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Conserved domains on  [gi|1061385493|ref|NP_001317900|]
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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
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
1889-2282 3.10e-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: 3.10e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1889 NPIGVMAAACRLPGGVSsPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYG-NPVEGGNFItQDVTQFDPSFFKISK 1967
Cdd:cd00833      1 EPIAIVGMACRFPGAAD-PDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGkTYTRRGGFL-DDVDAFDAAFFGISP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1968 SEAELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYQDMMESSSIL----AMLGSMAAVIAGRVNYIFG 2039
Cdd:cd00833     79 REAEAMDPQQRLLLEVAWEALEDAGYspesLAGSRTGVFVGASSSDYLELLARDPDEidayAATGTSRAFLANRISYFFD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2040 CYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDGCV 2119
Cdd:cd00833    159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2120 VLMLelaKP-------NFHYMSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS---PSlAIDYWEAHGTGTPLGDP 2189
Cdd:cd00833    239 VVVL---KRlsdalrdGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAgvdPS-DIDYVEAHGTGTPLGDP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2190 IEFNTLSSIL-------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDINAGSIRLPIIGEDS 2262
Cdd:cd00833    315 IEVEALAKVFggsrsadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEAR 394
                          410       420
                   ....*....|....*....|....*.
gi 1061385493 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 5.41e-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: 5.41e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   13 PNGEDGHEMAENIFLNRNNIALLPVEKNYLSDFREKHPE------VKAALVDGIEYFDDQYFGTGESEAICMDPQQRMLM 86
Cdd:cd00833     13 PGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytRRGGFLDDVDAFDAAFFGISPREAEAMDPQQRLLL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   87 QGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLL-----PPDQYMATGNSASVMCGRITYFLNSRGAAVGIETACSS 161
Cdd:cd00833     93 EVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLardpdEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSS 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  162 SLVAFHLARQAIQSGETKLALVCGANHVGS-RSFHSLYNSHMVSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENN 240
Cdd:cd00833    173 SLVALHLACQSLRSGECDLALVGGVNLILSpDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDG 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  241 LLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSDIRVMS 318
Cdd:cd00833    253 DRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARagVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQ 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  319 P------KSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEME-------LNRVAISSYGF 385
Cdd:cd00833    333 PlligsvKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARpwpapagPRRAGVSSFGF 412

                   ....*....
gi 1061385493  386 GGTNACAII 394
Cdd:cd00833    413 GGTNAHVIL 421
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
3649-3927 6.15e-79

Acyl transferase domain in polyketide synthase (PKS) enzymes;


:

Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 264.26  E-value: 6.15e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3649 MLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLqgDVSLWEILFNTDHYKLLQLTKHMQPIMFCFGYATAQLWLS 3728
Cdd:smart00827    1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLL--GWSLLDVLLGEDGAASLLDTEVAQPALFAVQVALARLLRS 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3729 LGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIAGLGALLAVQREiADEVL-----RKFKVSVATINSP 3803
Cdd:smart00827   79 WGVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLS-EEEVEpllagVPDRVSVAAVNSP 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3804 KQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQEThLVSLRQCLADIKFSAGRTPLVSNVTGQIINT---FS 3880
Cdd:smart00827  158 SSVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPI-LDEFRAALAGLTPRPPRIPFVSTVTGTLIDGaelDD 236
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 1061385493  3881 EAYIVKHTVSAVKFVDCVETLQA-KGVTVWIDAGSAAVLATFVKRIIQ 3927
Cdd:smart00827  237 ADYWVRNLREPVRFADAVRALLAeGGVTVFLEVGPHPVLTGPIKQTLA 284
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
830-1197 7.42e-65

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: 7.42e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  830 IACdyQFAGVEGEKELWDTLLTSRLTTGKISDIRKKQCEGDAGLEV---------GLLKqDISMFDNSFFAIAKDEAEFL 900
Cdd:cd00833      8 MAC--RFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytrrgGFLD-DVDAFDAAFFGISPREAEAM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  901 DPQHRLLLNAAYNALEKSGLT--SIPDAD--LFLAISaHSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGIRGRA 976
Cdd:cd00833     85 DPQQRLLLEVAWEALEDAGYSpeSLAGSRtgVFVGAS-SSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  977 MIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL---KTLLDHHSTNSFSVDGSGFCRSDGVGVIILK 1052
Cdd:cd00833    164 LTVDTACSSSLVALHLACQSLRSGEcDLALVGGVNLILSPDMFVGFskaGMLSPDGRCRPFDADADGYVRGEGVGVVVLK 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1053 ---TAEK-GDS--AVIKiSSAKSH--HCGAVMTPVVSS----ISQLLEEAG----SFSYVEGHGTATSAGDSAE----SM 1112
Cdd:cd00833    244 rlsDALRdGDRiyAVIR-GSAVNQdgRTKGITAPSGEAqaalIRRAYARAGvdpsDIDYVEAHGTGTPLGDPIEvealAK 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1113 AYQKLGSE---LIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVHNILPSEHIRNNE-NIRLPFVAEE----KQI 1184
Cdd:cd00833    323 VFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEEsPLRVPTEARPwpapAGP 402
                          410
                   ....*....|...
gi 1061385493 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 4.83e-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: 4.83e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTA----KALREFEHWKSKVHTIAADINDKE---KLIRELTKLNV 3275
Cdd:smart00822    1 GTYLITGGLGGLGRALARWLAERGARRLVLLSRSGPDApgaaALLAELEAAGARVTVVACDVADRDalaAVLAAIPAVEG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3276 GITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHfnYKIENFIMMSSFTAACGNEGQLNYGVSNAYLEY 3355
Cdd:smart00822   81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTAD--LPLDFFVLFSSIAGVLGSPGQANYAAANAFLDA 158
                           170       180
                    ....*....|....*....|..
gi 1061385493  3356 QVQRRRRQGKSGCAIQWGNWID 3377
Cdd:smart00822  159 LAEYRRARGLPALSIAWGAWAE 180
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
4359-4569 1.17e-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: 1.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4359 IYLVHAIGGTIYPYYSFLQIFPKDISLYGIEF----DLKYPSNDLRELAHFYAEEIAAHAGNKRIFVMGHSMGGIMSREI 4434
Cdd:COG3319    604 LFCVHPAGGNVLCYRPLARALGPDRPVYGLQApgldGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEM 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4435 VAELKIWGYDIPFVMLFDSWV--LRTNELDIENIKQFITYVFSGLP-----------DSEHRINRAIKLA---------- 4491
Cdd:COG3319    684 ARQLEAQGEEVALLVLLDSYApgALARLDEAELLAALLRDLARGVDlpldaeelralDPEERLARLLERLreaglpagld 763
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4492 ---------------QLLREYKTSVSDTKLYLFkskqlgdaafkkavRSDLNEELSRSMTCNGFDELSLQPVETYLIDGD 4556
Cdd:COG3319    764 aerlrrllrvfranlRALRRYRPRPYDGPVLLF--------------RAEEDPPGRADDPALGWRPLVAGGLEVHDVPGD 829
                          250
                   ....*....|...
gi 1061385493 4557 HESCLKAENLKKV 4569
Cdd:COG3319    830 HFSMLREPHVAEL 842
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
1544-1759 2.16e-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: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1544 HVVDSKIVLPGATSIRL----VHQLNGKPT-VELSNIDFLN--KITPSEAPSV---VKIEEQDGLEKLVF---------- 1603
Cdd:pfam14765   33 HRVGGTVVLPGAGYLEMaleaARQLFGGSGaVALRDVSILKalVLPEDDPVEVqtsLTPEEDGADSWWEFeifsragggw 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1604 -------------GETDAISFKLTELQNFNPIPNERLNAEVHHtdnIYERFANSHLTYRNEFQMVDSLKY--TMGKGEVR 1668
Cdd:pfam14765  113 ewtlhatgtvrlaPGEPAAPVDLESLPARCAQPADPRSVSSAE---FYERLAARGLFYGPAFQGLRRIWRgdGEALAEAR 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1669 FVSMKDLD--------ILIDGTLQAIVGCYFFENTNDNSPFVPFTIDQLSILNGDISQKQLHAVLKYDSSGN-FINGDAT 1739
Cdd:pfam14765  190 LPEAAAGGespyllhpALLDAALQLLGAALPAEAEHADQAYLPVGIERLRIYRSLPPGEPLWVHARLERRGGrTIVGDLT 269
                          250       260
                   ....*....|....*....|
gi 1061385493 1740 VYDALGNIILHISNVTFKRL 1759
Cdd:pfam14765  270 LVDEDGRVVARIEGLRLRRV 289
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2943-3024 5.91e-11

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: 5.91e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  2943 ATVDRTEIRRKVSLAVFDLATETL---SAEDLQ-SKGFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDELS 3018
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLghaAAEAIDpDRPFRDLGLDSLMAVELRNRLEAAT--GLRLPATLVFDHPTPAALA 79

                    ....*.
gi 1061385493  3019 DHIVRK 3024
Cdd:smart00823   80 EHLAAE 85
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
3994-4216 2.39e-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: 2.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3994 DEFELLEGHQLNGKIVVAGA-Y---------QLFKIDQLVKLKaagmelmlkNVKFLKPWYIEDNREYQIQ--------- 4054
Cdd:pfam14765   25 ADLPWLRDHRVGGTVVLPGAgYlemaleaarQLFGGSGAVALR---------DVSILKALVLPEDDPVEVQtsltpeedg 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4055 -----------WNSDMTiELIVNSVIVCSLEVEPQNSVLKLETI------SENEKPFEVHDFYETLFRNGLQYDSGFRRI 4117
Cdd:pfam14765   96 adswwefeifsRAGGGW-EWTLHATGTVRLAPGEPAAPVDLESLparcaqPADPRSVSSAEFYERLAARGLFYGPAFQGL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4118 ESARRSDKRCFSQIKSS----PFAWP------LIDSAMHSITASVVP--RRPDCYFLPVAMGSVTMKDTNSFTLPnLHAQ 4185
Cdd:pfam14765  175 RRIWRGDGEALAEARLPeaaaGGESPyllhpaLLDAALQLLGAALPAeaEHADQAYLPVGIERLRIYRSLPPGEP-LWVH 253
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1061385493 4186 TVITSETDKFIQVNVALLAGD-TPICEVRNMT 4216
Cdd:pfam14765  254 ARLERRGGRTIVGDLTLVDEDgRVVARIEGLR 285
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2790-2867 5.85e-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: 5.85e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493  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 3.05e-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: 3.05e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1061385493  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 1.15e-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: 51.78  E-value: 1.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1061385493 3485 IKEKVSSILMCSPTKLKNNKNIM-DMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLEKLAAHI 3549
Cdd:COG0236     10 LAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4268-4325 1.46e-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: 51.02  E-value: 1.46e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061385493 4268 EKVINVFSKILGRN---VAPTDKFESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLK 4325
Cdd:pfam00550    1 ERLRELLAEVLGVPaeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
KAsynt_C_assoc super family cl24694
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
376-431 3.98e-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: 3.98e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1061385493  376 NRVAISSYGFGGTNACAIIEKPEKPSLVQKESYAESNVLFLSAKSHESLKLQIEEY 431
Cdd:pfam16197   25 GIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKALLEKL 80
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
730-803 5.25e-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: 47.16  E-value: 5.25e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493  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 ...
2267-2347 6.22e-03

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: 39.45  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2267 AGISSFGVSGTNAAAI-AFNDNNKLEPYIPIHKYYILPISAKNQISLDNLEKQILSvIPLTDVPICNIASALANNRSHFT 2345
Cdd:pfam16197   27 VGVNSFGFGGANAHVIlKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKALLEKLEN-HLDDAEFLSLLNDIHSLPISGHP 105

                   ..
gi 1061385493 2346 IR 2347
Cdd:pfam16197  106 YR 107
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
1889-2282 3.10e-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: 3.10e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1889 NPIGVMAAACRLPGGVSsPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYG-NPVEGGNFItQDVTQFDPSFFKISK 1967
Cdd:cd00833      1 EPIAIVGMACRFPGAAD-PDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGkTYTRRGGFL-DDVDAFDAAFFGISP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1968 SEAELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYQDMMESSSIL----AMLGSMAAVIAGRVNYIFG 2039
Cdd:cd00833     79 REAEAMDPQQRLLLEVAWEALEDAGYspesLAGSRTGVFVGASSSDYLELLARDPDEidayAATGTSRAFLANRISYFFD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2040 CYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDGCV 2119
Cdd:cd00833    159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2120 VLMLelaKP-------NFHYMSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS---PSlAIDYWEAHGTGTPLGDP 2189
Cdd:cd00833    239 VVVL---KRlsdalrdGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAgvdPS-DIDYVEAHGTGTPLGDP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2190 IEFNTLSSIL-------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDINAGSIRLPIIGEDS 2262
Cdd:cd00833    315 IEVEALAKVFggsrsadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEAR 394
                          410       420
                   ....*....|....*....|....*.
gi 1061385493 2263 ELVS------AGISSFGVSGTNAAAI 2282
Cdd:cd00833    395 PWPApagprrAGVSSFGFGGTNAHVI 420
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1887-2354 5.21e-112

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: 5.21e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1887 AENPIGVMAAACRLPGgVSSPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNPV---EGGnFItQDVTQFDPSFF 1963
Cdd:COG3321      2 ADEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTyvrWGG-FL-DDVDEFDALFF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1964 KISKSEAELIDPQQRLLLECVQECLENSGVIET----SNVGVFVGLMEKEYQDMM----ESSSILAMLGSMAAVIAGRVN 2035
Cdd:COG3321     79 GISPREAEAMDPQQRLLLEVAWEALEDAGYDPEslagSRTGVFVGASSNDYALLLladpEAIDAYALTGNAKSVLAGRIS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2036 YIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRS 2115
Cdd:COG3321    159 YKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2116 DGCVVLMLE------------LAkpnfhymsTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQ---SPSlAIDYWEAH 2180
Cdd:COG3321    239 EGVGVVVLKrlsdalrdgdriYA--------VIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADagvDPA-TVDYVEAH 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2181 GTGTPLGDPIEFNTLSSIL-------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDIN--AG 2251
Cdd:COG3321    310 GTGTPLGDPIEAAALTAAFgqgrpadQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDfeNS 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2252 SIRLPiigedSELVS---------AGISSFGVSGTNAAAIafndnnkLE--------PYIPIHKYYILPISAKNQISLDN 2314
Cdd:COG3321    390 PFYVN-----TELRPwpagggprrAGVSSFGFGGTNAHVV-------LEeapaaapaAAAAARPPQLLVLSAKTEEALRA 457
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1061385493 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 5.41e-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: 5.41e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   13 PNGEDGHEMAENIFLNRNNIALLPVEKNYLSDFREKHPE------VKAALVDGIEYFDDQYFGTGESEAICMDPQQRMLM 86
Cdd:cd00833     13 PGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytRRGGFLDDVDAFDAAFFGISPREAEAMDPQQRLLL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   87 QGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLL-----PPDQYMATGNSASVMCGRITYFLNSRGAAVGIETACSS 161
Cdd:cd00833     93 EVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLardpdEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSS 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  162 SLVAFHLARQAIQSGETKLALVCGANHVGS-RSFHSLYNSHMVSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENN 240
Cdd:cd00833    173 SLVALHLACQSLRSGECDLALVGGVNLILSpDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDG 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  241 LLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSDIRVMS 318
Cdd:cd00833    253 DRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARagVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQ 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  319 P------KSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEME-------LNRVAISSYGF 385
Cdd:cd00833    333 PlligsvKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARpwpapagPRRAGVSSFGF 412

                   ....*....
gi 1061385493  386 GGTNACAII 394
Cdd:cd00833    413 GGTNAHVIL 421
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
54-600 1.89e-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: 1.89e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   54 AALVDGIEYFDDQYFGTGESEAICMDPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLLPP-----DQY 128
Cdd:COG3321     64 GGFLDDVDEFDALFFGISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLAdpeaiDAY 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  129 MATGNSASVMCGRITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNG 207
Cdd:COG3321    144 ALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNlMLTPESFILFSKGGMLSPDG 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  208 RLAAFDRSANGFVRAESFAVAVLcsKQF--AEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKD 283
Cdd:COG3321    224 RCRAFDADADGYVRGEGVGVVVL--KRLsdALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADagVDPA 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  284 SVQLVTCHGTGTKLGDQVELTAINRSFKSD------IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPS 357
Cdd:COG3321    302 TVDYVEAHGTGTPLGDPIEAAALTAAFGQGrpadqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPN 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  358 EDLGEDKSMGFVNEE-MELN------RVAISSYGFGGTNACAIIEKPEKPSLVQKESYAESNVLFLSAKSHESLKLQIEE 430
Cdd:COG3321    382 PHIDFENSPFYVNTElRPWPagggprRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAAR 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  431 YTQFMAQ-SDSAMEDILYTVNERKTKYDFRAAVFGKDNEEIARKL------QDGDYSLTNLQESTFEVEF---GEGNEKL 500
Cdd:COG3321    462 LAAFLEAhPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLralaagEAAPGVVTGAAAAAPKVAFlfpGQGSQYV 541
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  501 WLLRMLYEKNETFHSTVDKYCK-LAETCGFPeaRTALFFP----FKLTLT----PLTYNVsrlisSMATFELLVQYNTLP 571
Cdd:COG3321    542 GMGRELYETEPVFRAALDECDAlLRPHLGWS--LREVLFPdeeeSRLDRTevaqPALFAV-----EYALARLWRSWGVRP 614
                          570       580
                   ....*....|....*....|....*....
gi 1061385493  572 NKLRGKGLGQIFCLAVAKVITFESAVQLI 600
Cdd:COG3321    615 DAVIGHSVGEYAAACVAGVLSLEDALRLV 643
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
1891-2282 8.49e-82

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: 8.49e-82
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  1891 IGVmaaACRLPGgVSSPSELWELLKIGKNassripatrvptrntlisgskygnpveggnfitqDVTQFDPSFFKISKSEA 1970
Cdd:smart00825    4 VGM---SCRFPG-ADDPEEFWDLLLAGLD----------------------------------DVDLFDAAFFGISPREA 45
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  1971 ELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYqdmmesssilamlgsmaaviagrvnyifgcygpSVT 2046
Cdd:smart00825   46 EAMDPQQRLLLEVAWEALEDAGIdpesLRGSRTGVFVGVSSSDY---------------------------------SVT 92
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  2047 IDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILN-EKGQGLrTNGKMLSQHGMSLSFDSRASGYGRSDGCVVLMLE- 2124
Cdd:smart00825   93 VDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSpDTFVGL-SRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKr 171
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  2125 -----------LAkpnfhymsTIQSVNVNHGGRSVSLTAPNGVAHkmlltsvinqspslaidyweahgtgtplgdpiefn 2193
Cdd:smart00825  172 lsdalrdgdpiLA--------VIRGSAVNQDGRSNGITAPSGPAQ----------------------------------- 208
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  2194 tlssilqnIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDINAGSIRLPIIGEDSELVS------A 2267
Cdd:smart00825  209 --------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWPPpgrprrA 280
                           410
                    ....*....|....*
gi 1061385493  2268 GISSFGVSGTNAAAI 2282
Cdd:smart00825  281 GVSSFGFGGTNAHVI 295
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
3649-3927 6.15e-79

Acyl transferase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 264.26  E-value: 6.15e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3649 MLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLqgDVSLWEILFNTDHYKLLQLTKHMQPIMFCFGYATAQLWLS 3728
Cdd:smart00827    1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLL--GWSLLDVLLGEDGAASLLDTEVAQPALFAVQVALARLLRS 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3729 LGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIAGLGALLAVQREiADEVL-----RKFKVSVATINSP 3803
Cdd:smart00827   79 WGVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLS-EEEVEpllagVPDRVSVAAVNSP 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3804 KQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQEThLVSLRQCLADIKFSAGRTPLVSNVTGQIINT---FS 3880
Cdd:smart00827  158 SSVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPI-LDEFRAALAGLTPRPPRIPFVSTVTGTLIDGaelDD 236
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 1061385493  3881 EAYIVKHTVSAVKFVDCVETLQA-KGVTVWIDAGSAAVLATFVKRIIQ 3927
Cdd:smart00827  237 ADYWVRNLREPVRFADAVRALLAeGGVTVFLEVGPHPVLTGPIKQTLA 284
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3617-3971 1.02e-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: 1.02e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3617 VVGKSIRDVVSKIKEAAPQQIKLC------QESSKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLqgDV 3690
Cdd:COG3321    494 VVASSREELAAKLRALAAGEAAPGvvtgaaAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALDECDALLRPHL--GW 571
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3691 SLWEILFNTDHYKLLQLTKHMQPIMFCFGYATAQLWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAME 3770
Cdd:COG3321    572 SLREVLFPDEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLEDALRLVAARGRLMQ 651
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3771 NIAGLGALLAVQ--REIADEVLRKF-KVSVATINSPKQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQETh 3847
Cdd:COG3321    652 ALPGGGAMLAVGlsEEEVEALLAGYdGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARRLPVSHAFHSPLMEPA- 730
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3848 LVSLRQCLADIKFSAGRTPLVSNVTGQIINT--FSEAYIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:COG3321    731 LEEFRAALAGVTPRAPRIPLISNVTGTWLTGeaLDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQC 810
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1061385493 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 1.52e-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: 1.52e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1889 NPIGVMAAACRLPGGVSsPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNPVEGGNFITQDVTQFDPSFFKISKS 1968
Cdd:pfam00109    1 EPVAIVGMGCRFPGGND-PEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKWGGLDDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1969 EAELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYQDMMESSSI-------LAMLGSMAAVIAGRVNYI 2037
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGItpdsLDGSRTGVFIGSGIGDYAALLLLDEDggprrgsPFAVGTMPSVIAGRISYF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2038 FGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDG 2117
Cdd:pfam00109  160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239

                   ....*..
gi 1061385493 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 1.98e-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: 1.98e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493    57 VDGIEYFDDQYFGTGESEAICMDPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYkdllppdqymatgnsas 136
Cdd:smart00825   27 LDDVDLFDAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY----------------- 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   137 vmcgrityflnsrgaAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNGRLAAFDRS 215
Cdd:smart00825   90 ---------------SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLSPDGRCKTFDAS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   216 ANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQyevqlealknidkdsvqlvtchgtgt 295
Cdd:smart00825  155 ADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ-------------------------- 208
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   296 klgdqveltainrsfksdIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEME- 374
Cdd:smart00825  209 ------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTp 270
                           330       340
                    ....*....|....*....|....*..
gi 1061385493   375 ------LNRVAISSYGFGGTNACAIIE 395
Cdd:smart00825  271 wpppgrPRRAGVSSFGFGGTNAHVILE 297
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
6-236 3.11e-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: 3.11e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493    6 VGSWAKIPNGEDGHEMAENIFLNRNNIALLP-----VEKNYL--SDFREKHPEVKAALvDGIEYFDDQYFGTGESEAICM 78
Cdd:pfam00109    6 VGMGCRFPGGNDPEEFWENLLEGRDGISEIPadrwdPDKLYDppSRIAGKIYTKWGGL-DDIFDFDPLFFGISPREAERM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   79 DPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLL-------PPDQYM-ATGNSASVMCGRITYFLNSRG 150
Cdd:pfam00109   85 DPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLlldedggPRRGSPfAVGTMPSVIAGRISYFLGLRG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  151 AAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNGRLAAFDRSANGFVRAESFAVAV 229
Cdd:pfam00109  165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVV 244

                   ....*..
gi 1061385493  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 7.42e-65

