--LACVFLGLPYAPIDPTWPEPRQLFVkskv 7073
Cdd:cd05907     4 QPITWAEFAEEVRALAK----GLI---ALGVEPGDRVAILSRNRPeWTIadLAILAIGAVPVPIYPTSSAEQIAYI---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7074 sftlencfscnlkLRNFNSRTQFGSIYS-----IFTSGSTGVPKGVLMAEQSVSSFMTSAskqcmfrsnIRVLDSVKQvf 7148
Cdd:cd05907    73 -------------LNDSEAKALFVEDPDdlatiIYTSGTTGRPKGVMLSHRNILSNALAL---------AERLPATEG-- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7149 DVSVS---------NIIGS--VLNGGVLISSEHST-TITDQLQKCQYAFLPAA------VFNGFTDKTMSRLES-IETLT 7209
Cdd:cd05907   129 DRHLSflplahvfeRRAGLyvPLLAGARIYFASSAeTLLDDLSEVRPTVFLAVprvwekVYAAIKVKAVPGLKRkLFDLA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7210 IGGETVSDVV----IETAMKKFPR---LRTIQIYGPTETciwsltnkCKVSTLN---------IGSALgdslsneTCTIC 7273
Cdd:cd05907   209 VGGRLRFAASggapLPAELLHFFRalgIPVYEGYGLTET--------SAVVTLNppgdnrigtVGKPL-------PGVEV 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7274 NNSVRGNVQVKGISLARGYItSAPHGTPFSDI----YSTGDIVDSKLNS-LQYIGRM-DSQVKCKGVRINISEIEKELIL 7347
Cdd:cd05907   274 RIADDGEILVRGPNVMLGYY-KNPEATAEALDadgwLHTGDLGEIDEDGfLHITGRKkDLIITSGGKNISPEPIENALKA 352
                         410       420
                  ....*....|....*....|..
gi 392926054 7348 CLGLLQIVVLYSNQ-MLIAFIV 7368
Cdd:cd05907   353 SPLISQAVVIGDGRpFLVALIV 374
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
3206-3279 2.35e-04

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 46.81  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRR----QPTAKALREFEhwKSKVHTIAADINDKE-------KLIRELTKLN 3274
Cdd:cd05369     7 FITGGGTGIGKAIAKAFAELGA-SVAIAGRKpevlEAAAEEISSAT--GGRAHPIQCDVRDPEaveaavdETLKEFGKID 83

                  ....*
gi 392926054 3275 VGITG 3279
Cdd:cd05369    84 ILINN 88
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
6469-6535 2.83e-04

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 48.12  E-value: 2.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054 6469 STSCEFVIAEIWKETLGISIlNDANPNFFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEF 6535
Cdd:PRK10252  976 KTGTETIIAAAFSSLLGCDV-VDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKL 1041
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
736-792 3.03e-04

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 42.17  E-value: 3.03e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054   736 STVRTIVKQFLDIEEDDI----NLLETGaVDSLTSIEMVEAFGTAVNQTMPFDLLEAYPTI 792
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIdpdtDLFDLG-LDSLLAVELIARLEEEFGVEIPPSDLFEHPTL 60
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
6232-6370 3.13e-04

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 46.40  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6232 SRGHALVFGANGFIGSIVFRLLQEMGMNVIPISR---------ASIPS---------CDITNIKDVQNVFKSLG--FKKF 6291
Cdd:COG0300     4 TGKTVLITGASSGIGRALARALAARGARVVLVARdaerlealaAELRAagarvevvaLDVTDPDAVAALAEAVLarFGPI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6292 SVVINCVGVETSAKMNKTSLEQ-EIVLSPKTFGSVNILK-CLEEFsIEVDK--LVNFSSLSSVVPLLGNFDYASANCFVE 6367
Cdd:COG0300    84 DVLVNNAGVGGGGPFEELDLEDlRRVFEVNVFGPVRLTRaLLPLM-RARGRgrIVNVSSVAGLRGLPGMAAYAASKAALE 162