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: 7.42e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  830 IACdyQFAGVEGEKELWDTLLTSRLTTGKISDIRKKQCEGDAGLEV---------GLLKqDISMFDNSFFAIAKDEAEFL 900
Cdd:cd00833      8 MAC--RFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytrrgGFLD-DVDAFDAAFFGISPREAEAM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  901 DPQHRLLLNAAYNALEKSGLT--SIPDAD--LFLAISaHSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGIRGRA 976
Cdd:cd00833     85 DPQQRLLLEVAWEALEDAGYSpeSLAGSRtgVFVGAS-SSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  977 MIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL---KTLLDHHSTNSFSVDGSGFCRSDGVGVIILK 1052
Cdd:cd00833    164 LTVDTACSSSLVALHLACQSLRSGEcDLALVGGVNLILSPDMFVGFskaGMLSPDGRCRPFDADADGYVRGEGVGVVVLK 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1053 ---TAEK-GDS--AVIKiSSAKSH--HCGAVMTPVVSS----ISQLLEEAG----SFSYVEGHGTATSAGDSAE----SM 1112
Cdd:cd00833    244 rlsDALRdGDRiyAVIR-GSAVNQdgRTKGITAPSGEAqaalIRRAYARAGvdpsDIDYVEAHGTGTPLGDPIEvealAK 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1113 AYQKLGSE---LIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVHNILPSEHIRNNE-NIRLPFVAEE----KQI 1184
Cdd:cd00833    323 VFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEEsPLRVPTEARPwpapAGP 402
                          410
                   ....*....|...
gi 1061385493 1185 DRSAIVSFGITGT 1197
Cdd:cd00833    403 RRAGVSSFGFGGT 415
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
830-1287 3.14e-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: 3.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  830 IACdyQFAGVEGEKELWDTLLTSRLTTGKISDIR---KKQCEGDAGLEV-------GLLKqDISMFDNSFFAIAKDEAEF 899
Cdd:COG3321     11 MAC--RFPGADDPEEFWRNLRAGRDAITEVPADRwdaDAYYDPDPDAPGktyvrwgGFLD-DVDEFDALFFGISPREAEA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  900 LDPQHRLLLNAAYNALEKSGltsIPDADL-------FLAISaHSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGI 972
Cdd:COG3321     88 MDPQQRLLLEVAWEALEDAG---YDPESLagsrtgvFVGAS-SNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  973 RGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL-KT-LL--DHHStNSFSVDGSGFCRSDGVG 1047
Cdd:COG3321    164 RGPSVTVDTACSSSLVAVHLACQSLRSGEcDLALAGGVNLMLTPESFILFsKGgMLspDGRC-RAFDADADGYVRGEGVG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1048 VIILKTAEK----GDS--AVIKiSSAKSH--HCGAVMTPVVSS----ISQLLEEAG----SFSYVEGHGTATSAGDSAE- 1110
Cdd:COG3321    243 VVVLKRLSDalrdGDRiyAVIR-GSAVNQdgRSNGLTAPNGPAqaavIRRALADAGvdpaTVDYVEAHGTGTPLGDPIEa 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1111 ---SMAYQKLGSE---LIMSSVKAQFGHCEVASGLIQLMKVS-SIgKHGIIPsivhnilPSEHIRN-NENI---RLPF-V 1178
Cdd:COG3321    322 aalTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVlAL-RHGVLP-------PTLHFETpNPHIdfeNSPFyV 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1179 AEE----KQID---RSAIVSFGITGTKT-VVTTE--RVSQLNVDNIQNCYLLPVSAKTKDGLKKACLSLIEMIDNSCE-S 1247
Cdd:COG3321    394 NTElrpwPAGGgprRAGVSSFGFGGTNAhVVLEEapAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDlD 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1061385493 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 ...
825-1056 1.71e-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: 1.71e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  825 SDINVIACDYQFAGVEGEKELWDTLLTSRLTTGKISDIR---------KKQCEGDAGLEVGLLkQDISMFDNSFFAIAKD 895
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRwdpdklydpPSRIAGKIYTKWGGL-DDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  896 EAEFLDPQHRLLLNAAYNALEKSGLT--SIPDAD--LFLAISAH--SEYRALAEKHINELDERLWMGTVHSMVAGRLAVL 969
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITpdSLDGSRtgVFIGSGIGdyAALLLLDEDGGPRRGSPFAVGTMPSVIAGRISYF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  970 MGIRGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL---KTLLDHHSTNSFSVDGSGFCRSDG 1045
Cdd:pfam00109  160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEaDVALAGGVNLLLTPLGFAGFsaaGMLSPDGPCKAFDPFADGFVRGEG 239
                          250
                   ....*....|.
gi 1061385493 1046 VGVIILKTAEK 1056
Cdd:pfam00109  240 VGAVVLKRLSD 250
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
3203-3377 4.83e-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: 4.83e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTA----KALREFEHWKSKVHTIAADINDKE---KLIRELTKLNV 3275
Cdd:smart00822    1 GTYLITGGLGGLGRALARWLAERGARRLVLLSRSGPDApgaaALLAELEAAGARVTVVACDVADRDalaAVLAAIPAVEG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3276 GITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHfnYKIENFIMMSSFTAACGNEGQLNYGVSNAYLEY 3355
Cdd:smart00822   81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTAD--LPLDFFVLFSSIAGVLGSPGQANYAAANAFLDA 158
                           170       180
                    ....*....|....*....|..
gi 1061385493  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 2.14e-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: 2.14e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3200 PITGNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWK---SKVHTIAADINDKE---KLIRELTKL 3273
Cdd:cd05274    148 GLDGTYLITGGLGGLGLLVARWLAARGARHLVLLSRRGPAPRAAARAALLRaggARVSVVRCDVTDPAalaALLAELAAG 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3274 nVGITGIIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHfnyKIENFIMMSSFTAACGNEGQLNYGVSNAY 3352
Cdd:cd05274    228 -GPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGaLNLHELTPDL---PLDFFVLFSSVAALLGGAGQAAYAAANAF 303
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1061385493 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 3.31e-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: 3.31e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   830 IACdyQFAGVEGEKELWDTLLtsrlttgkisdirkkqcegdAGLEvgllkqDISMFDNSFFAIAKDEAEFLDPQHRLLLN 909
Cdd:smart00825    6 MSC--RFPGADDPEEFWDLLL--------------------AGLD------DVDLFDAAFFGISPREAEAMDPQQRLLLE 57
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   910 AAYNALEKSGltsIPDADLflaisahseyralaekhinelderlwMGTvhsmvagRLAVLMGIRGR--AMIVDTTCSSVA 987
Cdd:smart00825   58 VAWEALEDAG---IDPESL--------------------------RGS-------RTGVFVGVSSSdySVTVDTACSSSL 101
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   988 TALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSLKTL--L--DHHStNSFSVDGSGFCRSDGVGVIILKTAEK----GD 1058
Cdd:smart00825  102 VALHLACQSLRSGEcDMALAGGVNLILSPDTFVGLSRAgmLspDGRC-KTFDASADGYVRGEGVGVVVLKRLSDalrdGD 180
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  1059 S--AVIKiSSAkSHHCGA---VMTPvvSSISQLLeeagsfsyveghgtatsagdsaesmayqkLGselimsSVKAQFGHC 1133
Cdd:smart00825  181 PilAVIR-GSA-VNQDGRsngITAP--SGPAQLL-----------------------------IG------SVKSNIGHL 221
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061385493  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 1.87e-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: 1.87e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPT----AKALREFEHWKSKVHTIAADINDK---EKLIRELTKLNV 3275
Cdd:pfam08659    1 GTYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPrpdaQALIAELEARGVEVVVVACDVSDPdavAALLAEIKAEGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3276 GITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFNykIENFIMMSSFTAACGNEGQLNYGVSNAYLEY 3355
Cdd:pfam08659   81 PIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEP--LDFFVLFSSIAGLLGSPGQANYAAANAFLDA 158
                          170       180
                   ....*....|....*....|..
gi 1061385493 3356 QVQRRRRQGKSGCAIQWGNWID 3377
Cdd:pfam08659  159 LAEYRRSQGLPATSINWGPWAE 180
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
3644-3925 2.09e-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: 2.09e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3644 SKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQsclkKCDEYLQgdVSLWEILFNTDhYKLLQLTKHMQPIMFCFGYATA 3723
Cdd:TIGR00128    1 MKIAYVFPGQGSQTVGMGKDLYEQYPIAKELFD----QASEALG--YDLKKLCQEGP-AEELNKTQYTQPALYVVSAILY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3724 QLWL-SLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENI-----AGLGALLAVQREIADEVLRKFK--- 3794
Cdd:TIGR00128   74 LKLKeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAvpeggGAMAAVIGLDEEQLAQACEEATend 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3795 VSVATINSPKQVVFAGTKSVLDAALAFVKGQG-KQATYVNQQYPFHSNLIQETHLvSLRQCLADIKFSAGRTPLVSNVTG 3873
Cdd:TIGR00128  154 VDLANFNSPGQVVISGTKDGVEAAAALFKEMGaKRAVPLEVSGAFHSRFMKPAAE-KFAETLEACQFNDPTVPVISNVDA 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1061385493 3874 QIINTFSEA--YIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:TIGR00128  233 KPYTNGDRIkeKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGLIKRI 286
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
129-390 4.26e-30

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 126.73  E-value: 4.26e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  129 MATGNSAsvmcgrITYflNSRGAAVGIETACSSSLVAFHLARQAIQSGETKlALVCGA--------NHVGSRSFHSLYNS 200
Cdd:PTZ00050   146 MAAGLVA------IKH--KLKGPSGSAVTACATGAHCIGEAFRWIKYGEAD-IMICGGteasitpvSFAGFSRMRALCTK 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  201 HMVSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNP-----ISQYEVQLE 275
Cdd:PTZ00050   217 YNDDPQRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAH--HITAPHPdgrgaRRCMENALK 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  276 ALKNIDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSD----IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQL 351
Cdd:PTZ00050   295 DGANININDVDYVNAHATSTPIGDKIELKAIKKVFGDSgapkLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTI 374
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1061385493  352 HLELPSEDLGEDKSMGFVNEEMELNRVAIS-SYGFGGTNA 390
Cdd:PTZ00050   375 NLENPDAECDLNLVQGKTAHPLQSIDAVLStSFGFGGVNT 414
Acyl_transf_1 pfam00698
Acyl transferase domain;
3647-3924 8.18e-30

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 123.35  E-value: 8.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3647 VLMLTGQGSQYPMMGRQLVENYEIFRTTLqsclKKCDEYL--QGDVSLWEILFNTDHyKLLQLTKHMQPIMFCFGYATAQ 3724
Cdd:pfam00698    1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVI----DRADEAFkpQYGFSVSDVLRNNPE-GTLDGTQFVQPALFAMQIALAA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3725 LWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIAGLGALLAVQREIADEVLRKF-KVSVATINSP 3803
Cdd:pfam00698   76 LLQSYGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPdDVVGAVVNSP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3804 KQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIqETHLVSLRQCLADIKFSAGRTPLVSNVTGQIIN--TFSE 3881
Cdd:pfam00698  156 RSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQM-DAIAPALLSALADIAPRTPRVPFISSTSIDPSDqrTLSA 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1061385493 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 2.45e-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: 123.96  E-value: 2.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  126 DQYMA------TGNSASVMCGRITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGanhVGSRSFHSLYN 199
Cdd:TIGR02813  167 DQYIHweensfPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---VCTDNSPFMYM 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  200 SHMVSP----NGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPisqyEVQLE 275
Cdd:TIGR02813  244 SFSKTPafttNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRP----EGQAK 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  276 ALKNIDKD------SVQLVTCHGTGTKLGDQVELTAINRSFKSD------IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQ 343
Cdd:TIGR02813  320 ALKRAYDDagfaphTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALH 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  344 HGIIPNQLHLELPSEDLGEDKSMGFVNEEMEL---------NRVAISSYGFGGTNACAIIEK--PEKPSLVQKESYAESN 412
Cdd:TIGR02813  400 HKVLPPTINVDQPNPKLDIENSPFYLNTETRPwmqredgtpRRAGISSFGFGGTNFHMVLEEysPKHQRDDQYRQRAVAQ 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  413 VLFLSAKSHESLklqIEEYTQFMAQSDSAMEDILYTVNERKTKYDFRA-----AVFG---KDNEEIARKLQDgdySLTNL 484
Cdd:TIGR02813  480 TLLFTAANEKAL---VSSLKDWKNKLSAKADDQPYAFNALAVENTLRTiavalARLGfvaKNADELITMLEQ---AITQL 553
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  485 QESTFE---VEFGEGNEKLWLLRMLYEKNETFHSTVDKYCKLAE--TCGFPEARTAL------FFPFKLT-LTPLTYNVS 552
Cdd:TIGR02813  554 EAKSCEewqLPSGISYRKSALVVESGKVAALFAGQGSQYLNMGRelACNFPEVRQAAadmdsvFTQAGKGaLSPVLYPIP 633
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  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 7.56e-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: 112.41  E-value: 7.56e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1885 RLAENPIGVMAAAcRLPGGVSSPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNP--VEGGNFITQdvTQFDPSF 1962
Cdd:TIGR02813    3 RLKDMPIAIVGMA-SIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADKsyCKRGGFLPE--VDFNPME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1963 FKISKSEAELIDPQQRLLLECVQECLENSGVIETSN---VGVFVG----------------------------------- 2004
Cdd:TIGR02813   80 FGLPPNILELTDISQLLSLVVAKEVLNDAGLPDGYDrdkIGITLGvgggqkqssslnarlqypvlkkvfkasgvededse 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2005 LMEKEYQDMM---ESSSILAMLGSmaaVIAGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGV--- 2078
Cdd:TIGR02813  160 MLIKKFQDQYihwEENSFPGSLGN---VISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVctd 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2079 ----NLILNEKGQGLRTNGKMlsqhgMSLSFDSRASGYGRSDGCVVLM-LELAKPNFHYM-STIQSVNVNHGGRSVSLTA 2152
Cdd:TIGR02813  237 nspfMYMSFSKTPAFTTNEDI-----QPFDIDSKGMMIGEGIGMMALKrLEDAERDGDRIyAVIKGVGASSDGKFKSIYA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2153 PNGVAHKMLLTSVINQS---PSlAIDYWEAHGTGTPLGDPIEFNTLSSI-------LQNIIIGSVKASLGHGEASAGTCG 2222
Cdd:TIGR02813  312 PRPEGQAKALKRAYDDAgfaPH-TCGLIEAHGTGTAAGDVAEFGGLVSVfsqdndqKQHIALGSVKSQIGHTKSTAGTAG 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2223 LLKLFLMLTYQYVPTLIHFHVLNKDINA--------GSIRLPIIGEDSELVSAGISSFGVSGTNAAAIafndnnkLEPYI 2294
Cdd:TIGR02813  391 MIKAVLALHHKVLPPTINVDQPNPKLDIenspfylnTETRPWMQREDGTPRRAGISSFGFGGTNFHMV-------LEEYS 463
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1061385493 2295 PIH----KY------YILPISAKNQISLdnlekqilsVIPLTDVPicNIASALANNRS-HFtirNALIVSNS 2355
Cdd:TIGR02813  464 PKHqrddQYrqravaQTLLFTAANEKAL---------VSSLKDWK--NKLSAKADDQPyAF---NALAVENT 521
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
4359-4569 1.17e-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: 1.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4359 IYLVHAIGGTIYPYYSFLQIFPKDISLYGIEF----DLKYPSNDLRELAHFYAEEIAAHAGNKRIFVMGHSMGGIMSREI 4434
Cdd:COG3319    604 LFCVHPAGGNVLCYRPLARALGPDRPVYGLQApgldGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEM 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4435 VAELKIWGYDIPFVMLFDSWV--LRTNELDIENIKQFITYVFSGLP-----------DSEHRINRAIKLA---------- 4491
Cdd:COG3319    684 ARQLEAQGEEVALLVLLDSYApgALARLDEAELLAALLRDLARGVDlpldaeelralDPEERLARLLERLreaglpagld 763
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4492 ---------------QLLREYKTSVSDTKLYLFkskqlgdaafkkavRSDLNEELSRSMTCNGFDELSLQPVETYLIDGD 4556
Cdd:COG3319    764 aerlrrllrvfranlRALRRYRPRPYDGPVLLF--------------RAEEDPPGRADDPALGWRPLVAGGLEVHDVPGD 829
                          250
                   ....*....|...
gi 1061385493 4557 HESCLKAENLKKV 4569
Cdd:COG3319    830 HFSMLREPHVAEL 842
PLN02752 PLN02752
[acyl-carrier protein] S-malonyltransferase
3643-3925 7.56e-16

[acyl-carrier protein] S-malonyltransferase


Pssm-ID: 215401 [Multi-domain]  Cd Length: 343  Bit Score: 82.50  E-value: 7.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3643 SSKCVLMLTGQGSQYPMMGRQLVENyeifrTTLQSCLKKCDEYLQGDvsLWEILFNTDHYKLlQLTKHMQPIMFCFGYAT 3722
Cdd:PLN02752    37 KPTTAFLFPGQGAQAVGMGKEAAEV-----PAAKALFDKASEILGYD--LLDVCVNGPKEKL-DSTVVSQPAIYVASLAA 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3723 AQLWLSLGIVP------DYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIA-----------GLG--ALLAVQR 3783
Cdd:PLN02752   109 VEKLRARDGGQavidsvDVCAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAAdagpsgmvsviGLDsdKVQELCA 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3784 EIADEVLRKFKVSVATINSPKQVVFAGTKSVLDAALAFVKGQG-KQATYVNQQYPFHSNLIqETHLVSLRQCLADIKFSA 3862
Cdd:PLN02752   189 AANEEVGEDDVVQIANYLCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFM-EPAVDALEAALAAVEIRT 267
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 3863 GRTPLVSNVTGQIintFSEAYIVKHT-----VSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:PLN02752   268 PRIPVISNVDAQP---HSDPATIKKIlarqvTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGIVKRV 332
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
867-1206 8.10e-16

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 83.24  E-value: 8.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  867 CEGDAGLEvgllkqDISMFDNSFFA--IAK-----DEAEFLDPQH--------RLLLNAAYNALEKSGLT-SIPDADLFl 930
Cdd:PRK08439    27 CNGECGIK------KITLFDASDFPvqIAGeitdfDPTEVMDPKEvkkadrfiQLGLKAAREAMKDAGFLpEELDAERF- 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  931 AISAHSEYRALA--EKHINELDER--------LWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREG 1000
Cdd:PRK08439   100 GVSSASGIGGLPniEKNSIICFEKgprkispfFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLG 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1001 ---RKFAIVATSQL----IQSSKWLYSLKTLLDH--HSTNSFSVDGSGFCRSDGVGVIILKTAEKGDSAVIKI------- 1064
Cdd:PRK08439   180 gadKMLVVGAESAIcpvgIGGFAAMKALSTRNDDpkKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIyaeiigf 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1065 -SSAKSHHcgaVMTPVV----SSISQLLEEAGS--FSYVEGHGTATSAGDSAESMAYQKL--GSELI--MSSVKAQFGHC 1133
Cdd:PRK08439   260 gESGDANH---ITSPAPegplRAMKAALEMAGNpkIDYINAHGTSTPYNDKNETAALKELfgSKEKVppVSSTKGQIGHC 336
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 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 3.73e-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: 83.52  E-value: 3.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  950 DERLWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVATSQLIQSSKWLYSLKTLLDHHS 1029
Cdd:TIGR02813  173 EENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFT 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1030 TNS----FSVDGSGFCRSDGVGVIILK---TAEK-GDS--AVIK-ISSAKSHHCGAVMTP----VVSSISQLLEEAG--- 1091
Cdd:TIGR02813  253 TNEdiqpFDIDSKGMMIGEGIGMMALKrleDAERdGDRiyAVIKgVGASSDGKFKSIYAPrpegQAKALKRAYDDAGfap 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1092 -SFSYVEGHGTATSAGDSAESMAYQKLGSE-------LIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVH---- 1159
Cdd:TIGR02813  333 hTCGLIEAHGTGTAAGDVAEFGGLVSVFSQdndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINvdqp 412
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1061385493 1160 ----NILPSEHIRNNENirLPFVAEEKQIDRSA-IVSFGITGT 1197
Cdd:TIGR02813  413 npklDIENSPFYLNTET--RPWMQREDGTPRRAgISSFGFGGT 453
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
3203-3381 4.11e-15

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 78.37  E-value: 4.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3203 GNWLITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALR-EFEHWKSKVHTIAADINDKE---KLIRELTKLNVGIT 3278
Cdd:COG0300      6 KTVLITGASSGIGRALARALAARGA-RVVLVARDAERLEALAaELRAAGARVEVVALDVTDPDavaALAEAVLARFGPID 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3279 GIIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN----FIMMSSFTAACGNEGQLNYGVSNAYL 3353
Cdd:COG0300     85 VLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGpVRLTRALLPLM---RARgrgrIVNVSSVAGLRGLPGMAAYAASKAAL 161
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1061385493 3354 E-YQVQRRRRQGKSG---CAIQWGnWIDTGMA 3381
Cdd:COG0300    162 EgFSESLRAELAPTGvrvTAVCPG-PVDTPFT 192
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
1901-2280 1.43e-13

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 76.27  E-value: 1.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1901 PGGVSsPSELWELLKIGKNASSRI---PATRVPTRNTLISGSKY--GNPVEGGNFITQDVtqFDPSFFKISKSEAELIdp 1975
Cdd:PTZ00050     4 PLGVG-AESTWEALIAGKSGIRKLtefPKFLPDCIPEQKALENLvaAMPCQIAAEVDQSE--FDPSDFAPTKRESRAT-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1976 qqRLLLECVQECLENSGVIETSN-----VGVFVGLMEKEYQDMMESSS--------------ILAMLGSMAAviaGRVNY 2036
Cdd:PTZ00050    79 --HFAMAAAREALADAKLDILSEkdqerIGVNIGSGIGSLADLTDEMKtlyekghsrvspyfIPKILGNMAA---GLVAI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2037 IFGCYGPSVTIDTACSSSLVALEMAINALLDNRcSKVIVAG--------VNLILNEKGQGLRTNGKMLSQHGmSLSFDSR 2108
Cdd:PTZ00050   154 KHKLKGPSGSAVTACATGAHCIGEAFRWIKYGE-ADIMICGgteasitpVSFAGFSRMRALCTKYNDDPQRA-SRPFDKD 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2109 ASGYGRSDGCVVLMLE----LAKPNFHYMSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS---PSLAIDYWEAHG 2181
Cdd:PTZ00050   232 RAGFVMGEGAGILVLEelehALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGaniNINDVDYVNAHA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2182 TGTPLGDPIEFNTLSSIL-----QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKD----INAGS 2252
Cdd:PTZ00050   312 TSTPIGDKIELKAIKKVFgdsgaPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAEcdlnLVQGK 391
                          410       420
                   ....*....|....*....|....*...
gi 1061385493 2253 IRLPIIGEDSELVsagiSSFGVSGTNAA 2280
Cdd:PTZ00050   392 TAHPLQSIDAVLS----TSFGFGGVNTA 415
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
1544-1759 2.16e-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: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1544 HVVDSKIVLPGATSIRL----VHQLNGKPT-VELSNIDFLN--KITPSEAPSV---VKIEEQDGLEKLVF---------- 1603
Cdd:pfam14765   33 HRVGGTVVLPGAGYLEMaleaARQLFGGSGaVALRDVSILKalVLPEDDPVEVqtsLTPEEDGADSWWEFeifsragggw 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1604 -------------GETDAISFKLTELQNFNPIPNERLNAEVHHtdnIYERFANSHLTYRNEFQMVDSLKY--TMGKGEVR 1668
Cdd:pfam14765  113 ewtlhatgtvrlaPGEPAAPVDLESLPARCAQPADPRSVSSAE---FYERLAARGLFYGPAFQGLRRIWRgdGEALAEAR 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1669 FVSMKDLD--------ILIDGTLQAIVGCYFFENTNDNSPFVPFTIDQLSILNGDISQKQLHAVLKYDSSGN-FINGDAT 1739
Cdd:pfam14765  190 LPEAAAGGespyllhpALLDAALQLLGAALPAEAEHADQAYLPVGIERLRIYRSLPPGEPLWVHARLERRGGrTIVGDLT 269
                          250       260
                   ....*....|....*....|
gi 1061385493 1740 VYDALGNIILHISNVTFKRL 1759
Cdd:pfam14765  270 LVDEDGRVVARIEGLRLRRV 289
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3354 5.08e-11

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 66.05  E-value: 5.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKEKLIR---ELTKLNVGITGII 3281
Cdd:PRK12825    10 LVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELvEAVEALGRRAQAVQADVTDKAALEAavaAAVERFGRIDILV 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061385493 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 5.91e-11

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: 5.91e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  2943 ATVDRTEIRRKVSLAVFDLATETL---SAEDLQ-SKGFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDELS 3018
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLghaAAEAIDpDRPFRDLGLDSLMAVELRNRLEAAT--GLRLPATLVFDHPTPAALA 79

                    ....*.
gi 1061385493  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 4.92e-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: 58.71  E-value: 4.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2946 DRTEIRRKVS--LA-VFDLATETLSAED-LqskgFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDELSDHI 3021
Cdd:COG0236      2 PREELEERLAeiIAeVLGVDPEEITPDDsF----FEDLGLDSLDAVELIAALEEEF--GIELPDTELFEYPTVADLADYL 75

                   ....*
gi 1061385493 3022 VRKKS 3026
Cdd:COG0236     76 EEKLA 80
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
3994-4216 2.39e-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: 2.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3994 DEFELLEGHQLNGKIVVAGA-Y---------QLFKIDQLVKLKaagmelmlkNVKFLKPWYIEDNREYQIQ--------- 4054
Cdd:pfam14765   25 ADLPWLRDHRVGGTVVLPGAgYlemaleaarQLFGGSGAVALR---------DVSILKALVLPEDDPVEVQtsltpeedg 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4055 -----------WNSDMTiELIVNSVIVCSLEVEPQNSVLKLETI------SENEKPFEVHDFYETLFRNGLQYDSGFRRI 4117
Cdd:pfam14765   96 adswwefeifsRAGGGW-EWTLHATGTVRLAPGEPAAPVDLESLparcaqPADPRSVSSAEFYERLAARGLFYGPAFQGL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4118 ESARRSDKRCFSQIKSS----PFAWP------LIDSAMHSITASVVP--RRPDCYFLPVAMGSVTMKDTNSFTLPnLHAQ 4185
Cdd:pfam14765  175 RRIWRGDGEALAEARLPeaaaGGESPyllhpaLLDAALQLLGAALPAeaEHADQAYLPVGIERLRIYRSLPPGEP-LWVH 253
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1061385493 4186 TVITSETDKFIQVNVALLAGD-TPICEVRNMT 4216
Cdd:pfam14765  254 ARLERRGGRTIVGDLTLVDEDgRVVARIEGLR 285
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2790-2867 5.85e-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: 5.85e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493  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 3.05e-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: 3.05e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1061385493  1806 DIDNTTGFFDLGLTSIQAVKLRNAIKSNYP-NASSTCVFDYPSIDLLSGYLST 1857
Cdd:smart00823   32 AIDPDRPFRDLGLDSLMAVELRNRLEAATGlRLPATLVFDHPTPAALAEHLAA 84
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2800-2863 3.97e-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: 52.57  E-value: 3.97e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1061385493 2800 HKVCLAVGDVIesGLDIDESQLSTGFSELGIDSLATVDLLNRLNQKYfpEIELTTSDLFDNPSI 2863
Cdd:pfam00550    1 ERLRELLAEVL--GVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEF--GVEIPPSDLFEHPTL 60
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2808-2875 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: 52.16  E-value: 1.00e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061385493 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 1.15e-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: 51.78  E-value: 1.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1061385493 3485 IKEKVSSILMCSPTKLKNNKNIM-DMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLEKLAAHI 3549
Cdd:COG0236     10 LAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4268-4325 1.46e-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: 51.02  E-value: 1.46e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061385493 4268 EKVINVFSKILGRN---VAPTDKFESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLK 4325
Cdd:pfam00550    1 ERLRELLAEVLGVPaeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
3485-3543 1.69e-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: 51.02  E-value: 1.69e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1061385493 3485 IKEKVSSILMCSPTKLKNNKNIMDMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLE 3543
Cdd:pfam00550    3 LRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3485-3552 3.15e-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: 3.15e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061385493  3485 IKEKVSSILMCSPTKLKN-NKNIMDMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLEKLAAHIFEQ 3552
Cdd:smart00823   17 VREQVAAVLGHAAAEAIDpDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
376-431 3.98e-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: 3.98e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1061385493  376 NRVAISSYGFGGTNACAIIEKPEKPSLVQKESYAESNVLFLSAKSHESLKLQIEEY 431
Cdd:pfam16197   25 GIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKALLEKL 80
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
730-803 5.25e-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: 47.16  E-value: 5.25e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493  730 SDAEIESTVRTIVKQFLDIEEDDI----NLLETGAVDSLTSIEMVEAFGTAVNQTMPFDLLEAYPTILNIVDFLKTLV 803
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEItpddSFFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2949-3016 6.36e-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: 46.40  E-value: 6.36e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 2949 EIRRKVSlAVFDLATETLSAEDlqskGFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDE 3016
Cdd:pfam00550    2 RLRELLA-EVLGVPAEEIDPDT----DLFDLGLDSLLAVELIARLEEEF--GVEIPPSDLFEHPTLAE 62
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
4359-4454 2.51e-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: 2.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4359 IYLVHAIGGTIYPYYSFLQIFPKDISLYGIEfdlkYPS--------NDLRELAHFYAEEIAAHAGNKRIFVMGHSMGGIM 4430
Cdd:pfam00975    3 LFCFPPAGGSASSFRSLARRLPPPAEVLAVQ----YPGrgrgepplNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78
                           90       100
                   ....*....|....*....|....
gi 1061385493 4431 SREIVAELKIWGYDIPFVMLFDSW 4454
Cdd:pfam00975   79 AFEVARRLERQGEAVRSLFLSDAS 102
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
736-792 2.81e-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: 41.78  E-value: 2.81e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061385493  736 STVRTIVKQFLDIEEDDI----NLLETGaVDSLTSIEMVEAFGTAVNQTMPFDLLEAYPTI 792
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIdpdtDLFDLG-LDSLLAVELIARLEEEFGVEIPPSDLFEHPTL 60
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
4263-4336 5.83e-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: 41.38  E-value: 5.83e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 4263 KNSLEEKVINVFSKILGRN---VAPTDKF-ESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLKTFCNTLKNSVQ 4336
Cdd:COG0236      3 REELEERLAEIIAEVLGVDpeeITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
2267-2347 6.22e-03

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: 39.45  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2267 AGISSFGVSGTNAAAI-AFNDNNKLEPYIPIHKYYILPISAKNQISLDNLEKQILSvIPLTDVPICNIASALANNRSHFT 2345
Cdd:pfam16197   27 VGVNSFGFGGANAHVIlKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKALLEKLEN-HLDDAEFLSLLNDIHSLPISGHP 105

                   ..
gi 1061385493 2346 IR 2347
Cdd:pfam16197  106 YR 107
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1806-1848 6.80e-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: 37.93  E-value: 6.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1061385493 1806 DIDNTTGFFDLGLTSIQAVKLRNAIKSNYP-NASSTCVFDYPSI 1848
Cdd:pfam00550   17 EIDPDTDLFDLGLDSLLAVELIARLEEEFGvEIPPSDLFEHPTL 60
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
1889-2282 3.10e-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: 3.10e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1889 NPIGVMAAACRLPGGVSsPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYG-NPVEGGNFItQDVTQFDPSFFKISK 1967
Cdd:cd00833      1 EPIAIVGMACRFPGAAD-PDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGkTYTRRGGFL-DDVDAFDAAFFGISP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1968 SEAELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYQDMMESSSIL----AMLGSMAAVIAGRVNYIFG 2039
Cdd:cd00833     79 REAEAMDPQQRLLLEVAWEALEDAGYspesLAGSRTGVFVGASSSDYLELLARDPDEidayAATGTSRAFLANRISYFFD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2040 CYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDGCV 2119
Cdd:cd00833    159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2120 VLMLelaKP-------NFHYMSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS---PSlAIDYWEAHGTGTPLGDP 2189
Cdd:cd00833    239 VVVL---KRlsdalrdGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAgvdPS-DIDYVEAHGTGTPLGDP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2190 IEFNTLSSIL-------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDINAGSIRLPIIGEDS 2262
Cdd:cd00833    315 IEVEALAKVFggsrsadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEAR 394
                          410       420
                   ....*....|....*....|....*.
gi 1061385493 2263 ELVS------AGISSFGVSGTNAAAI 2282
Cdd:cd00833    395 PWPApagprrAGVSSFGFGGTNAHVI 420
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1887-2354 5.21e-112

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: 5.21e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1887 AENPIGVMAAACRLPGgVSSPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNPV---EGGnFItQDVTQFDPSFF 1963
Cdd:COG3321      2 ADEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTyvrWGG-FL-DDVDEFDALFF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1964 KISKSEAELIDPQQRLLLECVQECLENSGVIET----SNVGVFVGLMEKEYQDMM----ESSSILAMLGSMAAVIAGRVN 2035
Cdd:COG3321     79 GISPREAEAMDPQQRLLLEVAWEALEDAGYDPEslagSRTGVFVGASSNDYALLLladpEAIDAYALTGNAKSVLAGRIS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2036 YIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRS 2115
Cdd:COG3321    159 YKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2116 DGCVVLMLE------------LAkpnfhymsTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQ---SPSlAIDYWEAH 2180
Cdd:COG3321    239 EGVGVVVLKrlsdalrdgdriYA--------VIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADagvDPA-TVDYVEAH 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2181 GTGTPLGDPIEFNTLSSIL-------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDIN--AG 2251
Cdd:COG3321    310 GTGTPLGDPIEAAALTAAFgqgrpadQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDfeNS 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2252 SIRLPiigedSELVS---------AGISSFGVSGTNAAAIafndnnkLE--------PYIPIHKYYILPISAKNQISLDN 2314
Cdd:COG3321    390 PFYVN-----TELRPwpagggprrAGVSSFGFGGTNAHVV-------LEeapaaapaAAAAARPPQLLVLSAKTEEALRA 457
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1061385493 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 5.41e-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: 5.41e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   13 PNGEDGHEMAENIFLNRNNIALLPVEKNYLSDFREKHPE------VKAALVDGIEYFDDQYFGTGESEAICMDPQQRMLM 86
Cdd:cd00833     13 PGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytRRGGFLDDVDAFDAAFFGISPREAEAMDPQQRLLL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   87 QGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLL-----PPDQYMATGNSASVMCGRITYFLNSRGAAVGIETACSS 161
Cdd:cd00833     93 EVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLardpdEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSS 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  162 SLVAFHLARQAIQSGETKLALVCGANHVGS-RSFHSLYNSHMVSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENN 240
Cdd:cd00833    173 SLVALHLACQSLRSGECDLALVGGVNLILSpDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDG 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  241 LLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSDIRVMS 318
Cdd:cd00833    253 DRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARagVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQ 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  319 P------KSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEME-------LNRVAISSYGF 385
Cdd:cd00833    333 PlligsvKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARpwpapagPRRAGVSSFGF 412

                   ....*....
gi 1061385493  386 GGTNACAII 394
Cdd:cd00833    413 GGTNAHVIL 421
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
54-600 1.89e-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: 1.89e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   54 AALVDGIEYFDDQYFGTGESEAICMDPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLLPP-----DQY 128
Cdd:COG3321     64 GGFLDDVDEFDALFFGISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLAdpeaiDAY 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  129 MATGNSASVMCGRITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNG 207
Cdd:COG3321    144 ALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNlMLTPESFILFSKGGMLSPDG 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  208 RLAAFDRSANGFVRAESFAVAVLcsKQF--AEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKD 283
Cdd:COG3321    224 RCRAFDADADGYVRGEGVGVVVL--KRLsdALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADagVDPA 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  284 SVQLVTCHGTGTKLGDQVELTAINRSFKSD------IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPS 357
Cdd:COG3321    302 TVDYVEAHGTGTPLGDPIEAAALTAAFGQGrpadqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPN 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  358 EDLGEDKSMGFVNEE-MELN------RVAISSYGFGGTNACAIIEKPEKPSLVQKESYAESNVLFLSAKSHESLKLQIEE 430
Cdd:COG3321    382 PHIDFENSPFYVNTElRPWPagggprRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAAR 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  431 YTQFMAQ-SDSAMEDILYTVNERKTKYDFRAAVFGKDNEEIARKL------QDGDYSLTNLQESTFEVEF---GEGNEKL 500
Cdd:COG3321    462 LAAFLEAhPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLralaagEAAPGVVTGAAAAAPKVAFlfpGQGSQYV 541
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  501 WLLRMLYEKNETFHSTVDKYCK-LAETCGFPeaRTALFFP----FKLTLT----PLTYNVsrlisSMATFELLVQYNTLP 571
Cdd:COG3321    542 GMGRELYETEPVFRAALDECDAlLRPHLGWS--LREVLFPdeeeSRLDRTevaqPALFAV-----EYALARLWRSWGVRP 614
                          570       580
                   ....*....|....*....|....*....
gi 1061385493  572 NKLRGKGLGQIFCLAVAKVITFESAVQLI 600
Cdd:COG3321    615 DAVIGHSVGEYAAACVAGVLSLEDALRLV 643
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
1891-2282 8.49e-82

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: 8.49e-82
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  1891 IGVmaaACRLPGgVSSPSELWELLKIGKNassripatrvptrntlisgskygnpveggnfitqDVTQFDPSFFKISKSEA 1970
Cdd:smart00825    4 VGM---SCRFPG-ADDPEEFWDLLLAGLD----------------------------------DVDLFDAAFFGISPREA 45
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  1971 ELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYqdmmesssilamlgsmaaviagrvnyifgcygpSVT 2046
Cdd:smart00825   46 EAMDPQQRLLLEVAWEALEDAGIdpesLRGSRTGVFVGVSSSDY---------------------------------SVT 92
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  2047 IDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILN-EKGQGLrTNGKMLSQHGMSLSFDSRASGYGRSDGCVVLMLE- 2124
Cdd:smart00825   93 VDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSpDTFVGL-SRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKr 171
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  2125 -----------LAkpnfhymsTIQSVNVNHGGRSVSLTAPNGVAHkmlltsvinqspslaidyweahgtgtplgdpiefn 2193
Cdd:smart00825  172 lsdalrdgdpiLA--------VIRGSAVNQDGRSNGITAPSGPAQ----------------------------------- 208
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  2194 tlssilqnIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDINAGSIRLPIIGEDSELVS------A 2267
Cdd:smart00825  209 --------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWPPpgrprrA 280
                           410
                    ....*....|....*
gi 1061385493  2268 GISSFGVSGTNAAAI 2282
Cdd:smart00825  281 GVSSFGFGGTNAHVI 295
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
3649-3927 6.15e-79

Acyl transferase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 264.26  E-value: 6.15e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3649 MLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLqgDVSLWEILFNTDHYKLLQLTKHMQPIMFCFGYATAQLWLS 3728
Cdd:smart00827    1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLL--GWSLLDVLLGEDGAASLLDTEVAQPALFAVQVALARLLRS 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3729 LGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIAGLGALLAVQREiADEVL-----RKFKVSVATINSP 3803
Cdd:smart00827   79 WGVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLS-EEEVEpllagVPDRVSVAAVNSP 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3804 KQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQEThLVSLRQCLADIKFSAGRTPLVSNVTGQIINT---FS 3880
Cdd:smart00827  158 SSVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPI-LDEFRAALAGLTPRPPRIPFVSTVTGTLIDGaelDD 236
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 1061385493  3881 EAYIVKHTVSAVKFVDCVETLQA-KGVTVWIDAGSAAVLATFVKRIIQ 3927
Cdd:smart00827  237 ADYWVRNLREPVRFADAVRALLAeGGVTVFLEVGPHPVLTGPIKQTLA 284
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3617-3971 1.02e-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: 1.02e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3617 VVGKSIRDVVSKIKEAAPQQIKLC------QESSKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLqgDV 3690
Cdd:COG3321    494 VVASSREELAAKLRALAAGEAAPGvvtgaaAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALDECDALLRPHL--GW 571
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3691 SLWEILFNTDHYKLLQLTKHMQPIMFCFGYATAQLWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAME 3770
Cdd:COG3321    572 SLREVLFPDEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLEDALRLVAARGRLMQ 651
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3771 NIAGLGALLAVQ--REIADEVLRKF-KVSVATINSPKQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQETh 3847
Cdd:COG3321    652 ALPGGGAMLAVGlsEEEVEALLAGYdGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARRLPVSHAFHSPLMEPA- 730
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3848 LVSLRQCLADIKFSAGRTPLVSNVTGQIINT--FSEAYIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:COG3321    731 LEEFRAALAGVTPRAPRIPLISNVTGTWLTGeaLDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQC 810
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1061385493 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 1.52e-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: 1.52e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1889 NPIGVMAAACRLPGGVSsPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNPVEGGNFITQDVTQFDPSFFKISKS 1968
Cdd:pfam00109    1 EPVAIVGMGCRFPGGND-PEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKWGGLDDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1969 EAELIDPQQRLLLECVQECLENSGV----IETSNVGVFVGLMEKEYQDMMESSSI-------LAMLGSMAAVIAGRVNYI 2037
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGItpdsLDGSRTGVFIGSGIGDYAALLLLDEDggprrgsPFAVGTMPSVIAGRISYF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2038 FGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDG 2117
Cdd:pfam00109  160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239

                   ....*..
gi 1061385493 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 1.98e-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: 1.98e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493    57 VDGIEYFDDQYFGTGESEAICMDPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYkdllppdqymatgnsas 136
Cdd:smart00825   27 LDDVDLFDAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY----------------- 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   137 vmcgrityflnsrgaAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNGRLAAFDRS 215
Cdd:smart00825   90 ---------------SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLSPDGRCKTFDAS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   216 ANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQyevqlealknidkdsvqlvtchgtgt 295
Cdd:smart00825  155 ADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ-------------------------- 208
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   296 klgdqveltainrsfksdIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFVNEEME- 374
Cdd:smart00825  209 ------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTp 270
                           330       340
                    ....*....|....*....|....*..
gi 1061385493   375 ------LNRVAISSYGFGGTNACAIIE 395
Cdd:smart00825  271 wpppgrPRRAGVSSFGFGGTNAHVILE 297
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
6-236 3.11e-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: 3.11e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493    6 VGSWAKIPNGEDGHEMAENIFLNRNNIALLP-----VEKNYL--SDFREKHPEVKAALvDGIEYFDDQYFGTGESEAICM 78
Cdd:pfam00109    6 VGMGCRFPGGNDPEEFWENLLEGRDGISEIPadrwdPDKLYDppSRIAGKIYTKWGGL-DDIFDFDPLFFGISPREAERM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   79 DPQQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLL-------PPDQYM-ATGNSASVMCGRITYFLNSRG 150
Cdd:pfam00109   85 DPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLlldedggPRRGSPfAVGTMPSVIAGRISYFLGLRG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  151 AAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN-HVGSRSFHSLYNSHMVSPNGRLAAFDRSANGFVRAESFAVAV 229
Cdd:pfam00109  165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVV 244

                   ....*..
gi 1061385493  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 7.42e-65

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: 7.42e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  830 IACdyQFAGVEGEKELWDTLLTSRLTTGKISDIRKKQCEGDAGLEV---------GLLKqDISMFDNSFFAIAKDEAEFL 900
Cdd:cd00833      8 MAC--RFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKpgktytrrgGFLD-DVDAFDAAFFGISPREAEAM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  901 DPQHRLLLNAAYNALEKSGLT--SIPDAD--LFLAISaHSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGIRGRA 976
Cdd:cd00833     85 DPQQRLLLEVAWEALEDAGYSpeSLAGSRtgVFVGAS-SSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  977 MIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL---KTLLDHHSTNSFSVDGSGFCRSDGVGVIILK 1052
Cdd:cd00833    164 LTVDTACSSSLVALHLACQSLRSGEcDLALVGGVNLILSPDMFVGFskaGMLSPDGRCRPFDADADGYVRGEGVGVVVLK 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1053 ---TAEK-GDS--AVIKiSSAKSH--HCGAVMTPVVSS----ISQLLEEAG----SFSYVEGHGTATSAGDSAE----SM 1112
Cdd:cd00833    244 rlsDALRdGDRiyAVIR-GSAVNQdgRTKGITAPSGEAqaalIRRAYARAGvdpsDIDYVEAHGTGTPLGDPIEvealAK 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1113 AYQKLGSE---LIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVHNILPSEHIRNNE-NIRLPFVAEE----KQI 1184
Cdd:cd00833    323 VFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEEsPLRVPTEARPwpapAGP 402
                          410
                   ....*....|...
gi 1061385493 1185 DRSAIVSFGITGT 1197
Cdd:cd00833    403 RRAGVSSFGFGGT 415
FabD COG0331
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...
3644-3925 9.99e-62

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: 9.99e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3644 SKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQsclkKCDEYLqgDVSLWEILFNTDhYKLLQLTKHMQPIMFCFGYATA 3723
Cdd:COG0331      1 MKLAFLFPGQGSQYVGMGKDLYENFPVAREVFE----EASEAL--GYDLSALCFEGP-EEELNLTENTQPAILAASVAAY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3724 QLWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIA--GLGALLAVQ-------REIADEVLRKFK 3794
Cdd:COG0331     74 RALEEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVpaGPGGMAAVLglddeevEALCAEAAQGEV 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3795 VSVATINSPKQVVFAGTKSVLDAALAFVKGQG-KQATYVNQQYPFHSNLIQEThLVSLRQCLADIKFSAGRTPLVSNVTG 3873
Cdd:COG0331    154 VEIANYNSPGQIVISGEKEAVEAAAELAKEAGaKRAVPLPVSGPFHTPLMAPA-AEKLAEALAAVTFADPKIPVVSNVDA 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1061385493 3874 QIINTFSE--AYIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:COG0331    233 APVTDPEEirELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRI 286
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
830-1287 3.14e-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: 3.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  830 IACdyQFAGVEGEKELWDTLLTSRLTTGKISDIR---KKQCEGDAGLEV-------GLLKqDISMFDNSFFAIAKDEAEF 899
Cdd:COG3321     11 MAC--RFPGADDPEEFWRNLRAGRDAITEVPADRwdaDAYYDPDPDAPGktyvrwgGFLD-DVDEFDALFFGISPREAEA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  900 LDPQHRLLLNAAYNALEKSGltsIPDADL-------FLAISaHSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGI 972
Cdd:COG3321     88 MDPQQRLLLEVAWEALEDAG---YDPESLagsrtgvFVGAS-SNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  973 RGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL-KT-LL--DHHStNSFSVDGSGFCRSDGVG 1047
Cdd:COG3321    164 RGPSVTVDTACSSSLVAVHLACQSLRSGEcDLALAGGVNLMLTPESFILFsKGgMLspDGRC-RAFDADADGYVRGEGVG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1048 VIILKTAEK----GDS--AVIKiSSAKSH--HCGAVMTPVVSS----ISQLLEEAG----SFSYVEGHGTATSAGDSAE- 1110
Cdd:COG3321    243 VVVLKRLSDalrdGDRiyAVIR-GSAVNQdgRSNGLTAPNGPAqaavIRRALADAGvdpaTVDYVEAHGTGTPLGDPIEa 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1111 ---SMAYQKLGSE---LIMSSVKAQFGHCEVASGLIQLMKVS-SIgKHGIIPsivhnilPSEHIRN-NENI---RLPF-V 1178
Cdd:COG3321    322 aalTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVlAL-RHGVLP-------PTLHFETpNPHIdfeNSPFyV 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1179 AEE----KQID---RSAIVSFGITGTKT-VVTTE--RVSQLNVDNIQNCYLLPVSAKTKDGLKKACLSLIEMIDNSCE-S 1247
Cdd:COG3321    394 NTElrpwPAGGgprRAGVSSFGFGGTNAhVVLEEapAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDlD 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1061385493 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 ...
825-1056 1.71e-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: 1.71e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  825 SDINVIACDYQFAGVEGEKELWDTLLTSRLTTGKISDIR---------KKQCEGDAGLEVGLLkQDISMFDNSFFAIAKD 895
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRwdpdklydpPSRIAGKIYTKWGGL-DDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  896 EAEFLDPQHRLLLNAAYNALEKSGLT--SIPDAD--LFLAISAH--SEYRALAEKHINELDERLWMGTVHSMVAGRLAVL 969
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITpdSLDGSRtgVFIGSGIGdyAALLLLDEDGGPRRGSPFAVGTMPSVIAGRISYF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  970 MGIRGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSL---KTLLDHHSTNSFSVDGSGFCRSDG 1045
Cdd:pfam00109  160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEaDVALAGGVNLLLTPLGFAGFsaaGMLSPDGPCKAFDPFADGFVRGEG 239
                          250
                   ....*....|.
gi 1061385493 1046 VGVIILKTAEK 1056
Cdd:pfam00109  240 VGAVVLKRLSD 250
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
13-394 1.80e-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: 1.80e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   13 PNGEDGHEMAENIFLNRNNIAllPVEKNYLSDFREKHpevkAALVDGieyFDDQYFGTgESEAICMDPQQRMLMQGVIKG 92
Cdd:cd00834     13 PLGNGVEEFWEALLAGRSGIR--PITRFDASGFPSRI----AGEVPD---FDPEDYLD-RKELRRMDRFAQFALAAAEEA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   93 LENAGITLEMASEARVAVY-------TAAWCYDYKDLL--------PPDQYMATGNSASvmcGRITYFLNSRGAAVGIET 157
Cdd:cd00834     83 LADAGLDPEELDPERIGVVigsgiggLATIEEAYRALLekgprrvsPFFVPMALPNMAA---GQVAIRLGLRGPNYTVST 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  158 ACSSSLVAFHLARQAIQSGETKLALVCGA----NHVGSRSFHSLY--NSHMVSPNGRLAAFDRSANGFVRAESFAVAVLC 231
Cdd:cd00834    160 ACASGAHAIGDAARLIRLGRADVVIAGGAealiTPLTLAGFAALRalSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  232 SKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNP--ISQYEVQLEALK--NIDKDSVQLVTCHGTGTKLGDQVELTAIN 307
Cdd:cd00834    240 SLEHAKARGAKIYAEILGYGASSDAY--HITAPDPdgEGAARAMRAALAdaGLSPEDIDYINAHGTSTPLNDAAESKAIK 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  308 RSFKSD---IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDksmgFVNEEME--LNRVAIS- 381
Cdd:cd00834    318 RVFGEHakkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLD----YVPNEAReaPIRYALSn 393
                          410
                   ....*....|...
gi 1061385493  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 4.83e-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: 4.83e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTA----KALREFEHWKSKVHTIAADINDKE---KLIRELTKLNV 3275
Cdd:smart00822    1 GTYLITGGLGGLGRALARWLAERGARRLVLLSRSGPDApgaaALLAELEAAGARVTVVACDVADRDalaAVLAAIPAVEG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  3276 GITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHfnYKIENFIMMSSFTAACGNEGQLNYGVSNAYLEY 3355
Cdd:smart00822   81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTAD--LPLDFFVLFSSIAGVLGSPGQANYAAANAFLDA 158
                           170       180
                    ....*....|....*....|..
gi 1061385493  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 2.14e-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: 2.14e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3200 PITGNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWK---SKVHTIAADINDKE---KLIRELTKL 3273
Cdd:cd05274    148 GLDGTYLITGGLGGLGLLVARWLAARGARHLVLLSRRGPAPRAAARAALLRaggARVSVVRCDVTDPAalaALLAELAAG 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3274 nVGITGIIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHfnyKIENFIMMSSFTAACGNEGQLNYGVSNAY 3352
Cdd:cd05274    228 -GPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGaLNLHELTPDL---PLDFFVLFSSVAALLGGAGQAAYAAANAF 303
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1061385493 3353 LEYQVQRRRRQGKSGCAIQWGNWIDTGMATDENVRKFLANLGFLGQHNKDALKYLRACILTKPELIMVANID 3424
Cdd:cd05274    304 LDALAAQRRRRGLPATSVQWGAWAGGGMAAAAALRARLARSGLGPLAPAEALEALEALLASDAPQAVVASVD 375
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
13-396 2.89e-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: 2.89e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   13 PNGEDGHEMAENIFLNRNNIAllPVEKNYLSDFREKHpevkAALVDGieyFD-DQYFGtgESEAICMDPQQRMLMQGVIK 91
Cdd:COG0304     13 PLGNGVEEFWEALLAGRSGIR--PITRFDASGLPVRI----AGEVKD---FDpEEYLD--RKELRRMDRFTQYALAAARE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   92 GLENAGITLEMASEARVAVY-------TAAWCYDYKDL-------LPPDQY-MATGNSASvmcGRITYFLNSRGAAVGIE 156
Cdd:COG0304     82 ALADAGLDLDEVDPDRTGVIigsgiggLDTLEEAYRALlekgprrVSPFFVpMMMPNMAA---GHVSIRFGLKGPNYTVS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  157 TACSSSLVAFHLARQAIQSGETKLALVCGA----NHVGSRSFHSLynsHMVSP-NGRLAA----FDRSANGFVRAESFAV 227
Cdd:COG0304    159 TACASGAHAIGEAYRLIRRGRADVMIAGGAeaaiTPLGLAGFDAL---GALSTrNDDPEKasrpFDKDRDGFVLGEGAGV 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  228 AVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTA 305
Cdd:COG0304    236 LVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDagLSPEDIDYINAHGTSTPLGDAAETKA 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  306 INRSFK---SDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDksmgFV-NE--EMELNRVA 379
Cdd:COG0304    316 IKRVFGdhaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLD----YVpNEarEAKIDYAL 391
                          410
                   ....*....|....*..
gi 1061385493  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 3.31e-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: 3.31e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   830 IACdyQFAGVEGEKELWDTLLtsrlttgkisdirkkqcegdAGLEvgllkqDISMFDNSFFAIAKDEAEFLDPQHRLLLN 909
Cdd:smart00825    6 MSC--RFPGADDPEEFWDLLL--------------------AGLD------DVDLFDAAFFGISPREAEAMDPQQRLLLE 57
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   910 AAYNALEKSGltsIPDADLflaisahseyralaekhinelderlwMGTvhsmvagRLAVLMGIRGR--AMIVDTTCSSVA 987
Cdd:smart00825   58 VAWEALEDAG---IDPESL--------------------------RGS-------RTGVFVGVSSSdySVTVDTACSSSL 101
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   988 TALEMAVKSIREGR-KFAIVATSQLIQSSKWLYSLKTL--L--DHHStNSFSVDGSGFCRSDGVGVIILKTAEK----GD 1058
Cdd:smart00825  102 VALHLACQSLRSGEcDMALAGGVNLILSPDTFVGLSRAgmLspDGRC-KTFDASADGYVRGEGVGVVVLKRLSDalrdGD 180
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  1059 S--AVIKiSSAkSHHCGA---VMTPvvSSISQLLeeagsfsyveghgtatsagdsaesmayqkLGselimsSVKAQFGHC 1133
Cdd:smart00825  181 PilAVIR-GSA-VNQDGRsngITAP--SGPAQLL-----------------------------IG------SVKSNIGHL 221
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061385493  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 1.87e-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: 1.87e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPT----AKALREFEHWKSKVHTIAADINDK---EKLIRELTKLNV 3275
Cdd:pfam08659    1 GTYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPrpdaQALIAELEARGVEVVVVACDVSDPdavAALLAEIKAEGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3276 GITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFNykIENFIMMSSFTAACGNEGQLNYGVSNAYLEY 3355
Cdd:pfam08659   81 PIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEP--LDFFVLFSSIAGLLGSPGQANYAAANAFLDA 158
                          170       180
                   ....*....|....*....|..
gi 1061385493 3356 QVQRRRRQGKSGCAIQWGNWID 3377
Cdd:pfam08659  159 LAEYRRSQGLPATSINWGPWAE 180
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
3644-3925 2.09e-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: 2.09e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3644 SKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQsclkKCDEYLQgdVSLWEILFNTDhYKLLQLTKHMQPIMFCFGYATA 3723
Cdd:TIGR00128    1 MKIAYVFPGQGSQTVGMGKDLYEQYPIAKELFD----QASEALG--YDLKKLCQEGP-AEELNKTQYTQPALYVVSAILY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3724 QLWL-SLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENI-----AGLGALLAVQREIADEVLRKFK--- 3794
Cdd:TIGR00128   74 LKLKeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAvpeggGAMAAVIGLDEEQLAQACEEATend 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3795 VSVATINSPKQVVFAGTKSVLDAALAFVKGQG-KQATYVNQQYPFHSNLIQETHLvSLRQCLADIKFSAGRTPLVSNVTG 3873
Cdd:TIGR00128  154 VDLANFNSPGQVVISGTKDGVEAAAALFKEMGaKRAVPLEVSGAFHSRFMKPAAE-KFAETLEACQFNDPTVPVISNVDA 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1061385493 3874 QIINTFSEA--YIVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:TIGR00128  233 KPYTNGDRIkeKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGLIKRI 286
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
81-394 2.08e-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: 2.08e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   81 QQRMLMQGVIKGLENAGITLEMASEARVAVYTAAWCYDYKDLLPPDQ-------YMATGNSASVMCGRITYFLNSRGAAV 153
Cdd:cd00825     11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADamravgpYVVTKAMFPGASGQIATPLGIHGPAY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  154 GIETACSSSLVAFHLARQAIQSGETKLALvCGANHVGSRSFHSLYNSH--MVSPNGRLAAFDRSANGFVRAESFAVAVLC 231
Cdd:cd00825     91 DVSAACAGSLHALSLAADAVQNGKQDIVL-AGGSEELAAPMDCEFDAMgaLSTPEKASRTFDAAADGFVFGDGAGALVVE 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  232 SKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALK--NIDKDSVQLVTCHGTGTKLGDQVELTAINRS 309
Cdd:cd00825    170 ELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAvaGLTVWDIDYLVAHGTGTPIGDVKELKLLRSE 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  310 FKSDIR-VMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLgeDKSMGFVNEEmELNRVAISSYGFGGT 388
Cdd:cd00825    250 FGDKSPaVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAG--LNIVTETTPR-ELRTALLNGFGLGGT 326