                  ...
gi 392926054 6368 ALT 6370
Cdd:COG0300   163 GFS 165
PLN02752 PLN02752
[acyl-carrier protein] S-malonyltransferase
5735-5861 3.21e-04

[acyl-carrier protein] S-malonyltransferase


Pssm-ID: 215401 [Multi-domain]  Cd Length: 343  Bit Score: 47.06  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 5735 FNGKSPKIALFFAPQGIQFTNILpneylKNSAYRREVEYLCELASsfgipsleGIL-Y---------PTKNFDhlihATQ 5804
Cdd:PLN02752   33 FADYKPTTAFLFPGQGAQAVGMG-----KEAAEVPAAKALFDKAS--------EILgYdlldvcvngPKEKLD----STV 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926054 5805 FAQIAIFVQCMAIFKAIKN-------VFNPTCLIGHSVGEYAAAVISGALKTEEALKLLIKRSE 5861
Cdd:PLN02752   96 VSQPAIYVASLAAVEKLRArdggqavIDSVDVCAGLSLGEYTALVFAGALSFEDGLKLVKLRGE 159
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3304 3.26e-04

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 46.37  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADI---NDKEKLIRELTKLNVGITGII 3281
Cdd:PRK05565    9 IVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELlEEIKEEGGDAIAVKADVsseEDVENLVEQIVEKFGKIDILV 88
                          90       100
                  ....*....|....*....|...
gi 392926054 3282 HSAGVLKDSKIERQNKESFNQVF 3304
Cdd:PRK05565   89 NNAGISNFGLVTDMTDEEWDRVI 111
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
3206-3321 3.39e-04

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 46.30  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVIlISRRQPTAKALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGIIH 3282
Cdd:cd05349     4 LVTGASRGLGAAIARSFAREGA-RVV-VNYYRSTESAEAVAAEAGERAIAIQADVRDRDqvqAMIEEAKNHFGPVDTIVN 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 392926054 3283 SAGV------LKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHF 3321
Cdd:cd05349    82 NALIdfpfdpDQRKTFDTIDWEDYQQQLEGAVKGaLNLLQAVLPDF 127
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
5168-5222 3.76e-04

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 42.17  E-value: 3.76e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392926054  5168 EIFFEIVGITDISSKLNIPFMDLGIDSLCMENLRYSLNKNFDLELTVSEMFENAT 5222
Cdd:pfam00550    5 ELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
7527-7622 4.30e-04

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 45.84  E-value: 4.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  7527 IYLVHAIGGTIYPYYSFLQIFPKDISLYGIEfdlkYPS--------NDLRELAHFYAEEIAAHAGNKRIFVMGHSMGGIM 7598
Cdd:pfam00975    3 LFCFPPAGGSASSFRSLARRLPPPAEVLAVQ----YPGrgrgepplNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78
                           90       100
                   ....*....|....*....|....
gi 392926054  7599 SREIVAELKIWGYDIPFVMLFDSW 7622
Cdd:pfam00975   79 AFEVARRLERQGEAVRSLFLSDAS 102
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
6235-6362 4.38e-04

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 45.71  E-value: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6235 HALVFGANGFIG-SIVFRLLQEmGMNVIPISRA----------------------SIPSCDITNIKDVQNVFKSLGFKKF 6291
Cdd:cd08939     3 HVLITGGSSGIGkALAKELVKE-GANVIIVARSeskleeaveeieaeanasgqkvSYISADLSDYEEVEQAFAQAVEKGG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926054 6292 --SVVINCVGVETSAKMNKTSLEQ-EIVLSPKTFGSVNILK--CLEEFSIEVDKLVNFSSLSSVVPLLGNFDYASA 6362
Cdd:cd08939    82 ppDLVVNCAGISIPGLFEDLTAEEfERGMDVNYFGSLNVAHavLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPS 157
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
6145-6372 4.75e-04