                   ....*.
gi 1061385493  389 NACAII 394
Cdd:cd00825    327 NATLVL 332
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
78-394 1.03e-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: 1.03e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   78 MDPQQRMLMQGVIKGLENAGIT-LEMASEARVAVYT-------AAWCYDYKDLLP---PDQYMATGNSASVMCGRI-TYF 145
Cdd:cd00828     69 VDRTTLLALVATEEALADAGITdPYEVHPSEVGVVVgsgmgglRFLRRGGKLDARavnPYVSPKWMLSPNTVAGWVnILL 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  146 LNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGANHVGSRSFHSLYNSHMVS-----PNGRLAAFDRSANGFV 220
Cdd:cd00828    149 LSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALStaeeePEEMSRPFDETRDGFV 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  221 RAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISqYEVQLEALK--NIDKDSVQLVTCHGTGTKLG 298
Cdd:cd00828    229 EAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGI-ARAIRTALAkaGLSLDDLDVISAHGTSTPAN 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  299 DQVELTAINRSFK---SDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDkSMGFVNEEMEL 375
Cdd:cd00828    308 DVAESRAIAEVAGalgAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHL-SVVGLSRDLNL 386
                          330       340
                   ....*....|....*....|.
gi 1061385493  376 N-RVAIS-SYGFGGTNACAII 394
Cdd:cd00828    387 KvRAALVnAFGFGGSNAALVL 407
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
3203-3425 1.68e-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: 1.68e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKA---LREFEHWKSKVHTIAADINDKEKLIRELTKLNVG--- 3276
Cdd:cd08955    150 ATYLITGGLGGLGLLVAEWLVERGARHLVLTGRRAPSAAArqaIAALEEAGAEVVVLAADVSDRDALAAALAQIRASlpp 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3277 ITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFNykIENFIMMSSFTAACGNEGQLNYGVSNAYLEYQ 3356
Cdd:cd08955    230 LRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLP--LDFFVLFSSVASLLGSPGQANYAAANAFLDAL 307
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061385493 3357 VQRRRRQGKSGCAIQWGNWIDTGMATDENVRKFLANLGFLGQHNKDALKYLRACILTKPELIMVANIDW 3425
Cdd:cd08955    308 AHYRRARGLPALSINWGPWAEVGMAASLARQARLEARGVGAISPAAGLQALGQLLRTGSTQVGVAPVDW 376
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
244-354 1.21e-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: 1.21e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  244 HCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSD-----IRV 316
Cdd:pfam02801    1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADagVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGarkqpLAI 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1061385493  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 6.20e-37

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: 6.20e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3203 GNWLITGGLSGIGLEIGKFIANNGAENVILISRR------QPTAKALREFEHWKSKVHTIAADINDKE---KLIRELTKL 3273
Cdd:cd08953    206 GVYLVTGGAGGIGRALARALARRYGARLVLLGRSplppeeEWKAQTLAALEALGARVLYISADVTDAAavrRLLEKVRER 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3274 NVGITGIIHSAGVLKDSKIERQNKESFNQVFTPKANG----FHVLEEIEKHFnykienFIMMSSFTAACGNEGQLNYGVS 3349
Cdd:cd08953    286 YGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGllnlAQALADEPLDF------FVLFSSVSAFFGGAGQADYAAA 359
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1061385493 3350 NAYLEYQVQRRRRQGKSG--CAIQWGNWIDTGMATDENVRKFLANLGFLGQHNKDALKYLRACILTKPELIMVANID 3424
Cdd:cd08953    360 NAFLDAFAAYLRQRGPQGrvLSINWPAWREGGMAADLGARELLARAGLLPIEPEEGLQALEQALSSDLPQVLVSPGD 436
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
2133-2242 9.04e-34

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: 9.04e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2133 MSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS--PSLAIDYWEAHGTGTPLGDPIEFNTLSSIL------QNIII 2204
Cdd:pfam02801    1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAgvDPEDVDYVEAHGTGTPLGDPIEAEALKRVFgsgarkQPLAI 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1061385493 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 1.74e-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: 1.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1976 QQRLLLECVQECLENSG----VIETSNVGVFVGLMEKEY------QDMMESSSILAMLGSMAAVIAGRVNYIFGCYGPSV 2045
Cdd:cd00825     11 VSILGFEAAERAIADAGlsreYQKNPIVGVVVGTGGGSPrfqvfgADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2046 TIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHGMSLSFDSRASGYGRSDGCVVLMLE- 2124
Cdd:cd00825     91 DVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEe 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2125 ---LAKPNFHYMSTIQSVNVNHGGRSVSLTAP--NGVAHKMLLT-SVINQSPSlAIDYWEAHGTGTPLGDPIEFNTLSSI 2198
Cdd:cd00825    171 lehALARGAHIYAEIVGTAATIDGAGMGAFAPsaEGLARAAKEAlAVAGLTVW-DIDYLVAHGTGTPIGDVKELKLLRSE 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2199 LQ--NIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDInagsirLPIIGE--DSELVSAGISSFGV 2274
Cdd:cd00825    250 FGdkSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAG------LNIVTEttPRELRTALLNGFGL 323

                   ....*...
gi 1061385493 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 6.80e-32

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: 132.57  E-value: 6.80e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3177 KNPLISFAWYQNV-----QQVSFVDSDSPITGNWLITGGLSGIGLEIGKFIANNGA-ENVILISRRQPT---AKALREFE 3247
Cdd:cd08954    188 KNVYKSGSWGDFRhllldLSILKTNYPINLGKSYLITGGSGGLGLEILKWLVKRGAvENIIILSRSGMKwelELLIREWK 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3248 HWKSKVHTIAADINDK---EKLIRELTKLN--VGITGIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFN 3322
Cdd:cd08954    268 SQNIKFHFVSVDVSDVsslEKAINLILNAPkiGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRC 347
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1061385493 3323 YKIENFIMMSSFTAACGNEGQLNYGVSNAYLEYQVQRRRRQGKSGCAIQWGNWIDTGM-ATDENVRKFLANLGFLGQ 3398
Cdd:cd08954    348 WKLDYFVLFSSVSSIRGSAGQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGFvSRNESVDTLLGGQGLLPQ 424
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
129-390 4.26e-30

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 126.73  E-value: 4.26e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  129 MATGNSAsvmcgrITYflNSRGAAVGIETACSSSLVAFHLARQAIQSGETKlALVCGA--------NHVGSRSFHSLYNS 200
Cdd:PTZ00050   146 MAAGLVA------IKH--KLKGPSGSAVTACATGAHCIGEAFRWIKYGEAD-IMICGGteasitpvSFAGFSRMRALCTK 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  201 HMVSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNP-----ISQYEVQLE 275
Cdd:PTZ00050   217 YNDDPQRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAH--HITAPHPdgrgaRRCMENALK 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  276 ALKNIDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSD----IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQL 351
Cdd:PTZ00050   295 DGANININDVDYVNAHATSTPIGDKIELKAIKKVFGDSgapkLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTI 374
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1061385493  352 HLELPSEDLGEDKSMGFVNEEMELNRVAIS-SYGFGGTNA 390
Cdd:PTZ00050   375 NLENPDAECDLNLVQGKTAHPLQSIDAVLStSFGFGGVNT 414
Acyl_transf_1 pfam00698
Acyl transferase domain;
3647-3924 8.18e-30

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 123.35  E-value: 8.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3647 VLMLTGQGSQYPMMGRQLVENYEIFRTTLqsclKKCDEYL--QGDVSLWEILFNTDHyKLLQLTKHMQPIMFCFGYATAQ 3724
Cdd:pfam00698    1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVI----DRADEAFkpQYGFSVSDVLRNNPE-GTLDGTQFVQPALFAMQIALAA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3725 LWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIAGLGALLAVQREIADEVLRKF-KVSVATINSP 3803
Cdd:pfam00698   76 LLQSYGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPdDVVGAVVNSP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3804 KQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIqETHLVSLRQCLADIKFSAGRTPLVSNVTGQIIN--TFSE 3881
Cdd:pfam00698  156 RSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQM-DAIAPALLSALADIAPRTPRVPFISSTSIDPSDqrTLSA 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1061385493 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 2.45e-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: 123.96  E-value: 2.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  126 DQYMA------TGNSASVMCGRITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGanhVGSRSFHSLYN 199
Cdd:TIGR02813  167 DQYIHweensfPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---VCTDNSPFMYM 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  200 SHMVSP----NGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPisqyEVQLE 275
Cdd:TIGR02813  244 SFSKTPafttNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRP----EGQAK 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  276 ALKNIDKD------SVQLVTCHGTGTKLGDQVELTAINRSFKSD------IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQ 343
Cdd:TIGR02813  320 ALKRAYDDagfaphTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALH 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  344 HGIIPNQLHLELPSEDLGEDKSMGFVNEEMEL---------NRVAISSYGFGGTNACAIIEK--PEKPSLVQKESYAESN 412
Cdd:TIGR02813  400 HKVLPPTINVDQPNPKLDIENSPFYLNTETRPwmqredgtpRRAGISSFGFGGTNFHMVLEEysPKHQRDDQYRQRAVAQ 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  413 VLFLSAKSHESLklqIEEYTQFMAQSDSAMEDILYTVNERKTKYDFRA-----AVFG---KDNEEIARKLQDgdySLTNL 484
Cdd:TIGR02813  480 TLLFTAANEKAL---VSSLKDWKNKLSAKADDQPYAFNALAVENTLRTiavalARLGfvaKNADELITMLEQ---AITQL 553
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  485 QESTFE---VEFGEGNEKLWLLRMLYEKNETFHSTVDKYCKLAE--TCGFPEARTAL------FFPFKLT-LTPLTYNVS 552
Cdd:TIGR02813  554 EAKSCEewqLPSGISYRKSALVVESGKVAALFAGQGSQYLNMGRelACNFPEVRQAAadmdsvFTQAGKGaLSPVLYPIP 633
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  553 RL-----------------------ISSMATFELLVQYNTLPNKLRGKGLGQIFCLAVAKVITFESAVQL 599
Cdd:TIGR02813  634 VFndesrkaqeealtntqhaqsaigTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMML 703
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
139-396 8.26e-27

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 116.67  E-value: 8.26e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  139 CGRITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGA----NHVGSRSFHSL-------YNSHmvsPNG 207
Cdd:PRK07103   147 VGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGAlmdlSYWECQALRSLgamgsdrFADE---PEA 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  208 RLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPISQYEVQLEALK--NIDKDSV 285
Cdd:PRK07103   224 ACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDAN--RGPDPSLEGEMRVIRAALRraGLGPEDI 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  286 QLVTCHGTGTKLGDQVELTAINRSFKSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGiipnQLHlelPSEDLGE--D 363
Cdd:PRK07103   302 DYVNPHGTGSPLGDETELAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAG----FLH---PSRNLDEpiD 374
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1061385493  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 2.86e-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: 120.11  E-value: 2.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3639 LCQESSKCVLMLTGQGSQYPMMGRQLVENYEIFRTTLQSCLKKCDEYLQGDVS--LWEI-LFNTDHYK----LLQLTKHM 3711
Cdd:TIGR02813  574 LVVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSpvLYPIpVFNDESRKaqeeALTNTQHA 653
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3712 QPIMFCFGYATAQLWLSLGIVPDYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAM-----ENIAGL--GALLAVQRE 3784
Cdd:TIGR02813  654 QSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMaaptgEADIGFmyAVILAVVGS 733
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3785 IADE--VLRKFK-VSVATINSPKQVVFAGTKSVLDAALAFVKGQGKQATYVNQQYPFHSNLIQETHlVSLRQCLADIKFS 3861
Cdd:TIGR02813  734 PTVIanCIKDFEgVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTPLVAHAQ-KPFSAAIDKAKFN 812
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3862 AGRTPLVSNVTGQIINTFSEAY---IVKHTVSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRIIQPTELSKHRIVQ 3938
Cdd:TIGR02813  813 TPLVPLYSNGTGKLHSNDAAAIkkaLKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNILQKLVENTLKDKENELCAISI 892
                          330       340
                   ....*....|....*....|....
gi 1061385493 3939 TCKEKESDVDNLVQACLELEQSGL 3962
Cdd:TIGR02813  893 NPNPKGDSDMQLRQAAVQLAVLGL 916
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
1974-2281 1.34e-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: 1.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1974 DPQQRLLLECVQECLENSGV-----IETSNVGVFVG-----LMEKEYQDMMES------SSILAMLG--SMAAVIAGRVN 2035
Cdd:cd00828     70 DRTTLLALVATEEALADAGItdpyeVHPSEVGVVVGsgmggLRFLRRGGKLDAravnpyVSPKWMLSpnTVAGWVNILLL 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2036 yifGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRtNGKMLS-----QHGMSLSFDSRAS 2110
Cdd:cd00828    150 ---SSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFA-NMGALStaeeePEEMSRPFDETRD 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2111 GYGRSDGCVVLMLE------------LAKPNFHYMSTIQSvnvnhgGRSVSLTAPnGVAHKMLLTSVINQSPSLAIDYWE 2178
Cdd:cd00828    226 GFVEAEGAGVLVLEraelalargapiYGRVAGTASTTDGA------GRSVPAGGK-GIARAIRTALAKAGLSLDDLDVIS 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2179 AHGTGTPLGDPIEFNTLSSILQNII----IGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTliHFHVLNKDINAGSIR 2254
Cdd:cd00828    299 AHGTSTPANDVAESRAIAEVAGALGaplpVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPP--TANLDDVDPDVEHLS 376
                          330       340
                   ....*....|....*....|....*....
gi 1061385493 2255 LPIIGEDSEL--VSAGISSFGVSGTNAAA 2281
Cdd:cd00828    377 VVGLSRDLNLkvRAALVNAFGFGGSNAAL 405
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
1885-2355 7.56e-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: 112.41  E-value: 7.56e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1885 RLAENPIGVMAAAcRLPGGVSSPSELWELLKIGKNASSRIPATRVPTRNTLISGSKYGNP--VEGGNFITQdvTQFDPSF 1962
Cdd:TIGR02813    3 RLKDMPIAIVGMA-SIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADKsyCKRGGFLPE--VDFNPME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1963 FKISKSEAELIDPQQRLLLECVQECLENSGVIETSN---VGVFVG----------------------------------- 2004
Cdd:TIGR02813   80 FGLPPNILELTDISQLLSLVVAKEVLNDAGLPDGYDrdkIGITLGvgggqkqssslnarlqypvlkkvfkasgvededse 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2005 LMEKEYQDMM---ESSSILAMLGSmaaVIAGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGV--- 2078
Cdd:TIGR02813  160 MLIKKFQDQYihwEENSFPGSLGN---VISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVctd 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2079 ----NLILNEKGQGLRTNGKMlsqhgMSLSFDSRASGYGRSDGCVVLM-LELAKPNFHYM-STIQSVNVNHGGRSVSLTA 2152
Cdd:TIGR02813  237 nspfMYMSFSKTPAFTTNEDI-----QPFDIDSKGMMIGEGIGMMALKrLEDAERDGDRIyAVIKGVGASSDGKFKSIYA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2153 PNGVAHKMLLTSVINQS---PSlAIDYWEAHGTGTPLGDPIEFNTLSSI-------LQNIIIGSVKASLGHGEASAGTCG 2222
Cdd:TIGR02813  312 PRPEGQAKALKRAYDDAgfaPH-TCGLIEAHGTGTAAGDVAEFGGLVSVfsqdndqKQHIALGSVKSQIGHTKSTAGTAG 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2223 LLKLFLMLTYQYVPTLIHFHVLNKDINA--------GSIRLPIIGEDSELVSAGISSFGVSGTNAAAIafndnnkLEPYI 2294
Cdd:TIGR02813  391 MIKAVLALHHKVLPPTINVDQPNPKLDIenspfylnTETRPWMQREDGTPRRAGISSFGFGGTNFHMV-------LEEYS 463
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1061385493 2295 PIH----KY------YILPISAKNQISLdnlekqilsVIPLTDVPicNIASALANNRS-HFtirNALIVSNS 2355
Cdd:TIGR02813  464 PKHqrddQYrqravaQTLLFTAANEKAL---------VSSLKDWK--NKLSAKADDQPyAF---NALAVENT 521
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
157-396 4.59e-23

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 105.20  E-value: 4.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  157 TACSSSLVAFHLARQAIQSGETKLALVCGANH----VGSRSFHSL-----YNShmvSPNGRLAAFDRSANGFVRAESFAV 227
Cdd:PRK08439   160 TACAAGTHAIIEAVKTIMLGGADKMLVVGAESaicpVGIGGFAAMkalstRND---DPKKASRPFDKDRDGFVMGEGAGA 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  228 AVLCSKQFAEENNLLIHCECVGsaFNSDGKTPSLTAPNPISQYEVQLEALKNIDKDSVQLVTCHGTGTKLGDQVELTAIN 307
Cdd:PRK08439   237 LVLEEYESAKKRGAKIYAEIIG--FGESGDANHITSPAPEGPLRAMKAALEMAGNPKIDYINAHGTSTPYNDKNETAALK 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  308 RSFKSDIR---VMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDkSMGFVNEEMELNRVAISSYG 384
Cdd:PRK08439   315 ELFGSKEKvppVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLD-YIPNVARKAELNVVMSNSFG 393
                          250
                   ....*....|..
gi 1061385493  385 FGGTNACAIIEK 396
Cdd:PRK08439   394 FGGTNGVVIFKK 405
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
129-398 9.47e-22

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 101.40  E-value: 9.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  129 MATGNsASVMCGrityflnSRGAAVGIETACSSSLVAFHLARQAIQSGETKlALVCGanhvGSRSfhslynshMVSPNGr 208
Cdd:PRK07314   140 MAAGH-VSIRYG-------AKGPNHSIVTACATGAHAIGDAARLIAYGDAD-VMVAG----GAEA--------AITPLG- 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  209 LAAF--------------------DRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNP-- 266
Cdd:PRK07314   198 IAGFaaaralstrnddperasrpfDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAY--HMTAPAPdg 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  267 ISQYEVQLEALKN--IDKDSVQLVTCHGTGTKLGDQVELTAINRSF---KSDIRVMSPKSSMGHGEGAAGLIGVLQSLYS 341
Cdd:PRK07314   276 EGAARAMKLALKDagINPEDIDYINAHGTSTPAGDKAETQAIKRVFgehAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLA 355
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061385493  342 MQHGIIPNQLHLELPSEDLGEDksmgFV-NE--EMELNrVAIS-SYGFGGTNACAIIEKPE 398
Cdd:PRK07314   356 IRDQVIPPTINLDNPDEECDLD----YVpNEarERKID-YALSnSFGFGGTNASLVFKRYE 411
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
3206-3425 3.37e-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: 3.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTA---KALR-EFEHWKSKVHTIAADINDKEKLIRELTKLNVG--ITG 3279
Cdd:cd08952    234 LVTGGTGALGAHVARWLARRGAEHLVLTSRRGPDApgaAELVaELTALGARVTVAACDVADRDALAALLAALPAGhpLTA 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3280 IIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHfnYKIENFIMMSSFTAACGNEGQLNYGVSNAYLEYQVQR 3359
Cdd:cd08952    314 VVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHLDELTRD--RDLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAER 391
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1061385493 3360 RRRQGKSGCAIQWGNWIDTGMATDEnVRKFLANLGFLGQHNKDALKYLRAcILTKPE-LIMVANIDW 3425
Cdd:cd08952    392 RRARGLPATSVAWGPWAGGGMAAGA-AAERLRRRGLRPMDPELALAALRR-ALDHDEtAVVVADVDW 456
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
142-393 1.50e-20

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 98.15  E-value: 1.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  142 ITYFL-NSRGAAVGIE-----------TACSSSLVAFHLARQAIQSGETKLAlVCGA-----NHVG------SRSFHSLY 198
Cdd:PRK06333   144 IPSFLtNMAAGHVSIRygfkgplgapvTACAAGVQAIGDAARLIRSGEADVA-VCGGteaaiDRVSlagfaaARALSTRF 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  199 NShmvSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPISQ--YEVQLEA 276
Cdd:PRK06333   223 ND---APEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAY--HMTAGPEDGEgaRRAMLIA 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  277 LK--NIDKDSVQLVTCHGTGTKLGDQVELTAINRSFKSD--IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLH 352
Cdd:PRK06333   298 LRqaGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVsgLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLN 377
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1061385493  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 2.93e-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: 2.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  843 KELWDTLLTSRltTGkISDIRKKQCEGDAGLEVGLLKqdismFDNSFFAIAKDEAEFLDPQHRLLLNAAYNALEKSGL-- 920
Cdd:cd00834     19 EEFWEALLAGR--SG-IRPITRFDASGFPSRIAGEVP-----DFDPEDYLDRKELRRMDRFAQFALAAAEEALADAGLdp 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  921 -------------TSIPDADLFLAisahsEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVA 987
Cdd:cd00834     91 eeldperigvvigSGIGGLATIEE-----AYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASGA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  988 TALEMAVKSIREGRKFAIVA--TSQLIQSSKW--LYSLKTLldhhSTNS---------FSVDGSGFCRSDGVGVIILKTA 1054
Cdd:cd00834    166 HAIGDAARLIRLGRADVVIAggAEALITPLTLagFAALRAL----STRNddpekasrpFDKDRDGFVLGEGAGVLVLESL 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1055 EkgdSAV---IKI--------SSAKSHHcgavMT-P------VVSSISQLLEEAG----SFSYVEGHGTATSAGDSAESM 1112
Cdd:cd00834    242 E---HAKargAKIyaeilgygASSDAYH----ITaPdpdgegAARAMRAALADAGlspeDIDYINAHGTSTPLNDAAESK 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1113 AYQKLGSE----LIMSSVKAQFGHCEVASGLIQLmkVSSIG--KHGIIPsivhnilPSEHIRN-NENIRLPFV---AEEK 1182
Cdd:cd00834    315 AIKRVFGEhakkVPVSSTKSMTGHLLGAAGAVEA--IATLLalRDGVLP-------PTINLEEpDPECDLDYVpneAREA 385
                          410
                   ....*....|....*....
gi 1061385493 1183 QIDRSAIVSFGITGTKTVV 1201
Cdd:cd00834    386 PIRYALSNSFGFGGHNASL 404
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
136-396 6.17e-20

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 95.84  E-value: 6.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  136 SVMCGRITYFLNSRGAAVGIETACSSSL---------VAFHLARQAIQSGETKLALVCGANHVGSRSFHSLYNShmvSPN 206
Cdd:PRK08722   141 NMIAGNLSIMRGLRGPNIAISTACTTGLhnighaarmIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRND---EPQ 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  207 GRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGsaFNSDGKTPSLTAPNPI-SQYEVQLEAL---KNIDK 282
Cdd:PRK08722   218 KASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVG--FGMSGDAYHMTSPSEDgSGGALAMEAAmrdAGVTG 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  283 DSVQLVTCHGTGTKLGDQVELTAINRSF----KSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSE 358
Cdd:PRK08722   296 EQIGYVNAHGTSTPAGDVAEIKGIKRALgeagSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEE 375
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1061385493  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 1.36e-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: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   81 QQRMLMQGVIKGLENAGITlemaSEARVAVYTAawcydykdllppdQYMATGNSASVMCGRITYFLNSRGAAVGIETACS 160
Cdd:cd00327      7 ASELGFEAAEQAIADAGLS----KGPIVGVIVG-------------TTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  161 SSLVAFHLARQAIQSGETKLALVCGANHvgsrsfhslynshmvspngrlaafdrsangFVRAESFAVAVLCSKQFAEENN 240
Cdd:cd00327     70 TGLTALALAVQQVQNGKADIVLAGGSEE------------------------------FVFGDGAAAAVVESEEHALRRG 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  241 LLIHCECVGSAFNSDGKT----PSLTAPNPISQyevqlEALK--NIDKDSVQLVTCHGTGTKLGDQVELTAINRSFK-SD 313
Cdd:cd00327    120 AHPQAEIVSTAATFDGASmvpaVSGEGLARAAR-----KALEgaGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGvRS 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  314 IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQlhlelpsedlgedksmgfvneEMELNRVAISSYGFGGTNACAI 393
Cdd:cd00327    195 PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------------PREPRTVLLLGFGLGGTNAAVV 253

                   .
gi 1061385493  394 I 394
Cdd:cd00327    254 L 254
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
892-1201 2.21e-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: 2.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  892 IAKDEAEFLDPQHRLLLNAAYNALEKSGLTsIPDAD-----LFLAISAHS------EYRALAEKHINELDERLWMGTVHS 960
Cdd:COG0304     60 LDRKELRRMDRFTQYALAAAREALADAGLD-LDEVDpdrtgVIIGSGIGGldtleeAYRALLEKGPRRVSPFFVPMMMPN 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  961 MVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIV-ATSQLIQSSKWL--YSLKTLldhhSTNS---- 1032
Cdd:COG0304    139 MAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRaDVMIAgGAEAAITPLGLAgfDALGAL----STRNddpe 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1033 -----FSVDGSGFCRSDGVGVIILKTAEkgdSAV---IKI--------SSAKSHHcgavMT-------PVVSSISQLLEE 1089
Cdd:COG0304    215 kasrpFDKDRDGFVLGEGAGVLVLEELE---HAKargAKIyaevvgygASSDAYH----ITapapdgeGAARAMRAALKD 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1090 AG----SFSYVEGHGTATSAGDSAESMAYQKL----GSELIMSSVKAQFGHCEVASGLIQLmkVSSIG--KHGIIPsivh 1159
Cdd:COG0304    288 AGlspeDIDYINAHGTSTPLGDAAETKAIKRVfgdhAYKVPVSSTKSMTGHLLGAAGAIEA--IASVLalRDGVIP---- 361
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1061385493 1160 nilPSEHIRN-NENIRLPFV---AEEKQIDRSAIVSFGITGTKTVV 1201
Cdd:COG0304    362 ---PTINLENpDPECDLDYVpneAREAKIDYALSNSFGFGGHNASL 404
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
212-390 3.19e-19

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 93.19  E-value: 3.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  212 FDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPisQYEVQLEALK------NIDKDSV 285
Cdd:PRK05952   199 FDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAY--HMSAPEP--DGKSAIAAIQqclarsGLTPEDI 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  286 QLVTCHGTGTKLGDQVELTAINRSFKSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLgedks 365
Cdd:PRK05952   275 DYIHAHGTATRLNDQREANLIQALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDL----- 349
                          170       180
                   ....*....|....*....|....*..
gi 1061385493  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 6.58e-19

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: 6.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1903 GVSSP-----SELWELLKIGKNASSRIPATRVPTRNTLISGSkygnpveggnfitqdVTQFDPSFFkISKSEAELIDPQQ 1977
Cdd:cd00834      9 GAVTPlgngvEEFWEALLAGRSGIRPITRFDASGFPSRIAGE---------------VPDFDPEDY-LDRKELRRMDRFA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1978 RLLLECVQECLENSGVIETS----NVGVFVG-------LMEKEYQDMMESSS-------ILAMLGSMAA-VIAGRvnyiF 2038
Cdd:cd00834     73 QFALAAAEEALADAGLDPEEldpeRIGVVIGsgigglaTIEEAYRALLEKGPrrvspffVPMALPNMAAgQVAIR----L 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2039 GCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKG----QGLRTngkmLSQHG-----MSLSFDSRA 2109
Cdd:cd00834    149 GLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTlagfAALRA----LSTRNddpekASRPFDKDR 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2110 SGYGRSDGCVVLMLE--------LAKPnfhymstiqsvnvnHG---GRSVS-----LTAPNGVAHKMLLtsVINQ----- 2168
Cdd:cd00834    225 DGFVLGEGAGVLVLEslehakarGAKI--------------YAeilGYGASsdayhITAPDPDGEGAAR--AMRAalada 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2169 --SPSlAIDYWEAHGTGTPLGDPIEFNTLSSIL----QNIIIGSVKASLGHGEASAG------TCgllklfLMLTYQYVP 2236
Cdd:cd00834    289 glSPE-DIDYINAHGTSTPLNDAAESKAIKRVFgehaKKVPVSSTKSMTGHLLGAAGaveaiaTL------LALRDGVLP 361
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1061385493 2237 TLIHFHVLNKDINagsirLPIIGEDSE--LVSAGIS-SFGVSGTNAAAI 2282
Cdd:cd00834    362 PTINLEEPDPECD-----LDYVPNEAReaPIRYALSnSFGFGGHNASLV 405
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
127-389 7.92e-19

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 92.49  E-value: 7.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  127 QYMATGNSASVMCgrityflnSRGAAVGIET---ACSSSLVAFHLARQAIQSGETKLAlVCG-------ANHVGS----R 192
Cdd:PRK07910   144 MYMPNGPAAAVGL--------ERHAKAGVITpvsACASGSEAIAQAWRQIVLGEADIA-ICGgvetrieAVPIAGfaqmR 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  193 SFHSLYNShmvSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPISQ--- 269
Cdd:PRK07910   215 IVMSTNND---DPAGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGF--HMVAPDPNGErag 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  270 ----YEVQLEALKNIDkdsVQLVTCHGTGTKLGDQVELTAINRSFKSD-IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQH 344
Cdd:PRK07910   290 hamtRAIELAGLTPGD---IDHVNAHATGTSVGDVAEGKAINNALGGHrPAVYAPKSALGHSVGAVGAVESILTVLALRD 366
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1061385493  345 GIIPNQLHLEL--PSEDL----GEDKSMGFvneemelnRVAIS-SYGFGGTN 389
Cdd:PRK07910   367 GVIPPTLNLENldPEIDLdvvaGEPRPGNY--------RYAINnSFGFGGHN 410
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
146-394 3.05e-18

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 90.29  E-value: 3.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  146 LNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGANHVgSRS----FHSLynsHMVSPnGRLAAFDRSANGFVR 221
Cdd:PRK09185   147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSL-CRLtlngFNSL---ESLSP-QPCRPFSANRDGINI 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  222 AESFAVAVLcSKQFAEENNLLIHCEcvgsafNSDGKTPSltAPNP--------ISQyevqleALK--NIDKDSVQLVTCH 291
Cdd:PRK09185   222 GEAAAFFLL-EREDDAAVALLGVGE------SSDAHHMS--APHPeglgailaMQQ------ALAdaGLAPADIGYINLH 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  292 GTGTKLGDQVELTAINRSFKSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDksmGFVNE 371
Cdd:PRK09185   287 GTATPLNDAMESRAVAAVFGDGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPL---YLVEN 363
                          250       260
                   ....*....|....*....|....*
gi 1061385493  372 EMELN-RVAIS-SYGFGGTNACAII 394
Cdd:PRK09185   364 AQALAiRYVLSnSFAFGGNNCSLIF 388
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
148-394 6.61e-18

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 89.69  E-value: 6.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  148 SRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGANhvGSRSFHSLYNSHMVS--------PNGRLAAFDRSANGF 219
Cdd:PRK06501   164 TRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATD--GSVSAEALIRFSLLSalstqndpPEKASKPFSKDRDGF 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  220 VRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDG--KTPSLTAPNPIsqyevqLEALKN------IDKDSVQLVTCH 291
Cdd:PRK06501   242 VMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSfhRTRSSPDGSPA------IGAIRAaladagLTPEQIDYINAH 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  292 GTGTKLGDQVELTAINRSFK---SDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDkSMGF 368
Cdd:PRK06501   316 GTSTPENDKMEYLGLSAVFGerlASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLD-VVPN 394
                          250       260
                   ....*....|....*....|....*.
gi 1061385493  369 VNEEMELNRVAISSYGFGGTNACAII 394
Cdd:PRK06501   395 VARDARVTAVLSNSFGFGGQNASLVL 420
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
4359-4569 1.17e-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: 1.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4359 IYLVHAIGGTIYPYYSFLQIFPKDISLYGIEF----DLKYPSNDLRELAHFYAEEIAAHAGNKRIFVMGHSMGGIMSREI 4434
Cdd:COG3319    604 LFCVHPAGGNVLCYRPLARALGPDRPVYGLQApgldGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEM 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4435 VAELKIWGYDIPFVMLFDSWV--LRTNELDIENIKQFITYVFSGLP-----------DSEHRINRAIKLA---------- 4491
Cdd:COG3319    684 ARQLEAQGEEVALLVLLDSYApgALARLDEAELLAALLRDLARGVDlpldaeelralDPEERLARLLERLreaglpagld 763
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4492 ---------------QLLREYKTSVSDTKLYLFkskqlgdaafkkavRSDLNEELSRSMTCNGFDELSLQPVETYLIDGD 4556
Cdd:COG3319    764 aerlrrllrvfranlRALRRYRPRPYDGPVLLF--------------RAEEDPPGRADDPALGWRPLVAGGLEVHDVPGD 829
                          250
                   ....*....|...
gi 1061385493 4557 HESCLKAENLKKV 4569
Cdd:COG3319    830 HFSMLREPHVAEL 842
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
151-390 1.91e-17

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 88.70  E-value: 1.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  151 AAVgieTACSSSLVAFHLARQAIQSGETKLaLVCGANH--------VG---SRSFHSLYNShmvSPNGRLAAFDRSANGF 219
Cdd:PLN02836   179 AAV---TACATGAHSIGDAFRMIQFGDADV-MVAGGTEssidalsiAGfsrSRALSTKFNS---CPTEASRPFDCDRDGF 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  220 VRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPISQYEV--QLEALKN--IDKDSVQLVTCHGTGT 295
Cdd:PLN02836   252 VIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAH--HITQPHEDGRGAVlaMTRALQQsgLHPNQVDYVNAHATST 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  296 KLGDQVELTAINRSFKSD-----IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPsEDLGEDKSMGFVN 370
Cdd:PLN02836   330 PLGDAVEARAIKTVFSEHatsggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERP-DPIFDDGFVPLTA 408
                          250       260
                   ....*....|....*....|.
gi 1061385493  371 EEMELNRVAIS-SYGFGGTNA 390
Cdd:PLN02836   409 SKAMLIRAALSnSFGFGGTNA 429
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
1902-2282 2.07e-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: 2.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1902 GGVSS----PSELWELLKIGKNASSRIPATRVPTRNTLISGSkygnpveggnfitqdVTQFDPSFFkISKSEAELIDPQQ 1977
Cdd:COG0304      9 GAVSPlgngVEEFWEALLAGRSGIRPITRFDASGLPVRIAGE---------------VKDFDPEEY-LDRKELRRMDRFT 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1978 RLLLECVQECLENSGV----IETSNVGVFVG-------LMEKEYQDMME-------SSSILAMLGSMAAviaGRVNYIFG 2039
Cdd:COG0304     73 QYALAAAREALADAGLdldeVDPDRTGVIIGsgiggldTLEEAYRALLEkgprrvsPFFVPMMMPNMAA---GHVSIRFG 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2040 CYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQ-----HGMSLSFDSRASGYGR 2114
Cdd:COG0304    150 LKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrnddpEKASRPFDKDRDGFVL 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2115 SDGCVVLMLE------------LAKpnfhymstIQSVNVNHGGRSVSLTAPNGVAhkmlLTSVINQ-------SPSlAID 2175
Cdd:COG0304    230 GEGAGVLVLEelehakargakiYAE--------VVGYGASSDAYHITAPAPDGEG----AARAMRAalkdaglSPE-DID 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2176 YWEAHGTGTPLGDPIEFNTLSSIL----QNIIIGSVKASLGHgeaSAGTCGLLKL---FLMLTYQYVPTLIHFHvlNKDI 2248
Cdd:COG0304    297 YINAHGTSTPLGDAAETKAIKRVFgdhaYKVPVSSTKSMTGH---LLGAAGAIEAiasVLALRDGVIPPTINLE--NPDP 371
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1061385493 2249 NagsIRLPIIGEDS-EL-VSAGIS-SFGVSGTNAAAI 2282
Cdd:COG0304    372 E---CDLDYVPNEArEAkIDYALSnSFGFGGHNASLV 405
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
60-399 2.66e-17

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 88.88  E-value: 2.66e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   60 IEYFDDQYFGT---GESEAICMD----PQ--QRM------LMQGVIKGLENAGITLEMASE---ARVAVYTA-------- 113
Cdd:PLN02787   163 IERFDCSQFPTriaGEIKSFSTDgwvaPKlsKRMdkfmlyLLTAGKKALADGGITEDVMKEldkTKCGVLIGsamggmkv 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  114 ------AWCYDYKDLLPPDQYMATGNSASVMcgrITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGAN 187
Cdd:PLN02787   243 fndaieALRISYRKMNPFCVPFATTNMGSAM---LAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSD 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  188 ----------HVGSRSFhSLYNShmvSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGK 257
Cdd:PLN02787   320 aaiipiglggFVACRAL-SQRND---DPTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAY 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  258 tpSLTAPNP-----ISQYEVQLeALKNIDKDSVQLVTCHGTGTKLGDQVELTAINRSF--KSDIRVMSPKSSMGHGEGAA 330
Cdd:PLN02787   396 --HMTEPHPegagvILCIEKAL-AQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFgqNPELRVNSTKSMIGHLLGAA 472
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  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 2.91e-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: 2.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGK-FIANNGAENVILISRRQPTAK---ALR-EFEHWKSKVHTIAADINDKEKLIRELTKLNVG--IT 3278
Cdd:cd08956    197 LITGGTGTLGALLARhLVTEHGVRHLLLVSRRGPDAPgaaELVaELAALGAEVTVAACDVADRAALAALLAAVPADhpLT 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3279 GIIHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFNYKIenFIMMSSFTAACGNEGQLNYGVSNAYLEYQVQ 3358
Cdd:cd08956    277 AVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWHLHELTRDLDLAA--FVLFSSAAGVLGSPGQANYAAANAFLDALAQ 354
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1061385493 3359 RRRRQGKSGCAIQWGNWIDTGMAT---DENVRKFLANLGFLGQHNKDALKYLRA 3409
Cdd:cd08956    355 HRRARGLPATSLAWGLWAQASGMTahlSDADLARLARGGLRPLSAEEGLALFDA 408
PLN02752 PLN02752
[acyl-carrier protein] S-malonyltransferase
3643-3925 7.56e-16

[acyl-carrier protein] S-malonyltransferase


Pssm-ID: 215401 [Multi-domain]  Cd Length: 343  Bit Score: 82.50  E-value: 7.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3643 SSKCVLMLTGQGSQYPMMGRQLVENyeifrTTLQSCLKKCDEYLQGDvsLWEILFNTDHYKLlQLTKHMQPIMFCFGYAT 3722
Cdd:PLN02752    37 KPTTAFLFPGQGAQAVGMGKEAAEV-----PAAKALFDKASEILGYD--LLDVCVNGPKEKL-DSTVVSQPAIYVASLAA 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3723 AQLWLSLGIVP------DYYLGHSVGELVAGVLAGIMSIEDGLRLIVERGKAMENIA-----------GLG--ALLAVQR 3783
Cdd:PLN02752   109 VEKLRARDGGQavidsvDVCAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAAdagpsgmvsviGLDsdKVQELCA 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3784 EIADEVLRKFKVSVATINSPKQVVFAGTKSVLDAALAFVKGQG-KQATYVNQQYPFHSNLIqETHLVSLRQCLADIKFSA 3862
Cdd:PLN02752   189 AANEEVGEDDVVQIANYLCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFM-EPAVDALEAALAAVEIRT 267
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 3863 GRTPLVSNVTGQIintFSEAYIVKHT-----VSAVKFVDCVETLQAKGVTVWIDAGSAAVLATFVKRI 3925
Cdd:PLN02752   268 PRIPVISNVDAQP---HSDPATIKKIlarqvTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGIVKRV 332
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
867-1206 8.10e-16

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 83.24  E-value: 8.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  867 CEGDAGLEvgllkqDISMFDNSFFA--IAK-----DEAEFLDPQH--------RLLLNAAYNALEKSGLT-SIPDADLFl 930
Cdd:PRK08439    27 CNGECGIK------KITLFDASDFPvqIAGeitdfDPTEVMDPKEvkkadrfiQLGLKAAREAMKDAGFLpEELDAERF- 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  931 AISAHSEYRALA--EKHINELDER--------LWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREG 1000
Cdd:PRK08439   100 GVSSASGIGGLPniEKNSIICFEKgprkispfFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLG 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1001 ---RKFAIVATSQL----IQSSKWLYSLKTLLDH--HSTNSFSVDGSGFCRSDGVGVIILKTAEKGDSAVIKI------- 1064
Cdd:PRK08439   180 gadKMLVVGAESAIcpvgIGGFAAMKALSTRNDDpkKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIyaeiigf 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1065 -SSAKSHHcgaVMTPVV----SSISQLLEEAGS--FSYVEGHGTATSAGDSAESMAYQKL--GSELI--MSSVKAQFGHC 1133
Cdd:PRK08439   260 gESGDANH---ITSPAPegplRAMKAALEMAGNpkIDYINAHGTSTPYNDKNETAALKELfgSKEKVppVSSTKGQIGHC 336
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 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 1.81e-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: 1.81e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1976 QQRLLLECVQECLENSGVIETSNVGVFVGLmekeyqdmmesssiLAMLGSMAAViAGRVNYIFG-CYGPSVTIDTACSSS 2054
Cdd:cd00327      7 ASELGFEAAEQAIADAGLSKGPIVGVIVGT--------------TGGSGEFSGA-AGQLAYHLGiSGGPAYSVNQACATG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2055 LVALEMAINALLDNRCSKVIVAGVNLIlnekgqglrtngkmlsqhgmslsfdsrasgyGRSDGCVVLML----ELAKPNF 2130
Cdd:cd00327     72 LTALALAVQQVQNGKADIVLAGGSEEF-------------------------------VFGDGAAAAVVeseeHALRRGA 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2131 HYMSTIQSVNVNHGGRS----VSLTAPNGVAHKMLltSVINQSPSlAIDYWEAHGTGTPLGDPIEFNTLSS--ILQNIII 2204
Cdd:cd00327    121 HPQAEIVSTAATFDGASmvpaVSGEGLARAARKAL--EGAGLTPS-DIDYVEAHGTGTPIGDAVELALGLDpdGVRSPAV 197
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 2205 GSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLihfhvlnkdinagsirlpiigeDSELVSAGISSFGVSGTNAAAI 2282
Cdd:cd00327    198 SATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----------------------PREPRTVLLLGFGLGGTNAAVV 253
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
129-399 2.27e-15

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 81.64  E-value: 2.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  129 MATGNSASVMcgriTYFlNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGA-----------NHVGSRSfhSL 197
Cdd:PRK07967   137 MASTVSACLA----TPF-KIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGeeldwemsclfDAMGALS--TK 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  198 YNShmvSPNGRLAAFDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPISQYEVQLEAL 277
Cdd:PRK07967   210 YND---TPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGY--DMVAPSGEGAVRCMQMAL 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  278 KNIDKDsVQLVTCHGTGTKLGDQVELTAINRSFKSDIRVMSPKSSM-GHGEGAAGLIGVLQSLYSMQHGIIPNQLHLElp 356
Cdd:PRK07967   285 ATVDTP-IDYINTHGTSTPVGDVKELGAIREVFGDKSPAISATKSLtGHSLGAAGVQEAIYSLLMMEHGFIAPSANIE-- 361
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1061385493  357 seDLGED-KSMGFVNEEME---LNRVAISSYGFGGTNACAIIEKPEK 399
Cdd:PRK07967   362 --ELDPQaAGMPIVTETTDnaeLTTVMSNSFGFGGTNATLVFRRYKG 406
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
1083-1159 2.82e-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: 2.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1083 ISQLLEEAG----SFSYVEGHGTATSAGDSAESMAYQKL------GSELIMSSVKAQFGHCEVASGLIQLMKVSSIGKHG 1152
Cdd:pfam02801   30 IRRALADAGvdpeDVDYVEAHGTGTPLGDPIEAEALKRVfgsgarKQPLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHG 109

                   ....*..
gi 1061385493 1153 IIPSIVH 1159
Cdd:pfam02801  110 VIPPTLN 116
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
950-1197 3.73e-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: 83.52  E-value: 3.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  950 DERLWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVATSQLIQSSKWLYSLKTLLDHHS 1029
Cdd:TIGR02813  173 EENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFT 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1030 TNS----FSVDGSGFCRSDGVGVIILK---TAEK-GDS--AVIK-ISSAKSHHCGAVMTP----VVSSISQLLEEAG--- 1091
Cdd:TIGR02813  253 TNEdiqpFDIDSKGMMIGEGIGMMALKrleDAERdGDRiyAVIKgVGASSDGKFKSIYAPrpegQAKALKRAYDDAGfap 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1092 -SFSYVEGHGTATSAGDSAESMAYQKLGSE-------LIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVH---- 1159
Cdd:TIGR02813  333 hTCGLIEAHGTGTAAGDVAEFGGLVSVFSQdndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINvdqp 412
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1061385493 1160 ----NILPSEHIRNNENirLPFVAEEKQIDRSA-IVSFGITGT 1197
Cdd:TIGR02813  413 npklDIENSPFYLNTET--RPWMQREDGTPRRAgISSFGFGGT 453
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
142-394 3.93e-15