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 47.06  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6145 SSPRCSTVVFVGMDNSPSVHLSLGLIRCYqLVS--RIDLKYVENFENIAMSIVIQKVLTANglYFRIDSTGLCKHGFRTT 6222
Cdd:cd08954   130 TADGCESSGVIGAVRYFREEPQLKLIRCL-FVSnlNSQKEPIIRNGKVYYERVKKNSNIKN--VYKSGSWGDFRHLLLDL 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6223 EIPSRLHPVSRGHA-LVFGANGFIGSIVFRLLQEMGM--NVIPISRASI--------------------PSCDITNIKDV 6279
Cdd:cd08954   207 SILKTNYPINLGKSyLITGGSGGLGLEILKWLVKRGAveNIIILSRSGMkwelellirewksqnikfhfVSVDVSDVSSL 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6280 QNVFKSL----------GFKKFSVVIN-CVGVETSAKMNKTsleqeiVLSPKTFGSVNilkcLEEFSIEVD-KLVNFSSL 6347
Cdd:cd08954   287 EKAINLIlnapkigpigGIFHLAFVLIdKVLEIDTESLFIS------VNKAKVMGAIN----LHNQSIKRCwKLDYFVLF 356
                         250       260
                  ....*....|....*....|....*...
gi 392926054 6348 SSVVPLLGNFD---YASANCFVEALTKQ 6372
Cdd:cd08954   357 SSVSSIRGSAGqcnYVCANSVLDSLSRY 384
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
7431-7499 5.38e-04

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 42.15  E-value: 5.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926054 7431 KNSLEEKVINVFSKILGRN---VAPTDKF-ESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLKTFCNTL 7499
Cdd:COG0236     3 REELEERLAEIIAEVLGVDpeeITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
3204-3351 5.39e-04

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 45.77  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3204 NWL--------ITGGLSGIGLEIGKFIANNGAeNVILISRRQptakalREFEHwkSKVHTIAADINDK---EKLIRELTK 3272
Cdd:PRK06171    3 DWLnlqgkiiiVTGGSSGIGLAIVKELLANGA-NVVNADIHG------GDGQH--ENYQFVPTDVSSAeevNHTVAEIIE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3273 LNVGITGIIHSAGV-----LKDSKIERQ----NKESFNQVFTPKANG-FHVLEEIEKHFNYKIENFIM-MSSFTAACGNE 3341
Cdd:PRK06171   74 KFGRIDGLVNNAGIniprlLVDEKDPAGkyelNEAAFDKMFNINQKGvFLMSQAVARQMVKQHDGVIVnMSSEAGLEGSE 153
                         170
                  ....*....|
gi 392926054 3342 GQLNYGVSNA 3351
Cdd:PRK06171  154 GQSCYAATKA 163
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
3205-3286 5.44e-04

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 45.65  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3205 WLITGGLSGIGLEIGKFIANNGAeNVILISRR----QPTAKALREFehWKSKVHTIAAD---INDKEKLIRELTKLNVGI 3277
Cdd:cd05332     6 VIITGASSGIGEELAYHLARLGA-RLVLSARReerlEEVKSECLEL--GAPSPHVVPLDmsdLEDAEQVVEEALKLFGGL 82

                  ....*....
gi 392926054 3278 TGIIHSAGV 3286
Cdd:cd05332    83 DILINNAGI 91
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
4989-5116 5.78e-04

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 44.81  E-value: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 4989 NYVFHLAGIVNNSLHENVKRDSLDEMVSIKLQGAKNLMKCCDE------TSHFVFSSSIANVLGSYGQSNYAFSN----G 5058
Cdd:cd02266    33 DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARElmkakrLGRFILISSVAGLFGAPGLGGYAASKaaldG 112
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054 5059 LVTSFLETSSTKS---TIIHWGPWKDVGMLAQPERREIVKQIESNGWKLLPNQDAISVFYT 5116
Cdd:cd02266   113 LAQQWASEGWGNGlpaTAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARALLN 173
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
2940-3024 7.42e-04