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 81.19  E-value: 3.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  142 ITYFLNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGANHV---GSRSFHSLY-----NSHmvsPNGRLAAFD 213
Cdd:PRK09116   147 VGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELcptEAAVFDTLFatstrNDA---PELTPRPFD 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  214 RSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKtpSLTAPNPIS-QYEVQLeALK--NIDKDSVQLVTC 290
Cdd:PRK09116   224 ANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGA--HVTQPQAETmQIAMEL-ALKdaGLAPEDIGYVNA 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  291 HGTGTKLGDQVELTAINRSFKSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGE-DKSMGFV 369
Cdd:PRK09116   301 HGTATDRGDIAESQATAAVFGARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGAlDYIMGEA 380
                          250       260
                   ....*....|....*....|....*
gi 1061385493  370 nEEMELNRVAISSYGFGGTNACAII 394
Cdd:PRK09116   381 -REIDTEYVMSNNFAFGGINTSLIF 404
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
3203-3381 4.11e-15

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 78.37  E-value: 4.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3203 GNWLITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALR-EFEHWKSKVHTIAADINDKE---KLIRELTKLNVGIT 3278
Cdd:COG0300      6 KTVLITGASSGIGRALARALAARGA-RVVLVARDAERLEALAaELRAAGARVEVVALDVTDPDavaALAEAVLARFGPID 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3279 GIIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN----FIMMSSFTAACGNEGQLNYGVSNAYL 3353
Cdd:COG0300     85 VLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGpVRLTRALLPLM---RARgrgrIVNVSSVAGLRGLPGMAAYAASKAAL 161
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1061385493 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 1.10e-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: 1.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  899 FLDPQHRLLLNAAYNALEKSGLTsipDADLF----LAISAHS---EYRALAekHINELDERLWMGTV-------HSMVAG 964
Cdd:cd00828     68 IVDRTTLLALVATEEALADAGIT---DPYEVhpseVGVVVGSgmgGLRFLR--RGGKLDARAVNPYVspkwmlsPNTVAG 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  965 RLAV-LMGIRGRAMIVDTTCSSVATALEMAVKSIREGR-KFAIVATSQLIQ--SSKWL-----YSLKTLLDHHSTNSFSV 1035
Cdd:cd00828    143 WVNIlLLSSHGPIKTPVGACATALEALDLAVEAIRSGKaDIVVVGGVEDPLeeGLSGFanmgaLSTAEEEPEEMSRPFDE 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1036 DGSGFCRSDGVGVIILKT---AEKGDSAVIKISSAKSHHC-GAVM------TPVVSSISQLLEEAGSF----SYVEGHGT 1101
Cdd:cd00828    223 TRDGFVEAEGAGVLVLERaelALARGAPIYGRVAGTASTTdGAGRsvpaggKGIARAIRTALAKAGLSlddlDVISAHGT 302
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1061385493 1102 ATSAGDSAES----MAYQKLGSELIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPSIVH 1159
Cdd:cd00828    303 STPANDVAESraiaEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTAN 364
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
883-1199 1.51e-14

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 79.35  E-value: 1.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  883 SMFDNSFFAIAKDEAEFLdpqhRLLLNAAYNALEKSGLTSIPDAD-------LFLAISA----HSEYRALAEKHINELDE 951
Cdd:PTZ00050    61 SEFDPSDFAPTKRESRAT----HFAMAAAREALADAKLDILSEKDqerigvnIGSGIGSladlTDEMKTLYEKGHSRVSP 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  952 RLWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVA-------TSQLIQSSKWLYSLKTL 1024
Cdd:PTZ00050   137 YFIPKILGNMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICggteasiTPVSFAGFSRMRALCTK 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1025 L-DHHSTNS--FSVDGSGFCRSDGVGVIILKTAEKGDSAVIKI--------SSAKSHHcgaVMTP------VVSSISQLL 1087
Cdd:PTZ00050   217 YnDDPQRASrpFDKDRAGFVMGEGAGILVLEELEHALRRGAKIyaeirgygSSSDAHH---ITAPhpdgrgARRCMENAL 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1088 EEAGSFS-----YVEGHGTATSAGDSAESMAYQKL-----GSELIMSSVKAQFGHCEVASGLIQ-LMKVSSIgKHGIIPS 1156
Cdd:PTZ00050   294 KDGANINindvdYVNAHATSTPIGDKIELKAIKKVfgdsgAPKLYVSSTKGGLGHLLGAAGAVEsIVTILSL-YEQIIPP 372
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1061385493 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 2.05e-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: 2.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  903 QHRLLLNAAYNALEKSGLTSIPDADLFLAISAHS--------EYRALAEKHINELDERLWMgtvHSMVAGRLAVLMGIRG 974
Cdd:cd00825     11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTgggsprfqVFGADAMRAVGPYVVTKAM---FPGASGQIATPLGIHG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  975 RAMIVDTTCSSVATALEMAVKSIR--EGRKFAIVATSQLIqsskWLYSL------KTLLDHHSTNSFSVDGSGFCRSDGV 1046
Cdd:cd00825     88 PAYDVSAACAGSLHALSLAADAVQngKQDIVLAGGSEELA----APMDCefdamgALSTPEKASRTFDAAADGFVFGDGA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1047 GVIILK----TAEKGDSAVIKISSAKSHHCGAVM-------TPVVSSISQLLEEAG----SFSYVEGHGTATSAGDSAES 1111
Cdd:cd00825    164 GALVVEelehALARGAHIYAEIVGTAATIDGAGMgafapsaEGLARAAKEALAVAGltvwDIDYLVAHGTGTPIGDVKEL 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1112 MAYQKL--GSELIMSSVKAQFGHCEVASGLIQLMKVSSIGKHGIIPsivhnilPSEHIRNNENIRLPFVAEE--KQIDRS 1187
Cdd:cd00825    244 KLLRSEfgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIP-------PSIHIEELDEAGLNIVTETtpRELRTA 316
                          330
                   ....*....|
gi 1061385493 1188 AIVSFGITGT 1197
Cdd:cd00825    317 LLNGFGLGGT 326
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
3206-3398 3.33e-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: 3.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:COG1028     10 LVTGGSSGIGRAIARALAAEGA-RVVITDRDAEALEAAaAELRAAGGRALAVAADVTDEAaveALVAAAVAAFGRLDILV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN----FIMMSSFTAACGNEGQLNYGVSNAYLEYQ 3356
Cdd:COG1028     89 NNAGITPPGPLEELTEEDWDRVLDVNLKGpFLLTRAALPHM---RERgggrIVNISSIAGLRGSPGQAAYAASKAAVVGL 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1061385493 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 3.50e-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: 3.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGIIH 3282
Cdd:cd05233      2 LVTGASSGIGRAIARRLAREGA-KVVLADRNEEALAELAAIEALGGNAVAVQADVSDEEdveALVEEALEEFGRLDILVN 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1061385493 3283 SAGVLKDSKIERQNKESFNQVFtpKAN---GFHVLEEIEKHFnyKIENF---IMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:cd05233     81 NAGIARPGPLEELTDEDWDRVL--DVNltgVFLLTRAALPHM--KKQGGgriVNISSVAGLRPLPGQAAYAASKA 151
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
1901-2280 1.43e-13

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 76.27  E-value: 1.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1901 PGGVSsPSELWELLKIGKNASSRI---PATRVPTRNTLISGSKY--GNPVEGGNFITQDVtqFDPSFFKISKSEAELIdp 1975
Cdd:PTZ00050     4 PLGVG-AESTWEALIAGKSGIRKLtefPKFLPDCIPEQKALENLvaAMPCQIAAEVDQSE--FDPSDFAPTKRESRAT-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1976 qqRLLLECVQECLENSGVIETSN-----VGVFVGLMEKEYQDMMESSS--------------ILAMLGSMAAviaGRVNY 2036
Cdd:PTZ00050    79 --HFAMAAAREALADAKLDILSEkdqerIGVNIGSGIGSLADLTDEMKtlyekghsrvspyfIPKILGNMAA---GLVAI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2037 IFGCYGPSVTIDTACSSSLVALEMAINALLDNRcSKVIVAG--------VNLILNEKGQGLRTNGKMLSQHGmSLSFDSR 2108
Cdd:PTZ00050   154 KHKLKGPSGSAVTACATGAHCIGEAFRWIKYGE-ADIMICGgteasitpVSFAGFSRMRALCTKYNDDPQRA-SRPFDKD 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2109 ASGYGRSDGCVVLMLE----LAKPNFHYMSTIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS---PSLAIDYWEAHG 2181
Cdd:PTZ00050   232 RAGFVMGEGAGILVLEelehALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGaniNINDVDYVNAHA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2182 TGTPLGDPIEFNTLSSIL-----QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKD----INAGS 2252
Cdd:PTZ00050   312 TSTPIGDKIELKAIKKVFgdsgaPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAEcdlnLVQGK 391
                          410       420
                   ....*....|....*....|....*...
gi 1061385493 2253 IRLPIIGEDSELVsagiSSFGVSGTNAA 2280
Cdd:PTZ00050   392 TAHPLQSIDAVLS----TSFGFGGVNTA 415
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
144-396 1.31e-12

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 72.45  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  144 YFLNSRGAAVgieTACSSSLVAFHLARQAIQSGETKLALVCGANHV----------GSRSFHSLYNShmvSPNGRLAAFD 213
Cdd:PRK14691    79 HFKGPIGAPV---TACAAGVQAIGDAVRMIRNNEADVALCGGAEAVidtvslagfaAARALSTHFNS---TPEKASRPFD 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  214 RSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEALKN--IDKDSVQLVTCH 291
Cdd:PRK14691   153 TARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQagITPEQVQHLNAH 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  292 GTGTKLGDQVELTAINRSF--KSDIRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGFV 369
Cdd:PRK14691   233 ATSTPVGDLGEINAIKHLFgeSNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGN 312
                          250       260
                   ....*....|....*....|....*..
gi 1061385493  370 NEEMELNRVAISSYGFGGTNACAIIEK 396
Cdd:PRK14691   313 AQPHDMTYALSNGFGFAGVNASILLKR 339
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
1544-1759 2.16e-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: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1544 HVVDSKIVLPGATSIRL----VHQLNGKPT-VELSNIDFLN--KITPSEAPSV---VKIEEQDGLEKLVF---------- 1603
Cdd:pfam14765   33 HRVGGTVVLPGAGYLEMaleaARQLFGGSGaVALRDVSILKalVLPEDDPVEVqtsLTPEEDGADSWWEFeifsragggw 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1604 -------------GETDAISFKLTELQNFNPIPNERLNAEVHHtdnIYERFANSHLTYRNEFQMVDSLKY--TMGKGEVR 1668
Cdd:pfam14765  113 ewtlhatgtvrlaPGEPAAPVDLESLPARCAQPADPRSVSSAE---FYERLAARGLFYGPAFQGLRRIWRgdGEALAEAR 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1669 FVSMKDLD--------ILIDGTLQAIVGCYFFENTNDNSPFVPFTIDQLSILNGDISQKQLHAVLKYDSSGN-FINGDAT 1739
Cdd:pfam14765  190 LPEAAAGGespyllhpALLDAALQLLGAALPAEAEHADQAYLPVGIERLRIYRSLPPGEPLWVHARLERRGGrTIVGDLT 269
                          250       260
                   ....*....|....*....|
gi 1061385493 1740 VYDALGNIILHISNVTFKRL 1759
Cdd:pfam14765  270 LVDEDGRVVARIEGLRLRRV 289
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
889-1155 2.49e-11

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 69.27  E-value: 2.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  889 FFAIAKDEAEFldPQHRLLLNAAynaleksGLTSIPDADLFLAISAHSEYRALAEkhineldeRLWMGTVhsmvAGRLAV 968
Cdd:PRK06501   102 FLAAPPVELEW--PARFALAAAV-------GDNDAPSYDRLLRAARGGRFDALHE--------RFQFGSI----ADRLAD 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  969 LMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFA--IVAT------SQLIQSSkWLYSLKTLLD--HHSTNSFSVDGS 1038
Cdd:PRK06501   161 RFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRalCIATdgsvsaEALIRFS-LLSALSTQNDppEKASKPFSKDRD 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1039 GFCRSDGVGVIILKTAEkgdSAV---IKI--------SSAKSHHC------GAvmtPVVSSISQLLEEAG----SFSYVE 1097
Cdd:PRK06501   240 GFVMAEGAGALVLESLE---SAVargAKIlgivagcgEKADSFHRtrsspdGS---PAIGAIRAALADAGltpeQIDYIN 313
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1061385493 1098 GHGTATSAGDSAESMAYQKLGSELI----MSSVKAQFGHCEVASGLIQlmKVSSIG--KHGIIP 1155
Cdd:PRK06501   314 AHGTSTPENDKMEYLGLSAVFGERLasipVSSNKSMIGHTLTAAGAVE--AVFSLLtiQTGRLP 375
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3354 5.08e-11

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 66.05  E-value: 5.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKEKLIR---ELTKLNVGITGII 3281
Cdd:PRK12825    10 LVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELvEAVEALGRRAQAVQADVTDKAALEAavaAAVERFGRIDILV 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061385493 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 5.91e-11

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: 5.91e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  2943 ATVDRTEIRRKVSLAVFDLATETL---SAEDLQ-SKGFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDELS 3018
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLghaAAEAIDpDRPFRDLGLDSLMAVELRNRLEAAT--GLRLPATLVFDHPTPAALA 79

                    ....*.
gi 1061385493  3019 DHIVRK 3024
Cdd:smart00823   80 EHLAAE 85
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
3206-3351 6.29e-11

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 65.95  E-value: 6.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGIIH 3282
Cdd:PRK05653     9 LVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAavrALIEAAVEAFGALDILVN 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1061385493 3283 SAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN----FIMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:PRK05653    89 NAGITRDALLPRMSEEDWDRVIDVNLTGtFNVVRAALPPM---IKArygrIVNISSVSGVTGNPGQTNYSAAKA 159
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
4263-4454 4.64e-10

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 66.61  E-value: 4.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4263 KNSLEEKVINVFSKILGRNVAPTD-KFESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLKTFCNTLKNSVQKPISK 4341
Cdd:PRK10252   976 KTGTETIIAAAFSSLLGCDVVDADaDFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRRL 1055
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4342 VPNVITKLREvpNSKFNIYLVHAIGGTIYPYYSFLQIFPKDISLYGIEFDLKYP----SNDLRELAHFYAEEIAAHAGNK 4417
Cdd:PRK10252  1056 GFGTILPLRE--GDGPTLFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGpmqtATSLDEVCEAHLATLLEQQPHG 1133
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1061385493 4418 RIFVMGHSMGGIMSREIVAELKIWGYDIPFVMLFDSW 4454
Cdd:PRK10252  1134 PYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTW 1170
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
1949-2282 4.73e-10

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 65.41  E-value: 4.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1949 NFITQD---VTQFDPSFFkISKSEAELIDPQQRLLLECVQECLENSGVIET----SNVGVFVG-------LMEKEYQDMM 2014
Cdd:PRK08722    45 NFSTRFaglVKDFNCEEY-MSKKDARKMDLFIQYGIAAGIQALDDSGLEVTeenaHRIGVAIGsgigglgLIEAGHQALV 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2015 ESS----SILAMLGSMAAVIAGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLR 2090
Cdd:PRK08722   124 EKGprkvSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGF 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2091 TNGKMLSQ-----HGMSLSFDSRASGYGRSDGCVVLMLELAKPNFHYMSTIQSVNVNHG--GRSVSLTAP--NGVAHKML 2161
Cdd:PRK08722   204 GAAKALSTrndepQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGmsGDAYHMTSPseDGSGGALA 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2162 LTSVINQSPSLA--IDYWEAHGTGTPLGDPIEFNTLSSIL-----QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQY 2234
Cdd:PRK08722   284 MEAAMRDAGVTGeqIGYVNAHGTSTPAGDVAEIKGIKRALgeagsKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQI 363
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1061385493 2235 VPTLIHF----HVLNKDINAGSIRlpiigEDSELVSAGISSFGVSGTNAAAI 2282
Cdd:PRK08722   364 VPPTINLddpeEGLDIDLVPHTAR-----KVESMEYAICNSFGFGGTNGSLI 410
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2946-3026 4.92e-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: 58.71  E-value: 4.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2946 DRTEIRRKVS--LA-VFDLATETLSAED-LqskgFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDELSDHI 3021
Cdd:COG0236      2 PREELEERLAeiIAeVLGVDPEEITPDDsF----FEDLGLDSLDAVELIAALEEEF--GIELPDTELFEYPTVADLADYL 75

                   ....*
gi 1061385493 3022 VRKKS 3026
Cdd:COG0236     76 EEKLA 80
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
3994-4216 2.39e-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: 2.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3994 DEFELLEGHQLNGKIVVAGA-Y---------QLFKIDQLVKLKaagmelmlkNVKFLKPWYIEDNREYQIQ--------- 4054
Cdd:pfam14765   25 ADLPWLRDHRVGGTVVLPGAgYlemaleaarQLFGGSGAVALR---------DVSILKALVLPEDDPVEVQtsltpeedg 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4055 -----------WNSDMTiELIVNSVIVCSLEVEPQNSVLKLETI------SENEKPFEVHDFYETLFRNGLQYDSGFRRI 4117
Cdd:pfam14765   96 adswwefeifsRAGGGW-EWTLHATGTVRLAPGEPAAPVDLESLparcaqPADPRSVSSAEFYERLAARGLFYGPAFQGL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4118 ESARRSDKRCFSQIKSS----PFAWP------LIDSAMHSITASVVP--RRPDCYFLPVAMGSVTMKDTNSFTLPnLHAQ 4185
Cdd:pfam14765  175 RRIWRGDGEALAEARLPeaaaGGESPyllhpaLLDAALQLLGAALPAeaEHADQAYLPVGIERLRIYRSLPPGEP-LWVH 253
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1061385493 4186 TVITSETDKFIQVNVALLAGD-TPICEVRNMT 4216
Cdd:pfam14765  254 ARLERRGGRTIVGDLTLVDEDgRVVARIEGLR 285
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
864-1197 3.82e-09

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 62.33  E-value: 3.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  864 KKQCEGDAGLeVGLLKQDISMFDNSFFAIAKD----------EAEFLDPQHRLLLNAAYNALEKSGLTSIPD--ADLFLA 931
Cdd:PRK08722    26 KALLAGQSGI-VNIEHFDTTNFSTRFAGLVKDfnceeymskkDARKMDLFIQYGIAAGIQALDDSGLEVTEEnaHRIGVA 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  932 ISA--------HSEYRALAEKHINELDERLWMGTVHSMVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKF 1003
Cdd:PRK08722   105 IGSgigglgliEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDAD 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1004 AIVATSQLIQSSKW-------LYSLKTLLD--HHSTNSFSVDGSGFCRSDGVGVIILKTAEKGDSAVIKI--------SS 1066
Cdd:PRK08722   185 AMVAGGAEKASTPLgmagfgaAKALSTRNDepQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIyaelvgfgMS 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1067 AKSHHcgavMTPVVS-------SISQLLEEAG----SFSYVEGHGTATSAGDSAESMAYQK-LGSE----LIMSSVKAQF 1130
Cdd:PRK08722   265 GDAYH----MTSPSEdgsggalAMEAAMRDAGvtgeQIGYVNAHGTSTPAGDVAEIKGIKRaLGEAgskqVLVSSTKSMT 340
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1061385493 1131 GHCEVASGLIQ-LMKVSSIGKHGIIPSIvhNILPSEhirnnENIRLPFVAEE----KQIDRSAIVSFGITGT 1197
Cdd:PRK08722   341 GHLLGAAGSVEaIITVMSLVDQIVPPTI--NLDDPE-----EGLDIDLVPHTarkvESMEYAICNSFGFGGT 405
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
3206-3351 4.21e-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: 60.25  E-value: 4.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAK-ALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:cd05333      4 LVTGASRGIGRAIALRLAAEGA-KVAVTDRSEEAAAeTVEEIKALGGNAAALEADVSDREaveALVEKVEAEFGPVDILV 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN----FIMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:cd05333     83 NNAGITRDNLLMRMSEEDWDAVINVNLTGvFNVTQAVIRAM---IKRrsgrIINISSVVGLIGNPGQANYAASKA 154
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
3206-3381 4.64e-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: 4.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRqptakalrefehwkskvhtiaaDIndkeklireltklnvgitgIIHSAG 3285
Cdd:cd02266      2 LVTGGSGGIGGAIARWLASRGSPKVLVVSRR----------------------DV-------------------VVHNAA 40
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3286 VLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFNYKIE-NFIMMSSFTAACGNEGQLNYGVSNAYLEYQVQRRRRQ 3363
Cdd:cd02266     41 ILDDGRLIDLTGSRIERAIRANVVGtRRLLEAARELMKAKRLgRFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASE 120
                          170       180
                   ....*....|....*....|..
gi 1061385493 3364 GKSG----CAIQWGNWIDTGMA 3381
Cdd:cd02266    121 GWGNglpaTAVACGTWAGSGMA 142
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2790-2867 5.85e-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: 5.85e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493  2790 AAKTLQMAVRHKVCLAVGDVIESGLDIDESqlstgFSELGIDSLATVDLLNRLNQKYfpEIELTTSDLFDNPSIIDLS 2867
Cdd:smart00823    9 RRRLLLDLVREQVAAVLGHAAAEAIDPDRP-----FRDLGLDSLMAVELRNRLEAAT--GLRLPATLVFDHPTPAALA 79
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
3206-3304 1.35e-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: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQ-PTAKALREFEHWKSKVHTIAADINDK-------EKLIRELTKLNVgi 3277
Cdd:pfam00106    4 LVTGASSGIGRAIAKRLAKEGA-KVVLVDRSEeKLEAVAKELGALGGKALFIQGDVTDRaqvkalvEQAVERLGRLDI-- 80
                           90       100
                   ....*....|....*....|....*..
gi 1061385493 3278 tgIIHSAGVLKDSKIERQNKESFNQVF 3304
Cdd:pfam00106   81 --LVNNAGITGLGPFSELSDEDWERVI 105
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
1951-2282 1.95e-08

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 60.13  E-value: 1.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1951 ITQDVTQFDPSFFkISKSEAELIDPQQRLLLECVQECLENS------------GVIETSNVGvfvGL--MEKEYQDMMES 2016
Cdd:PRK08439    48 IAGEITDFDPTEV-MDPKEVKKADRFIQLGLKAAREAMKDAgflpeeldaerfGVSSASGIG---GLpnIEKNSIICFEK 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2017 -----------SSILAMLGsmaaviaGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEK 2085
Cdd:PRK08439   124 gprkispffipSALVNMLG-------GFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPV 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2086 GQGLRTNGKMLS------QHGmSLSFDSRASGYGRSDGCVVLMLE-----LAKPNFHYMSTI---QSVNVNHggrsVSLT 2151
Cdd:PRK08439   197 GIGGFAAMKALStrnddpKKA-SRPFDKDRDGFVMGEGAGALVLEeyesaKKRGAKIYAEIIgfgESGDANH----ITSP 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2152 APNGVAHKMllTSVINQSPSLAIDYWEAHGTGTPLGDPIEFNTLSSIL---QNI-IIGSVKASLGHGEASAGTCGLLKLF 2227
Cdd:PRK08439   272 APEGPLRAM--KAALEMAGNPKIDYINAHGTSTPYNDKNETAALKELFgskEKVpPVSSTKGQIGHCLGAAGAIEAVISI 349
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1061385493 2228 LMLTYQYVPTLIHFhvLNKDINAGSIRLPIIGEDSELVSAGISSFGVSGTNAAAI 2282
Cdd:PRK08439   350 MAMRDGILPPTINQ--ETPDPECDLDYIPNVARKAELNVVMSNSFGFGGTNGVVI 402
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
2005-2231 2.20e-08

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 60.04  E-value: 2.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2005 LMEKEYQDMMESSSILAMLGSMAAVIAGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVnliLNE 2084
Cdd:PRK07103   121 LVHETYRDRPAFLRPSYGLSFMDTDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGA---LMD 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2085 KG----QGLRTNGKMLSQHGMSL------SFDSRASG--YGRSDGCVVLmlELAKP----NFHYMSTIQSVNVNHGGRSV 2148
Cdd:PRK07103   198 LSywecQALRSLGAMGSDRFADEpeaacrPFDQDRDGfiYGEACGAVVL--ESAESarrrGARPYAKLLGWSMRLDANRG 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2149 SLTAPNGVAHkmlltsVINQSPSLA------IDYWEAHGTGTPLGDPIEFNTL-SSILQNIIIGSVKASLGHGEASAGTC 2221
Cdd:PRK07103   276 PDPSLEGEMR------VIRAALRRAglgpedIDYVNPHGTGSPLGDETELAALfASGLAHAWINATKSLTGHGLSAAGIV 349
                          250
                   ....*....|
gi 1061385493 2222 GLLKLFLMLT 2231
Cdd:PRK07103   350 ELIATLLQMR 359
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
3206-3351 2.46e-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: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPT----AKALREfEHwKSKVHTIAADINDK---EKLIRELTKLNVGIT 3278
Cdd:cd05352     12 IVTGGSRGIGLAIARALAEAGA-DVAIIYNSAPRaeekAEELAK-KY-GVKTKAYKCDVSSQesvEKTFKQIQKDFGKID 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1061385493 3279 GIIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFNYKIE-NFIMMSSFTAACGNEGQLN--YGVSNA 3351
Cdd:cd05352     89 ILIANAGITVHKPALDYTYEQWNKVIDVNLNGvFNCAQAAAKIFKKQGKgSLIITASMSGTIVNRPQPQaaYNASKA 165
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
961-1197 3.03e-08

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 59.42  E-value: 3.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  961 MVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVA------TSQL----IQSSKwlySLKTLLDHHST 1030
Cdd:PRK07314   140 MAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAggaeaaITPLgiagFAAAR---ALSTRNDDPER 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1031 NS--FSVDGSGFCRSDGVGVIILKTAE--KGDSAviKI--------SSAKSHHcgavMT-PV------VSSISQLLEEAG 1091
Cdd:PRK07314   217 ASrpFDKDRDGFVMGEGAGILVLEELEhaKARGA--KIyaevvgygMTGDAYH----MTaPApdgegaARAMKLALKDAG 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1092 ----SFSYVEGHGTATSAGDSAESMAYQKL----GSELIMSSVKAQFGHCEVASGLIQ-LMKVSSIgKHGIIPsivhnil 1162
Cdd:PRK07314   291 inpeDIDYINAHGTSTPAGDKAETQAIKRVfgehAYKVAVSSTKSMTGHLLGAAGAVEaIFSVLAI-RDQVIP------- 362
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1061385493 1163 PSEHIRN-NENIRLPFV---AEEKQIDRSAIVSFGITGT 1197
Cdd:PRK07314   363 PTINLDNpDEECDLDYVpneARERKIDYALSNSFGFGGT 401
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1806-1857 3.05e-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: 3.05e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1061385493  1806 DIDNTTGFFDLGLTSIQAVKLRNAIKSNYP-NASSTCVFDYPSIDLLSGYLST 1857
Cdd:smart00823   32 AIDPDRPFRDLGLDSLMAVELRNRLEAATGlRLPATLVFDHPTPAALAEHLAA 84
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2800-2863 3.97e-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: 52.57  E-value: 3.97e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1061385493 2800 HKVCLAVGDVIesGLDIDESQLSTGFSELGIDSLATVDLLNRLNQKYfpEIELTTSDLFDNPSI 2863
Cdd:pfam00550    1 ERLRELLAEVL--GVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEF--GVEIPPSDLFEHPTL 60
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
903-1155 4.91e-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: 4.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  903 QHRLLLNAAYNALEKSGLTSIPDADLFLAISAhseyralaekhinelderlwMGTVHSMVAGRLAVLMGIR-GRAMIVDT 981
Cdd:cd00327      7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTG--------------------GSGEFSGAAGQLAYHLGISgGPAYSVNQ 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  982 TCSSVATALEMAVKSIREGRKFAIVAtsqliqsskwlyslktlldhhstnsfsVDGSGFCRSDGVGVIILKT----AEKG 1057
Cdd:cd00327     67 ACATGLTALALAVQQVQNGKADIVLA---------------------------GGSEEFVFGDGAAAAVVESeehaLRRG 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1058 DSAVIKISSAKSHHCGAVMTPVVS------SISQLLEEAG----SFSYVEGHGTATSAGDSAESMAYQKL--GSELIMSS 1125
Cdd:cd00327    120 AHPQAEIVSTAATFDGASMVPAVSgeglarAARKALEGAGltpsDIDYVEAHGTGTPIGDAVELALGLDPdgVRSPAVSA 199
                          250       260       270
                   ....*....|....*....|....*....|
gi 1061385493 1126 VKAQFGHCEVASGLIQLMKVSSIGKHGIIP 1155
Cdd:cd00327    200 TLIMTGHPLGAAGLAILDELLLMLEHEFIP 229
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
3206-3286 5.29e-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: 56.88  E-value: 5.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISR-----RQPTAKALREFEHWKSKVHTIAADINDK---EKLIRELTKLNVGI 3277
Cdd:cd08939      5 LITGGSSGIGKALAKELVKEGA-NVIIVARsesklEEAVEEIEAEANASGQKVSYISADLSDYeevEQAFAQAVEKGGPP 83

                   ....*....
gi 1061385493 3278 TGIIHSAGV 3286
Cdd:cd08939     84 DLVVNCAGI 92
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2808-2875 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: 52.16  E-value: 1.00e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061385493 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 1.15e-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: 51.78  E-value: 1.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1061385493 3485 IKEKVSSILMCSPTKLKNNKNIM-DMGLDSKLIVEFLNFINSTFKISVNLSDAYNHPTLEKLAAHI 3549
Cdd:COG0236     10 LAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
3206-3304 1.32e-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: 55.76  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGK-FIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAAD---INDKEKLIRELTKLNVGITGII 3281
Cdd:cd05367      3 ILTGASRGIGRALAEeLLKRGSPSVVVLLARSEEPLQELKEELRPGLRVTTVKADlsdAAGVEQLLEAIRKLDGERDLLI 82
                           90       100
                   ....*....|....*....|....
gi 1061385493 3282 HSAGVLKD-SKIERQNKESFNQVF 3304
Cdd:cd05367     83 NNAGSLGPvSKIEFIDLDELQKYF 106
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4268-4325 1.46e-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: 51.02  E-value: 1.46e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061385493 4268 EKVINVFSKILGRN---VAPTDKFESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLK 4325
Cdd:pfam00550    1 ERLRELLAEVLGVPaeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
2020-2280 1.48e-07

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 56.98  E-value: 1.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2020 LAMLGSMAAVIAGRvnyIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVN-----LILnekgQGLRTNGk 2094
Cdd:PRK05952   118 LDTLPHQAAIAAAR---QIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEapitpLTL----AGFQQMG- 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2095 MLSQHGmSLSFDSRASGYGRSDGCVVLMLELAkpnfhymSTIQSVNVNHGGR--SVSLTAPngvAHKMLLTSVINQSPSL 2172
Cdd:PRK05952   190 ALAKTG-AYPFDRQREGLVLGEGGAILVLESA-------ELAQKRGAKIYGQilGFGLTCD---AYHMSAPEPDGKSAIA 258
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2173 A--------------IDYWEAHGTGTPLGDPIEFNTLSSIL-QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPT 2237
Cdd:PRK05952   259 AiqqclarsgltpedIDYIHAHGTATRLNDQREANLIQALFpHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPP 338
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1061385493 2238 LIHFHVLNKDINAgsIRLPiigEDSELVSAGISSFGVSGTNAA 2280
Cdd:PRK05952   339 CVGLQEPEFDLNF--VRQA---QQSPLQNVLCLSFGFGGQNAA 376
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
961-1199 1.50e-07

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 57.49  E-value: 1.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  961 MVAGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVA--TSQLIQS--------SKWLYSLKTLLDHHST 1030
Cdd:PLN02836   162 MAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAggTESSIDAlsiagfsrSRALSTKFNSCPTEAS 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1031 NSFSVDGSGFCRSDGVGVIILKTAEKGDSAVIKIS--------SAKSHHC--------GAVMtpvvsSISQLLEEAG--- 1091
Cdd:PLN02836   242 RPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYaevrgygmSGDAHHItqphedgrGAVL-----AMTRALQQSGlhp 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1092 -SFSYVEGHGTATSAGDSAESMAYQKLGSE------LIMSSVKAQFGHCEVASGLIQ-LMKVSSIgKHGIIPSIVHNILP 1163
Cdd:PLN02836   317 nQVDYVNAHATSTPLGDAVEARAIKTVFSEhatsggLAFSSTKGATGHLLGAAGAVEaIFSVLAI-HHGIAPPTLNLERP 395
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1061385493 1164 SEHIRNNeniRLPFVAEEKQIDRSAIV-SFGITGTKT 1199
Cdd:PLN02836   396 DPIFDDG---FVPLTASKAMLIRAALSnSFGFGGTNA 429
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
2022-2282 1.65e-07

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 57.32  E-value: 1.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2022 MLGSMAAviaGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQHG- 2100
Cdd:PRK06333   147 FLTNMAA---GHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFn 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2101 -----MSLSFDSRASGYGRSDGCVVLMLEL--------AKPNFHYMSTIQSVNVNHggrsvsLTAP----NGVAHKMLLT 2163
Cdd:PRK06333   224 dapeqASRPFDRDRDGFVMGEGAGILVIETlehalargAPPLAELVGYGTSADAYH------MTAGpedgEGARRAMLIA 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2164 svINQ---SPSlAIDYWEAHGTGTPLGDPIEFNTLSSIL---QNIIIGSVKASLGHGEASAGtcGLLKLF--LMLTYQYV 2235
Cdd:PRK06333   298 --LRQagiPPE-EVQHLNAHATSTPVGDLGEVAAIKKVFghvSGLAVSSTKSATGHLLGAAG--GVEAIFtiLALRDQIA 372
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1061385493 2236 PTLIHFHvlNKDINAGSIRLpIIGEDSEL-VSAGIS-SFGVSGTNAAAI 2282
Cdd:PRK06333   373 PPTLNLE--NPDPAAEGLDV-VANKARPMdMDYALSnGFGFGGVNASIL 418
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
3485-3543 1.69e-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: 51.02  E-value: 1.69e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1061385493 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 2.02e-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: 55.55  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3201 ITGNW-LITGGLSGIGLEIGK-FIAnNGAEnVILISRRQPT-AKALREFEHwkskVHTIAADINDKE-------KLIREL 3270
Cdd:COG3967      3 LTGNTiLITGGTSGIGLALAKrLHA-RGNT-VIITGRREEKlEEAAAANPG----LHTIVLDVADPAsiaalaeQVTAEF 76
                           90
                   ....*....|....*.
gi 1061385493 3271 TKLNVgitgIIHSAGV 3286
Cdd:COG3967     77 PDLNV----LINNAGI 88
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3485-3552 3.15e-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: 3.15e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061385493  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 3.73e-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: 54.53  E-value: 3.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3203 GNW-LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKAL-REFEH-WKSKVHTIAADINDK----EKLIRELTKLNV 3275
Cdd:cd05356      1 GTWaVVTGATDGIGKAYAEELAKRGF-NVILISRTQEKLDAVaKEIEEkYGVETKTIAADFSAGddiyERIEKELEGLDI 79
                           90
                   ....*....|.
gi 1061385493 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 4.83e-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: 4.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  212 FDRSANGFVRAESFAVAVLCSKQFAEENNLLIHCECVGSAFNSDGKTPSLTAPNPISQYEVQLEAlKNIDKDSVQLVTCH 291
Cdd:cd00832    218 FDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPPGLARAIRLALAD-AGLTPEDVDVVFAD 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  292 GTGTKLGDQVELTAINRSFKSD-IRVMSPKSSMGHGEGAAGLIGVLQSLYSMQHGIIPNQLHLELPSEDLGEDKSMGfVN 370
Cdd:cd00832    297 AAGVPELDRAEAAALAAVFGPRgVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTG-RP 375
                          170       180
                   ....*....|....*....|....
gi 1061385493  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 8.50e-07

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: 8.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADIND-KEKLIRELTKLnVGITGI---I 3281
Cdd:cd05325      2 LITGASRGIGLELVRQLLARGNNTVIATCRDPSAATELAALGASHSRLHILELDVTDeIAESAEAVAER-LGDAGLdvlI 80
                           90       100
                   ....*....|....*....|....
gi 1061385493 3282 HSAGVL-KDSKIERQNKESFNQVF 3304
Cdd:cd05325     81 NNAGILhSYGPASEVDSEDLLEVF 104
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
1907-2284 9.97e-07

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 54.79  E-value: 9.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1907 PSELWELLKIGKNASSRIP---ATRVPTRntlISGSkygnpveggnfitqdVTQFDPSFFkISKSEAELIDPQQRLLLEC 1983
Cdd:PRK07314    19 VESTWKNLLAGKSGIGPIThfdTSDLAVK---IAGE---------------VKDFNPDDY-MSRKEARRMDRFIQYGIAA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1984 VQECLENSG-VIETSN---VGVFVG-------LMEKEYQDMMESS----SILAMLGSMAAVIAGRVNYIFGCYGPSVTID 2048
Cdd:PRK07314    80 AKQAVEDAGlEITEENadrIGVIIGsgiggleTIEEQHITLLEKGprrvSPFFVPMAIINMAAGHVSIRYGAKGPNHSIV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2049 TACSSSLVALEMA--INALLDnrcSKVIVAG-VNLILNEKGQGLRTNGKMLSQ-----HGMSLSFDSRASGYGRSDGCVV 2120
Cdd:PRK07314   160 TACATGAHAIGDAarLIAYGD---ADVMVAGgAEAAITPLGIAGFAAARALSTrnddpERASRPFDKDRDGFVMGEGAGI 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2121 LMLEL--------AKPnfhY-------MStiqsvnvnhgGRSVSLTAPN----GVAHKM---LLTSVINQSpslAIDYWE 2178
Cdd:PRK07314   237 LVLEElehakargAKI---YaevvgygMT----------GDAYHMTAPApdgeGAARAMklaLKDAGINPE---DIDYIN 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2179 AHGTGTPLGDPIEFNTLSSIL----QNIIIGSVKASLGHGEASAGtcGLLKLF--LMLTYQYVPTLIHFHVLNKDINAGS 2252
Cdd:PRK07314   301 AHGTSTPAGDKAETQAIKRVFgehaYKVAVSSTKSMTGHLLGAAG--AVEAIFsvLAIRDQVIPPTINLDNPDEECDLDY 378
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1061385493 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 1.35e-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: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493   69 GTGES---EAICMDPQQrMLMQGVIKGLENAGITLEMAsEARVAVYTAAWcydykdllppdqyMATGNSASVMCgriTYF 145
Cdd:cd00829      2 GVGMTpfgRRSDRSPLE-LAAEAARAALDDAGLEPADI-DAVVVGNAAGG-------------RFQSFPGALIA---EYL 63
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1061385493  146 LNSRGAAVGIETACSSSLVAFHLARQAIQSGETKLALVCGANHVGSRSFHSLYNSH 201
Cdd:cd00829     64 GLLGKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGR 119
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
3206-3351 1.55e-06

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 52.89  E-value: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVIL--ISRRQPTAKALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGI 3280
Cdd:PRK05557     9 LVTGASRGIGRAIAERLAAQGA-NVVInyASSEAGAEALVAEIGALGGKALAVQGDVSDAEsveRAVDEAKAEFGGVDIL 87
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1061385493 3281 IHSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHF----NYKIenfIMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:PRK05557    88 VNNAGITRDNLLMRMKEEDWDRVIDTNLTGvFNLTKAVARPMmkqrSGRI---INISSVVGLMGNPGQANYAASKA 160
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
3206-3358 1.62e-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: 1.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAK-ALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:cd05347      9 LVTGASRGIGFGIASGLAEAGA-NIVINSRNEEKAEeAQQLIEKEGVEATAFTCDVSDEEaikAAVEAIEEDFGKIDILV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHF----NYKIEN---------FIMMSSFTAACGNEGQLNYG 3347
Cdd:cd05347     88 NNAGIIRRHPAEEFPEAEWRDVIDVNLNGvFFVSQAVARHMikqgHGKIINicsllselgGPPVPAYAASKGGVAGLTKA 167
                          170
                   ....*....|.
gi 1061385493 3348 VSNAYLEYQVQ 3358
Cdd:cd05347    168 LATEWARHGIQ 178
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
376-431 3.98e-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: 3.98e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1061385493  376 NRVAISSYGFGGTNACAIIEKPEKPSLVQKESYAESNVLFLSAKSHESLKLQIEEY 431
Cdd:pfam16197   25 GIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKALLEKL 80
PRK12826 PRK12826
SDR family oxidoreductase;
3206-3351 5.00e-06

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 51.07  E-value: 5.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADINDKEKL---IRELTKLNVGITGIIH 3282
Cdd:PRK12826    10 LVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALkaaVAAGVEDFGRLDILVA 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1061385493 3283 SAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFnyKIENF---IMMSSFTA-ACGNEGQLNYGVSNA 3351
Cdd:PRK12826    90 NAGIFPLTPFAEMDDEQWERVIDVNLTGtFLLTQAALPAL--IRAGGgriVLTSSVAGpRVGYPGLAHYAASKA 161
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
730-803 5.25e-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: 47.16  E-value: 5.25e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493  730 SDAEIESTVRTIVKQFLDIEEDDI----NLLETGAVDSLTSIEMVEAFGTAVNQTMPFDLLEAYPTILNIVDFLKTLV 803
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEItpddSFFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2949-3016 6.36e-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: 46.40  E-value: 6.36e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 2949 EIRRKVSlAVFDLATETLSAEDlqskGFTELGMDSLSIVDFVNRLNDKYfpDDEITASDIFDYPTVDE 3016
Cdd:pfam00550    2 RLRELLA-EVLGVPAEEIDPDT----DLFDLGLDSLLAVELIARLEEEF--GVEIPPSDLFEHPTLAE 62
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
3205-3304 7.25e-06

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: 7.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3205 WLITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALREfEHwKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:COG4221      8 ALITGASSGIGAATARALAAAGA-RVVLAARRAERLEALAA-EL-GGRALAVPLDVTDEAaveAAVAAAVAEFGRLDVLV 84
                           90       100
                   ....*....|....*....|...
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQVF 3304
Cdd:COG4221     85 NNAGVALLGPLEELDPEDWDRMI 107
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
3206-3414 1.70e-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: 49.64  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALRE--FEHWKSKVHTIAADINDKEK---LIRELTKLNVGITGI 3280
Cdd:cd08930      6 LITGAAGLIGKAFCKALLSAGA-RLILADINAPALEQLKEelTNLYKNRVIALELDITSKESikeLIESYLEKFGRIDIL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3281 IHSAGV---LKDSKIERQNKESFNQVFTPKANGFHVL-EEIEKHF-NYKIENFIMMSSFTAACGNEgQLNYGVSNAY--L 3353
Cdd:cd08930     85 INNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCsQAFIKLFkKQGKGSIINIASIYGVIAPD-FRIYENTQMYspV 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1061385493 3354 EYQVqrrrrqGKSGcAIQWGNWIDTGMAtDENVR-KFLANLGFLGQHNKDALKYLRACILTK 3414
Cdd:cd08930    164 EYSV------IKAG-IIHLTKYLAKYYA-DTGIRvNAISPGGILNNQPSEFLEKYTKKCPLK 217
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
963-1141 2.85e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 49.99  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  963 AGRLAVLMGIRGRAMIVDTTCSSVATALEMAVKSIREGRKFAIVA--TSQLIQSSKW----LYSLKTLLDH-HSTNS-FS 1034
Cdd:PRK09116   144 AVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAggAEELCPTEAAvfdtLFATSTRNDApELTPRpFD 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1035 VDGSGFCRSDGVGVIILKTAE--KGDSAVI--KISSAKSHHCGAVMT-PVVSS----ISQLLEEAG----SFSYVEGHGT 1101
Cdd:PRK09116   224 ANRDGLVIGEGAGTLVLEELEhaKARGATIyaEIVGFGTNSDGAHVTqPQAETmqiaMELALKDAGlapeDIGYVNAHGT 303
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1061385493 1102 ATSAGDSAESMAYQKL-GSELIMSSVKAQFGHCEVASGLIQ 1141
Cdd:PRK09116   304 ATDRGDIAESQATAAVfGARMPISSLKSYFGHTLGACGALE 344
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
2174-2282 3.00e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 50.01  E-value: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2174 IDYWEAHGTGTPLGDPIEFNTLSSI----LQNIIIGSVKASLGHGEASAGTC-GLLKLFLMLTYQYVPTlihfhvLNKDI 2248
Cdd:PRK06501   309 IDYINAHGTSTPENDKMEYLGLSAVfgerLASIPVSSNKSMIGHTLTAAGAVeAVFSLLTIQTGRLPPT------INYDN 382
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1061385493 2249 NAGSIRLPIIGEDSE--LVSAGIS-SFGVSGTNAAAI 2282
Cdd:PRK06501   383 PDPAIPLDVVPNVARdaRVTAVLSnSFGFGGQNASLV 419
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
2174-2280 3.02e-05

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 50.05  E-value: 3.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2174 IDYWEAHGTGTPLGDPIEFNTLSSILQNII--IGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHVLNKDInAG 2251
Cdd:PRK07967   291 IDYINTHGTSTPVGDVKELGAIREVFGDKSpaISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQA-AG 369
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1061385493 2252 sirLPIIG---EDSELVSAGISSFGVSGTNAA 2280
Cdd:PRK07967   370 ---MPIVTettDNAELTTVMSNSFGFGGTNAT 398
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
3204-3333 3.47e-05

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 49.21  E-value: 3.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3204 NWLITGGLSGIGLEIGKFIANNGAEnVILISRRQPTAKALREFEHwkskVHTIAADINDKEKLIRELTklnvGITGIIHS 3283
Cdd:COG0451      1 RILVTGGAGFIGSHLARRLLARGHE-VVGLDRSPPGAANLAALPG----VEFVRGDLRDPEALAAALA----GVDAVVHL 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1061385493 3284 AGVlkdSKIERQNKESFNQVFtpkANGF-HVLEEIEKHfnyKIENFIMMSS 3333
Cdd:COG0451     72 AAP---AGVGEEDPDETLEVN---VEGTlNLLEAARAA---GVKRFVYASS 113
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
2022-2280 4.49e-05

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 49.41  E-value: 4.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2022 MLGSMAAviaGRVNYIFGCYGPSVTIDTACSSSLVALEMAINaLLDNRCSKVIVAG--------VNLILNEKGQGLRTNG 2093
Cdd:PLN02836   158 ILINMAA---GHVSIRYGFQGPNHAAVTACATGAHSIGDAFR-MIQFGDADVMVAGgtessidaLSIAGFSRSRALSTKF 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2094 KMLSQHGmSLSFDSRASGYGRSDGCVVLMLEL---AKPNFHYM-STIQSVNVNHGGRSVSLTAPNGVAHKMLLTSVINQS 2169
Cdd:PLN02836   234 NSCPTEA-SRPFDCDRDGFVIGEGAGVLVLEElehAKRRGAKIyAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQS 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2170 ---PSlAIDYWEAHGTGTPLGDPIEFNTLSSIL------QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIH 2240
Cdd:PLN02836   313 glhPN-QVDYVNAHATSTPLGDAVEARAIKTVFsehatsGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLN 391
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1061385493 2241 FHVLNKDINAGSIrlPIIGEDSELVSAGIS-SFGVSGTNAA 2280
Cdd:PLN02836   392 LERPDPIFDDGFV--PLTASKAMLIRAALSnSFGFGGTNAS 430
PRK09072 PRK09072
SDR family oxidoreductase;
3206-3305 4.64e-05

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 48.40  E-value: 4.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALREFEHWKSKVHTIAADINDKE--KLIRELTKLNVGITGIIHS 3283
Cdd:PRK09072     9 LLTGASGGIGQALAEALAAAGA-RLLLVGRNAEKLEALAARLPYPGRHRWVVADLTSEAgrEAVLARAREMGGINVLINN 87
                           90       100
                   ....*....|....*....|..
gi 1061385493 3284 AGVLKDSKIERQNKESFNQVFT 3305
Cdd:PRK09072    88 AGVNHFALLEDQDPEAIERLLA 109
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
3206-3323 4.68e-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: 48.37  E-value: 4.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALRE---FEHWKSKVHTIAADIND-------KEKLIRELTKLNV 3275
Cdd:cd05327      5 VITGANSGIGKETARELAKRGA-HVIIACRNEEKGEEAAAeikKETGNAKVEVIQLDLSSlasvrqfAEEFLARFPRLDI 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3276 gitgIIHSAGVlkdskierqnkesFNQVFTPKANGFhvleeiEKHF--NY 3323
Cdd:cd05327     84 ----LINNAGI-------------MAPPRRLTKDGF------ELQFavNY 110
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3351 5.01e-05

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 48.03  E-value: 5.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPT-AKALREFEHWKSKVHTIAADINDKEKLIRELTKLNV---GITGII 3281
Cdd:PRK08217     9 VITGGAQGLGRAMAEYLAQKGA-KLALIDLNQEKlEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEdfgQLNGLI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3282 HSAGVL--------KDSKI-ERQNKESFNQVFTPKANG-FHVLEEIEKHFnykIEN-----FIMMSSFTAAcGNEGQLNY 3346
Cdd:PRK08217    88 NNAGILrdgllvkaKDGKVtSKMSLEQFQSVIDVNLTGvFLCGREAAAKM---IESgskgvIINISSIARA-GNMGQTNY 163

                   ....*
gi 1061385493 3347 GVSNA 3351
Cdd:PRK08217   164 SASKA 168
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
4359-4438 6.00e-05

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: 6.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4359 IYLVHAIGGTIYPYYSFLQIFPKDislyGIE-FDLKYPSNDL------RELAHFyAEEIAAHAGNKRIFVMGHSMGGIMS 4431
Cdd:COG1075      8 VVLVHGLGGSAASWAPLAPRLRAA----GYPvYALNYPSTNGsiedsaEQLAAF-VDAVLAATGAEKVDLVGHSMGGLVA 82

                   ....*..
gi 1061385493 4432 REIVAEL 4438
Cdd:COG1075     83 RYYLKRL 89
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
3206-3351 6.08e-05