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 45.90  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2940 ESDATVDRTEIRRKVSlAVFDLATETLSAEDlqskGFTELGMDSLSIVDFVNRLNDKYFpddEITASDIFDYPTVDELSD 3019
Cdd:COG3433   214 ALETALTEEELRADVA-ELLGVDPEEIDPDD----NLFDLGLDSIRLMQLVERWRKAGL---DVSFADLAEHPTLAAWWA 285

                  ....*
gi 392926054 3020 HIVRK 3024
Cdd:COG3433   286 LLAAA 290
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
6236-6301 7.96e-04

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 45.31  E-value: 7.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6236 ALVFGANGFIGSIVFRLLQEMGMNVIPISRASIPS----------------CDITNIKDVQNVfkslgFKKFSVVINCVG 6299
Cdd:cd05271     3 VTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEAYArrllvmgdlgqvlfveFDLRDDESIRKA-----LEGSDVVINLVG 77

                  ..
gi 392926054 6300 VE 6301
Cdd:cd05271    78 RL 79
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
6237-6297 8.47e-04

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 45.34  E-value: 8.47e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926054  6237 LVFGANGFIGSIVFRLLQEMGMNVIPISRasiPSCDITNIKDVQNVFKSLgfkKFSVVINC 6297
Cdd:pfam04321    2 LITGANGQLGTELRRLLAERGIEVVALTR---AELDLTDPEAVARLLREI---KPDVVVNA 56
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
6475-6539 9.54e-04

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 41.85  E-value: 9.54e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054   6475 VIAEIWKETLGISILNDANPN--FFSLGGDSLSALQVVWKVQKKTDRIVDVNDLFDNPTLQEFTKFV 6539
Cdd:smart00823   16 LVREQVAAVLGHAAAEAIDPDrpFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
3205-3285 1.01e-03

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 44.91  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3205 WLITGGLSGIGLEIGKFIANNGaENVILISRRQPTAKALREFehWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:cd05374     3 VLITGCSSGIGLALALALAAQG-YRVIATARNPDKLESLGEL--LNDNLEVLELDVTDEEsikAAVKEVIERFGRIDVLV 79

                  ....
gi 392926054 3282 HSAG 3285
Cdd:cd05374    80 NNAG 83
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
3206-3287 1.28e-03

L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as L-threonine dehydrogenase (TDH). TDH catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. This group is distinct from TDHs that are members of the medium chain dehydrogenase/reductase family. This group has the NAD-binding motif and active site tetrad of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187580 [Multi-domain]  Cd Length: 308  Bit Score: 45.00  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANN-GAENVILISRRQPTAKAlreFEHWKSkvhtIAADINDKEKLiRELTKlNVGITGIIHSA 3284
Cdd:cd05272     3 LITGGLGQIGSELAKLLRKRyGKDNVIASDIRKPPAHV---VLSGPF----EYLDVLDFKSL-EEIVV-NHKITWIIHLA 73

                  ...
gi 392926054 3285 GVL 3287
Cdd:cd05272    74 ALL 76
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
3206-3354 1.44e-03

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 44.32  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRR----QPTAKALREFEHWKSKVHTIAADINDKEKL--IRELT-----KLN 3274
Cdd:cd05364     7 IITGSSSGIGAGTAILFARLGA-RLALTGRDaerlEETRQSCLQAGVSEKKILLVVADLTEEEGQdrIISTTlakfgRLD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3275 VgitgIIHSAGVLKDSKIERQNKESFNQVFtpKANGFHVLEEIEKHFNYKIE---NFIMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:cd05364    86 I----LVNNAGILAKGGGEDQDIEEYDKVM--NLNLRAVIYLTKLAVPHLIKtkgEIVNVSSVAGGRSFPGVLYYCISKA 159