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 48.08  E-value: 6.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADIN---DKEKLIRElTKLNVGITGI- 3280
Cdd:PRK12935    10 IVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLvNELGKEGHDVYAVQADVSkveDANRLVEE-AVNHFGKVDIl 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1061385493 3281 IHSAGVLKDSKIERQNKESFNQVFtpKANGFHVLEEIEKHFNYKIEN----FIMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:PRK12935    89 VNNAGITRDRTFKKLNREDWERVI--DVNLSSVFNTTSAVLPYITEAeegrIISISSIIGQAGGFGQTNYSAAKA 161
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
3206-3353 6.19e-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: 6.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALR-EFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:cd05350      2 LITGASSGIGRALAREFAKAGY-NVALAARRTDRLDELKaELLNPNPSVEVEILDVTDEErnqLVIAELEAELGGLDLVI 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQVFTPKANGFHV-LEEIEKHFNYKIENFI-MMSSFTAACGNEGQLNYGVSNAYL 3353
Cdd:cd05350     81 INAGVGKGTSLGDLSFKAFRETIDTNLLGAAAiLEAALPQFRAKGRGHLvLISSVAALRGLPGAAAYSASKAAL 154
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
2031-2282 6.90e-05

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 48.57  E-value: 6.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2031 AGRVNYIFGCYGPSVTIDTACSSSLVALEMAINALLDNRCSKVIVAGVNLILNEKGQGLRTNGKMLSQH------GMSLS 2104
Cdd:PRK14691    71 AGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfnstpeKASRP 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2105 FDSRASGYGRSDGCVVLMLEL--------AKPNFHYMSTIQSVNVNHggrsVSLTAPNGVAHKMLLTSVINQ---SPSlA 2173
Cdd:PRK14691   151 FDTARDGFVMGEGAGLLIIEElehalargAKPLAEIVGYGTSADAYH----MTSGAEDGDGAYRAMKIALRQagiTPE-Q 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2174 IDYWEAHGTGTPLGDPIEFNTLSSIL---QNIIIGSVKASLGHGEASAGTCGLLKLFLMLTYQYVPTLIHFHvlNKDINA 2250
Cdd:PRK14691   226 VQHLNAHATSTPVGDLGEINAIKHLFgesNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLE--NPDPAA 303
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1061385493 2251 GSIRLpIIG--EDSELVSAGISSFGVSGTNAAAI 2282
Cdd:PRK14691   304 KGLNI-IAGnaQPHDMTYALSNGFGFAGVNASIL 336
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
3206-3358 7.43e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 47.75  E-value: 7.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADINDKEKLIRELTKL--NVGITGI-IH 3282
Cdd:PRK07097    14 LITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIekEVGVIDIlVN 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3283 SAGVLKDSKIERQNKESFNQVFTPKANG-F----HVLEEIEKHFNYKIENFI-MMS--------SFTAACGNEGQLNYGV 3348
Cdd:PRK07097    94 NAGIIKRIPMLEMSAEDFRQVIDIDLNApFivskAVIPSMIKKGHGKIINICsMMSelgretvsAYAAAKGGLKMLTKNI 173
                          170
                   ....*....|
gi 1061385493 3349 SNAYLEYQVQ 3358
Cdd:PRK07097   174 ASEYGEANIQ 183
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
3206-3304 7.70e-05

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: 7.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAEnVILISRRQPTAKALREFEHwksKVHTIAADINDKEK---LIRELTKLNVGITGIIH 3282
Cdd:cd08932      4 LVTGASRGIGIEIARALARDGYR-VSLGLRNPEDLAALSASGG---DVEAVPYDARDPEDaraLVDALRDRFGRIDVLVH 79
                           90       100
                   ....*....|....*....|..
gi 1061385493 3283 SAGVLKDSKIERQNKESFNQVF 3304
Cdd:cd08932     80 NAGIGRPTTLREGSDAELEAHF 101
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
3206-3355 8.38e-05

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: 8.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:cd05362      7 LVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVvAEIEAAGGKAIAVQADVSDPSqvaRLFDAAEKAFGGVDILV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHF--NYKIENFimMSSFTAAcgneGQLNYGV---SNAYLEY 3355
Cdd:cd05362     87 NNAGVMLKKPIAETSEEEFDRMFTVNTKGaFFVLQEAAKRLrdGGRIINI--SSSLTAA----YTPNYGAyagSKAAVEA 160
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
3206-3351 8.77e-05

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 47.45  E-value: 8.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGaeNVILISRRQPTAKALR---EFEHWKSKVHTIAADINDKEKLIRELTKL---NVGITG 3279
Cdd:PRK12824     6 LVTGAKRGIGSAIARELLNDG--YRVIATYFSGNDCAKDwfeEYGFTEDQVRLKELDVTDTEECAEALAEIeeeEGPVDI 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1061385493 3280 IIHSAGVLKDSKIERQNKESFNQVFTPKANG-FHV----LEEIEKHFNYKIENfimMSSFTAACGNEGQLNYGVSNA 3351
Cdd:PRK12824    84 LVNNAGITRDSVFKRMSHQEWNDVINTNLNSvFNVtqplFAAMCEQGYGRIIN---ISSVNGLKGQFGQTNYSAAKA 157
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
3206-3273 9.21e-05

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: 47.27  E-value: 9.21e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALR-EF-EHWKSKVHTIAADINDKEKLIRELTKL 3273
Cdd:cd05346      4 LITGASSGIGEATARRFAKAGA-KLILTGRRAERLQELAdELgAKFPVKVLPLQLDVSDRESIEAALENL 72
PRK06198 PRK06198
short chain dehydrogenase; Provisional
3206-3333 1.01e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 47.31  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:PRK06198    10 LVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQaAELEALGAKAVFVQADLSDVEdcrRVVAAADEAFGRLDALV 89
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHFNYK-----IENFIMMSS 3333
Cdd:PRK06198    90 NAAGLTDRGTILDTSPELFDRHFAVNVRApFFLMQEAIKLMRRRkaegtIVNIGSMSA 147
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
3206-3279 1.37e-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: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRR----QPTAKALREFEhwKSKVHTIAADINDKE-------KLIRELTKLN 3274
Cdd:cd05369      7 FITGGGTGIGKAIAKAFAELGA-SVAIAGRKpevlEAAAEEISSAT--GGRAHPIQCDVRDPEaveaavdETLKEFGKID 83

                   ....*
gi 1061385493 3275 VGITG 3279
Cdd:cd05369     84 ILINN 88
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
3206-3289 1.53e-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: 46.53  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAEnVILISRRQptaKALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGIIH 3282
Cdd:cd05370      9 LITGGTSGIGLALARKFLEAGNT-VIITGRRE---ERLAEAKKELPNIHTIVLDVGDAEsveALAEALLSEYPNLDILIN 84

                   ....*..
gi 1061385493 3283 SAGVLKD 3289
Cdd:cd05370     85 NAGIQRP 91
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
3206-3321 1.98e-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: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVIlISRRQPTAKALREFEHWKSKVHTIAADINDKE---KLIRELTKLNVGITGIIH 3282
Cdd:cd05349      4 LVTGASRGLGAAIARSFAREGA-RVV-VNYYRSTESAEAVAAEAGERAIAIQADVRDRDqvqAMIEEAKNHFGPVDTIVN 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1061385493 3283 SAGV------LKDSKIERQNKESFNQVFTPKANG-FHVLEEIEKHF 3321
Cdd:cd05349     82 NALIdfpfdpDQRKTFDTIDWEDYQQQLEGAVKGaLNLLQAVLPDF 127
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3304 2.18e-04

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 46.37  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADI---NDKEKLIRELTKLNVGITGII 3281
Cdd:PRK05565     9 IVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELlEEIKEEGGDAIAVKADVsseEDVENLVEQIVEKFGKIDILV 88
                           90       100
                   ....*....|....*....|...
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQVF 3304
Cdd:PRK05565    89 NNAGISNFGLVTDMTDEEWDRVI 111
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
4359-4454 2.51e-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: 2.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4359 IYLVHAIGGTIYPYYSFLQIFPKDISLYGIEfdlkYPS--------NDLRELAHFYAEEIAAHAGNKRIFVMGHSMGGIM 4430
Cdd:pfam00975    3 LFCFPPAGGSASSFRSLARRLPPPAEVLAVQ----YPGrgrgepplNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78
                           90       100
                   ....*....|....*....|....
gi 1061385493 4431 SREIVAELKIWGYDIPFVMLFDSW 4454
Cdd:pfam00975   79 AFEVARRLERQGEAVRSLFLSDAS 102
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
736-792 2.81e-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: 41.78  E-value: 2.81e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061385493  736 STVRTIVKQFLDIEEDDI----NLLETGaVDSLTSIEMVEAFGTAVNQTMPFDLLEAYPTI 792
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIdpdtDLFDLG-LDSLLAVELIARLEEEFGVEIPPSDLFEHPTL 60
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
3205-3286 3.20e-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: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3205 WLITGGLSGIGLEIGKFIANNGAeNVILISRR----QPTAKALREFehWKSKVHTIAAD---INDKEKLIRELTKLNVGI 3277
Cdd:cd05332      6 VIITGASSGIGEELAYHLARLGA-RLVLSARReerlEEVKSECLEL--GAPSPHVVPLDmsdLEDAEQVVEEALKLFGGL 82

                   ....*....
gi 1061385493 3278 TGIIHSAGV 3286
Cdd:cd05332     83 DILINNAGI 91
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
3204-3351 3.90e-04

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 45.77  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3204 NWL--------ITGGLSGIGLEIGKFIANNGAeNVILISRRQptakalREFEHwkSKVHTIAADINDK---EKLIRELTK 3272
Cdd:PRK06171     3 DWLnlqgkiiiVTGGSSGIGLAIVKELLANGA-NVVNADIHG------GDGQH--ENYQFVPTDVSSAeevNHTVAEIIE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3273 LNVGITGIIHSAGV-----LKDSKIERQ----NKESFNQVFTPKANG-FHVLEEIEKHFNYKIENFIM-MSSFTAACGNE 3341
Cdd:PRK06171    74 KFGRIDGLVNNAGIniprlLVDEKDPAGkyelNEAAFDKMFNINQKGvFLMSQAVARQMVKQHDGVIVnMSSEAGLEGSE 153
                          170
                   ....*....|
gi 1061385493 3342 GQLNYGVSNA 3351
Cdd:PRK06171   154 GQSCYAATKA 163
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
2940-3024 4.33e-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: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2940 ESDATVDRTEIRRKVSlAVFDLATETLSAEDlqskGFTELGMDSLSIVDFVNRLNDKYFpddEITASDIFDYPTVDELSD 3019
Cdd:COG3433    214 ALETALTEEELRADVA-ELLGVDPEEIDPDD----NLFDLGLDSIRLMQLVERWRKAGL---DVSFADLAEHPTLAAWWA 285

                   ....*
gi 1061385493 3020 HIVRK 3024
Cdd:COG3433    286 LLAAA 290
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
4263-4336 5.83e-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: 41.38  E-value: 5.83e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 4263 KNSLEEKVINVFSKILGRN---VAPTDKF-ESIGGNSLNAIQIAHRLAEELKIEIKAHEILQSNSLKTFCNTLKNSVQ 4336
Cdd:COG0236      3 REELEERLAEIIAEVLGVDpeeITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
3205-3285 5.92e-04

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: 5.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3205 WLITGGLSGIGLEIGKFIANNGaENVILISRRQPTAKALREFehWKSKVHTIAADINDKE---KLIRELTKLNVGITGII 3281
Cdd:cd05374      3 VLITGCSSGIGLALALALAAQG-YRVIATARNPDKLESLGEL--LNDNLEVLELDVTDEEsikAAVKEVIERFGRIDVLV 79

                   ....
gi 1061385493 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 7.49e-04

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: 7.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANN-GAENVILISRRQPTAKAlreFEHWKSkvhtIAADINDKEKLiRELTKlNVGITGIIHSA 3284
Cdd:cd05272      3 LITGGLGQIGSELAKLLRKRyGKDNVIASDIRKPPAHV---VLSGPF----EYLDVLDFKSL-EEIVV-NHKITWIIHLA 73

                   ...
gi 1061385493 3285 GVL 3287
Cdd:cd05272     74 ALL 76
PRK12939 PRK12939
short chain dehydrogenase; Provisional
3206-3354 9.12e-04

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 44.19  E-value: 9.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAE---NVILISRRQPTAKALREFEHwksKVHTIAADINDKEKLIR---ELTKLNVGITG 3279
Cdd:PRK12939    11 LVTGAARGLGAAFAEALAEAGATvafNDGLAAEARELAAALEAAGG---RAHAIAADLADPASVQRffdAAAAALGGLDG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 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 9.81e-04

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: 9.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADINDKEKLIR--ELTKLNVG-ITGIIH 3282
Cdd:cd05339      3 LITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEaaKKIKKEVGdVTILIN 82
                           90       100
                   ....*....|....*....|..
gi 1061385493 3283 SAGVLKDSKIERQNKESFNQVF 3304
Cdd:cd05339     83 NAGVVSGKKLLELPDEEIEKTF 104
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
4363-4438 9.81e-04

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 44.07  E-value: 9.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 4363 HAiGGTIYPYYSFLQIFPKDISLYGIEfdlkYPS----------NDLRELAHFYAEEIAAHAgNKRIFVMGHSMGGIMSR 4432
Cdd:COG3208     14 YA-GGSASAYRPWAAALPPDIEVLAVQ----LPGrgdrlgepplTSLEELADDLAEELAPLL-DRPFALFGHSMGALLAF 87

                   ....*.
gi 1061385493 4433 EIVAEL 4438
Cdd:COG3208     88 ELARRL 93
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
3206-3354 1.08e-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: 43.94  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRR----QPTAKALREFEHWKSKVHTIAADINDKEKL--IRELT-----KLN 3274
Cdd:cd05364      7 IITGSSSGIGAGTAILFARLGA-RLALTGRDaerlEETRQSCLQAGVSEKKILLVVADLTEEEGQdrIISTTlakfgRLD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3275 VgitgIIHSAGVLKDSKIERQNKESFNQVFtpKANGFHVLEEIEKHFNYKIE---NFIMMSSFTAACGNEGQLNYGVSNA 3351
Cdd:cd05364     86 I----LVNNAGILAKGGGEDQDIEEYDKVM--NLNLRAVIYLTKLAVPHLIKtkgEIVNVSSVAGGRSFPGVLYYCISKA 159

                   ...
gi 1061385493 3352 YLE 3354
Cdd:cd05364    160 ALD 162
PRK06500 PRK06500
SDR family oxidoreductase;
3206-3304 1.27e-03

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 43.79  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAEnVILISRRQPT-AKALREFEHWKSKVHTIAADINDKEKLIRELTKLNVGITGIIHSA 3284
Cdd:PRK06500    10 LITGGTSGIGLETARQFLAEGAR-VAITGRDPASlEAARAELGESALVIRADAGDVAAQKALAQALAEAFGRLDAVFINA 88
                           90       100
                   ....*....|....*....|
gi 1061385493 3285 GVLKDSKIERQNKESFNQVF 3304
Cdd:PRK06500    89 GVAKFAPLEDWDEAMFDRSF 108
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
837-1138 1.35e-03

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 44.60  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  837 AGVEgekELWDTLLTSRltTGkISDIRKKQCEGDA---GLEVGLLKQDISMFDNSFFAIAKDEAEFLDPQHRLLLNAAYN 913
Cdd:PRK06333    19 CGVE---TFWQRLLAGQ--SG-IRTLTDFPVGDLAtkiGGQVPDLAEDAEAGFDPDRYLDPKDQRKMDRFILFAMAAAKE 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  914 ALEKSGL--TSIPDADLFLAI--SAHSEYRALAEKhINELDE----RLWMGTVHS----MVAGRLAVLMGIRGRAMIVDT 981
Cdd:PRK06333    93 ALAQAGWdpDTLEDRERTATIigSGVGGFPAIAEA-VRTLDSrgprRLSPFTIPSfltnMAAGHVSIRYGFKGPLGAPVT 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493  982 TCSSVATALEMAVKSIREGRkfAIVATSQLIQSSKWLYSL------KTLLDH------HSTNSFSVDGSGFCRSDGVGVI 1049
Cdd:PRK06333   172 ACAAGVQAIGDAARLIRSGE--ADVAVCGGTEAAIDRVSLagfaaaRALSTRfndapeQASRPFDRDRDGFVMGEGAGIL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 1050 ILKTAE----KGDSAVIKI----SSAKSHHcgavMTP-------VVSSISQLLEEAG----SFSYVEGHGTATSAGDSAE 1110
Cdd:PRK06333   250 VIETLEhalaRGAPPLAELvgygTSADAYH----MTAgpedgegARRAMLIALRQAGippeEVQHLNAHATSTPVGDLGE 325
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1061385493 1111 SMAYQKL---GSELIMSSVKAQFGHCEVASG 1138
Cdd:PRK06333   326 VAAIKKVfghVSGLAVSSTKSATGHLLGAAG 356
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3310 1.42e-03

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 43.62  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREfehwkSKVHTIAADINDKE---KLIRELTKLNVGITGIIH 3282
Cdd:PRK06463    11 LITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELRE-----KGVFTIKCDVGNRDqvkKSKEVVEKEFGRVDVLVN 85
                           90       100
                   ....*....|....*....|....*...
gi 1061385493 3283 SAGVLKDSKIERQNKESFNQVFTPKANG 3310
Cdd:PRK06463    86 NAGIMYLMPFEEFDEEKYNKMIKINLNG 113
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
2779-2872 1.48e-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: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2779 TLLSSQEASIVAAKTLQMAVRHKVCLAVGDVIESG---LDIDESqlstgFSELGIDSLATVDLLNRLNQKyfpEIELTTS 2855
Cdd:COG3433    201 AAEALLAAASPAPALETALTEEELRADVAELLGVDpeeIDPDDN-----LFDLGLDSIRLMQLVERWRKA---GLDVSFA 272
                           90
                   ....*....|....*..
gi 1061385493 2856 DLFDNPSIIDLSIMIEQ 2872
Cdd:COG3433    273 DLAEHPTLAAWWALLAA 289
PRK08628 PRK08628
SDR family oxidoreductase;
3206-3286 1.67e-03

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 43.41  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILiSRRQPTAKALREFEHWKSKVHTIAADINDK---EKLIRELTKLNVGITGIIH 3282
Cdd:PRK08628    11 IVTGGASGIGAAISLRLAEEGAIPVIF-GRSAPDDEFAEELRALQPRAEFVQVDLTDDaqcRDAVEQTVAKFGRIDGLVN 89

                   ....
gi 1061385493 3283 SAGV 3286
Cdd:PRK08628    90 NAGV 93
PRK08219 PRK08219
SDR family oxidoreductase;
3206-3304 1.67e-03

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 43.38  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIAnnGAENVILISRRQPTAKALREfEHwkSKVHTIAADINDKEKLIRELTKLnVGITGIIHSAG 3285
Cdd:PRK08219     7 LITGASRGIGAAIARELA--PTHTLLLGGRPAERLDELAA-EL--PGATPFPVDLTDPEAIAAAVEQL-GRLDVLVHNAG 80
                           90
                   ....*....|....*....
gi 1061385493 3286 VLKDSKIERQNKESFNQVF 3304
Cdd:PRK08219    81 VADLGPVAESTVDEWRATL 99
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
155-186 1.89e-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: 1.89e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1061385493  155 IETACSSSLVAFHLARQAIQSGETKLALVCGA 186
Cdd:pfam08545    3 INAACSGFVYALSTAAALIRSGRAKNVLVIGA 34
PRK12746 PRK12746
SDR family oxidoreductase;
3206-3353 3.02e-03

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 42.71  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTA-KALREFEHWKSKVHTIAADINDKE---KLIRELT---KLNVGIT 3278
Cdd:PRK12746    10 LVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAAdETIREIESNGGKAFLIEADLNSIDgvkKLVEQLKnelQIRVGTS 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 3279 GI---IHSAGVLKDSKIERQNKESFNQVFTPKANGFHVLEEIEKHFNYKIENFIMMSSFTAACGNEGQLNYGVSNAYL 3353
Cdd:PRK12746    90 EIdilVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEGRVINISSAEVRLGFTGSIAYGLSKGAL 167
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
3206-3268 4.04e-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: 4.04e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQP--TAKALREFEHwKSKVHTIAADINDKEKLIR 3268
Cdd:cd05323      4 IITGGASGIGLATAKLLLKKGA-KVAILDRNENpgAAAELQAINP-KVKATFVQCDVTSWEQLAA 66
PRK07326 PRK07326
SDR family oxidoreductase;
3206-3303 4.08e-03

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 42.31  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAEnVILISRRQPT-AKALREFEHwKSKVHTIAADI---NDKEKLIRELTKLNVGITGII 3281
Cdd:PRK07326    10 LITGGSKGIGFAIAEALLAEGYK-VAITARDQKElEEAAAELNN-KGNVLGLAADVrdeADVQRAVDAIVAAFGGLDVLI 87
                           90       100
                   ....*....|....*....|..
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQV 3303
Cdd:PRK07326    88 ANAGVGHFAPVEELTPEEWRLV 109
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
3212-3354 5.71e-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: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3212 SGIGLEIGKFIANNGAEnVILISRRQPTAKALREF-EHWKSKVhtIAADINDKE---KLIRELTKLNVGITGIIHSAGVL 3287
Cdd:pfam13561    6 SGIGWAIARALAEEGAE-VVLTDLNEALAKRVEELaEELGAAV--LPCDVTDEEqveALVAAAVEKFGRLDILVNNAGFA 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1061385493 3288 KDSK--IERQNKESFNQVFTPKANGFH-VLEEIEKHFNykiEN--FIMMSSFTAACGNEGQLNYGVSNAYLE 3354
Cdd:pfam13561   83 PKLKgpFLDTSREDFDRALDVNLYSLFlLAKAALPLMK---EGgsIVNLSSIGAERVVPNYNAYGAAKAALE 151
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
2267-2347 6.22e-03

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: 39.45  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 2267 AGISSFGVSGTNAAAI-AFNDNNKLEPYIPIHKYYILPISAKNQISLDNLEKQILSvIPLTDVPICNIASALANNRSHFT 2345
Cdd:pfam16197   27 VGVNSFGFGGANAHVIlKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKALLEKLEN-HLDDAEFLSLLNDIHSLPISGHP 105

                   ..
gi 1061385493 2346 IR 2347
Cdd:pfam16197  106 YR 107
PRK06101 PRK06101
SDR family oxidoreductase;
3206-3273 6.33e-03

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 41.78  E-value: 6.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAEnVILISRRQptaKALREFEHWKSKVHTIAADINDKEKLIRELTKL 3273
Cdd:PRK06101     5 LITGATSGIGKQLALDYAKQGWQ-VIACGRNQ---SVLDELHTQSANIFTLAFDVTDHPGTKAALSQL 68
PRK07201 PRK07201
SDR family oxidoreductase;
3179-3264 6.52e-03

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 42.63  E-value: 6.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3179 PLISFA------WYQNVQQVSFVDSDS--PITG-NWLITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKALR-EFEH 3248
Cdd:PRK07201   339 RLASYAprlwdyWERHLDPDRARRRDLrgPLVGkVVLITGASSGIGRATAIKVAEAGA-TVFLVARNGEALDELVaEIRA 417
                           90
                   ....*....|....*.
gi 1061385493 3249 WKSKVHTIAADINDKE 3264
Cdd:PRK07201   418 KGGTAHAYTCDLTDSA 433
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3206-3352 6.69e-03

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 41.60  E-value: 6.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQPTAKAL-REFEHWKSKVHTIAADINDKEKLIRELTKLNVGITGI---I 3281
Cdd:PRK07666    11 LITGAGRGIGRAVAIALAKEGV-NVGLLARTEENLKAVaEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGSIdilI 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQVFtpKANGFHVLEEIEKHFNYKIE----NFIMMSSfTAacgneGQLNYGVSNAY 3352
Cdd:PRK07666    90 NNAGISKFGKFLELDPAEWEKII--QVNLMGVYYATRAVLPSMIErqsgDIINISS-TA-----GQKGAAVTSAY 156
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1806-1848 6.80e-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: 37.93  E-value: 6.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1061385493 1806 DIDNTTGFFDLGLTSIQAVKLRNAIKSNYP-NASSTCVFDYPSI 1848
Cdd:pfam00550   17 EIDPDTDLFDLGLDSLLAVELIARLEEEFGvEIPPSDLFEHPTL 60
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
3206-3305 7.13e-03

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and 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: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 41.59  E-value: 7.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKAL-REFEHWKSKVHTIAADINDK---EKLIRELTKLNVGITGII 3281
Cdd:cd05366      6 IITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTiQEISEAGYNAVAVGADVTDKddvEALIDQAVEKFGSFDVMV 85
                           90       100
                   ....*....|....*....|....
gi 1061385493 3282 HSAGVLKDSKIERQNKESFNQVFT 3305
Cdd:cd05366     86 NNAGIAPITPLLTITEEDLKKVYA 109
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
3206-3268 9.02e-03

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. 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: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 41.10  E-value: 9.02e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAENVILISRRQPTAKALREFEHWKSKVHTIAADINDKEKLIR 3268
Cdd:cd05344      5 LVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDR 67
PRK07516 PRK07516
thiolase domain-containing protein;
152-186 9.43e-03

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 41.86  E-value: 9.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1061385493  152 AVGIETACSSSLVAFHLARQAIQSGETKLALVCGA 186
Cdd:PRK07516    78 ATRVENACATGSAAVYAALDAIEAGRARIVLVVGA 112
FabG-like PRK07231
SDR family oxidoreductase;
3206-3264 9.80e-03

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 40.97  E-value: 9.80e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1061385493 3206 LITGGLSGIGLEIGKFIANNGAeNVILISRRQ----PTAKALREFEHwkskVHTIAADINDKE 3264
Cdd:PRK07231     9 IVTGASSGIGEGIARRFAAEGA-RVVVTDRNEeaaeRVAAEILAGGR----AIAVAADVSDEA 66
 
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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