                  ...
gi 392926054 3352 YLE 3354
Cdd:cd05364   160 ALD 162
PRK12939 PRK12939
short chain dehydrogenase; Provisional
3206-3354 1.56e-03

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 44.19  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAE---NVILISRRQPTAKALREFEHwksKVHTIAADINDKEKLIR---ELTKLNVGITG 3279
Cdd:PRK12939   11 LVTGAARGLGAAFAEALAEAGATvafNDGLAAEARELAAALEAAGG---RAHAIAADLADPASVQRffdAAAAALGGLDG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3280 IIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHF----NYKIENFimmSSFTAACGNEGQLNYGVSNAYLE 3354
Cdd:PRK12939   88 LVNNAGITNSKSATELDIDTWDAVMNVNVRGtFLMLRAALPHLrdsgRGRIVNL---ASDTALWGAPKLGAYVASKGAVI 164
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
3206-3304 1.68e-03

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 44.16  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADINDKEKLIR--ELTKLNVG-ITGIIH 3282
Cdd:cd05339     3 LITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEaaKKIKKEVGdVTILIN 82
                          90       100
                  ....*....|....*....|..
gi 392926054 3283 SAGVLKDSKIERQNKESFNQVF 3304
Cdd:cd05339    83 NAGVVSGKKLLELPDEEIEKTF 104
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
7531-7606 1.68e-03

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 44.07  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 7531 HAiGGTIYPYYSFLQIFPKDISLYGIEfdlkYPS----------NDLRELAHFYAEEIAAHAgNKRIFVMGHSMGGIMSR 7600
Cdd:COG3208    14 YA-GGSASAYRPWAAALPPDIEVLAVQ----LPGrgdrlgepplTSLEELADDLAEELAPLL-DRPFALFGHSMGALLAF 87

                  ....*.
gi 392926054 7601 EIVAEL 7606
Cdd:COG3208    88 ELARRL 93
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3310 2.11e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 44.00  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREfehwkSKVHTIAADIND-------KEKLIRELTKLNVgit 3278
Cdd:PRK06463   11 LITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELRE-----KGVFTIKCDVGNrdqvkksKEVVEKEFGRVDV--- 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 392926054 3279 gIIHSAGVLKDSKIERQNKESFNQVFTPKANG 3310
Cdd:PRK06463   83 -LVNNAGIMYLMPFEEFDEEKYNKMIKINLNG 113
PRK06500 PRK06500
SDR family oxidoreductase;
3206-3304 2.17e-03

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 43.79  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAEnVILISRRQPT-AKALREFEHWKSKVHTIAADINDKEKLIRELTKLNVGITGIIHSA 3284
Cdd:PRK06500   10 LITGGTSGIGLETARQFLAEGAR-VAITGRDPASlEAARAELGESALVIRADAGDVAAQKALAQALAEAFGRLDAVFINA 88
                          90       100
                  ....*....|....*....|
gi 392926054 3285 GVLKDSKIERQNKESFNQVF 3304
Cdd:PRK06500   89 GVAKFAPLEDWDEAMFDRSF 108
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
6466-6540 2.18e-03

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 44.36  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6466 LPKSTSCEFVIAEIWKETLGIS---ILNDANpnFFSLGGDSLSALQVV--WkvqKKTDRIVDVNDLFDNPTLQEFTKFVK 6540
Cdd:COG3433   214 ALETALTEEELRADVAELLGVDpeeIDPDDN--LFDLGLDSIRLMQLVerW---RKAGLDVSFADLAEHPTLAAWWALLA 288
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
6236-6300 2.25e-03

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 43.83  E-value: 2.25e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926054  6236 ALVFGANGFIGSIVFRLLQEMGMNVIPISRASIPS------------CDITNIKDVQNVFKSlgfKKFSVVINCVGV 6300
Cdd:pfam01370    1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASntarladlrfveGDLTDRDALEKLLAD---VRPDAVIHLAAV 74
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
837-1138 2.31e-03

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 44.60  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  837 AGVEgekELWDTLLTSRltTGkISDIRKKQCEGDA---GLEVGLLKQDISMFDNSFFAIAKDEAEFLDPQHRLLLNAAYN 913
Cdd:PRK06333   19 CGVE---TFWQRLLAGQ--SG-IRTLTDFPVGDLAtkiGGQVPDLAEDAEAGFDPDRYLDPKDQRKMDRFILFAMAAAKE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  914 ALEKSGL--TSIPDADLFLAI--SAHSEYRALAEKhINELDE----RLWMGTVHS----MVAGRLAVLMGIRGRAMIVDT 981
Cdd:PRK06333   93 ALAQAGWdpDTLEDRERTATIigSGVGGFPAIAEA-VRTLDSrgprRLSPFTIPSfltnMAAGHVSIRYGFKGPLGAPVT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  982 TCSSVATALEMAVKSIREGRkfAIVATSQLIQSSKWLYSL------KTLLDH------HSTNSFSVDGSGFCRSDGVGVI 1049
Cdd:PRK06333  172 ACAAGVQAIGDAARLIRSGE--ADVAVCGGTEAAIDRVSLagfaaaRALSTRfndapeQASRPFDRDRDGFVMGEGAGIL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 1050 ILKTAE----KGDSAVIKI----SSAKSHHcgavMTP-------VVSSISQLLEEAG----SFSYVEGHGTATSAGDSAE 1110
Cdd:PRK06333  250 VIETLEhalaRGAPPLAELvgygTSADAYH----MTAgpedgegARRAMLIALRQAGippeEVQHLNAHATSTPVGDLGE 325
                         330       340       350
                  ....*....|....*....|....*....|.
gi 392926054 1111 SMAYQKL---GSELIMSSVKAQFGHCEVASG 1138
Cdd:PRK06333  326 VAAIKKVfghVSGLAVSSTKSATGHLLGAAG 356
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
2779-2872 2.53e-03

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 43.97  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 2779 TLLSSQEASIVAAKTLQMAVRHKVCLAVGDVIESG---LDIDESqlstgFSELGIDSLATVDLLNRLNQKyfpEIELTTS 2855
Cdd:COG3433   201 AAEALLAAASPAPALETALTEEELRADVAELLGVDpeeIDPDDN-----LFDLGLDSIRLMQLVERWRKA---GLDVSFA 272
                          90
                  ....*....|....*..
gi 392926054 2856 DLFDNPSIIDLSIMIEQ 2872
Cdd:COG3433   273 DLAEHPTLAAWWALLAA 289
PRK08219 PRK08219
SDR family oxidoreductase;
3206-3304 2.85e-03

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 43.38  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIAnnGAENVILISRRQPTAKALREfEHwkSKVHTIAADINDKEKLIRELTKLnVGITGIIHSAG 3285
Cdd:PRK08219    7 LITGASRGIGAAIARELA--PTHTLLLGGRPAERLDELAA-EL--PGATPFPVDLTDPEAIAAAVEQL-GRLDVLVHNAG 80
                          90
                  ....*....|....*....
gi 392926054 3286 VLKDSKIERQNKESFNQVF 3304
Cdd:PRK08219   81 VADLGPVAESTVDEWRATL 99
PRK08628 PRK08628
SDR family oxidoreductase;
3206-3286 2.85e-03

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 43.41  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILiSRRQPTAKALREFEHWKSKVHTIAADINDK---EKLIRELTKLNVGITGIIH 3282
Cdd:PRK08628   11 IVTGGASGIGAAISLRLAEEGAIPVIF-GRSAPDDEFAEELRALQPRAEFVQVDLTDDaqcRDAVEQTVAKFGRIDGLVN 89

                  ....
gi 392926054 3283 SAGV 3286
Cdd:PRK08628   90 NAGV 93
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
155-186 3.21e-03

3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.


Pssm-ID: 430064 [Multi-domain]  Cd Length: 80  Bit Score: 39.81  E-value: 3.21e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 392926054   155 IETACSSSLVAFHLARQAIQSGETKLALVCGA 186
Cdd:pfam08545    3 INAACSGFVYALSTAAALIRSGRAKNVLVIGA 34
PRK12746 PRK12746
SDR family oxidoreductase;
3206-3398 3.39e-03

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 43.48  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTA-KALREFEHWKSKVHTIAADINDKE---KLIRELT---KLNVGIT 3278
Cdd:PRK12746   10 LVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAAdETIREIESNGGKAFLIEADLNSIDgvkKLVEQLKnelQIRVGTS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 3279 GI---IHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFNYKIENFIMMSSFTAACGNEGQLNYGVSNAYLE- 3354
Cdd:PRK12746   90 EIdilVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEGRVINISSAEVRLGFTGSIAYGLSKGALNt 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392926054 3355 YQVQRRRRQGKSGCAIQ------WGNWIDTGMATDENVRKFLANLGFLGQ 3398
Cdd:PRK12746  170 MTLPLAKHLGERGITVNtimpgyTKTDINAKLLDDPEIRNFATNSSVFGR 219
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
5186-5230 4.22e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 39.93  E-value: 4.22e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 392926054   5186 PFMDLGIDSL-CMEnLRYSLNKNFDLELTVSEMFENATYQKLQTYV 5230
Cdd:smart00823   38 PFRDLGLDSLmAVE-LRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
3206-3268 6.32e-03

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 42.29  E-value: 6.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926054 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQP--TAKALREFEHwKSKVHTIAADINDKEKLIR 3268
Cdd:cd05323     4 IITGGASGIGLATAKLLLKKGA-KVAILDRNENpgAAAELQAINP-KVKATFVQCDVTSWEQLAA 66
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
6237-6350 6.52e-03

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 43.09  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054 6237 LVFGANGFIGSIVFRLLQEMGMNVIPI----------------------SRASIPSCDITNIKDVQNVFKslgFKKFSVV 6294
Cdd:cd05253     4 LVTGAAGFIGFHVAKRLLERGDEVVGIdnlndyydvrlkearlellgksGGFKFVKGDLEDREALRRLFK---DHEFDAV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392926054 6295 INC---VGVETSAKMNKTSLEQEIVlspktfGSVNILKCLEEFSIEvdKLVnFSSLSSV 6350
Cdd:cd05253    81 IHLaaqAGVRYSLENPHAYVDSNIV------GFLNLLELCRHFGVK--HLV-YASSSSV 130
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1806-1848 8.24e-03

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 38.31  E-value: 8.24e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 392926054  1806 DIDNTTGFFDLGLTSIQAVKLRNAIKSNYP-NASSTCVFDYPSI 1848
Cdd:pfam00550   17 EIDPDTDLFDLGLDSLLAVELIARLEEEFGvEIPPSDLFEHPTL 60
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
3212-3354 9.76e-03

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 41.65  E-value: 9.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926054  3212 SGIGLEIGKFIANNGAEnVILISRRQPTAKALREF-EHWKSKVhtIAADINDKE---KLIRELTKLNVGITGIIHSAGVL 3287
Cdd:pfam13561    6 SGIGWAIARALAEEGAE-VVLTDLNEALAKRVEELaEELGAAV--LPCDVTDEEqveALVAAAVEKFGRLDILVNNAGFA 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926054  3288 KDSK--IERQNKESFNQVFTPKANGFH-VLEEIEKHFNykiEN--FIMMSSFTAACGNEGQLNYGVSNAYLE 3354
Cdd:pfam13561   83 PKLKgpFLDTSREDFDRALDVNLYSLFlLAKAALPLMK---EGgsIVNLSSIGAERVVPNYNAYGAAKAALE 151
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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