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Conserved domains on  [gi|71425875|ref|XP_813186|]
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beta-ketoacyl synthase family protein, putative [Trypanosoma cruzi]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase family protein( domain architecture ID 11487926)

beta-ketoacyl-[acyl-carrier-protein] synthase family protein may catalyze the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
23-465 0e+00

3-oxoacyl-acyl carrier protein synthase; Provisional


:

Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 662.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   23 AVTPLGLDVASTWAALCQGRSATRPLKEVPFFFPACIDsdcrltpaaRQKSHEQLLAKMPCQVAAPVLAPSGGPN-FTPT 101
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIP---------EQKALENLVAAMPCQIAAEVDQSEFDPSdFAPT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  102 LRETRATLFAYYAAEEALTHAKLLespakrILASFAKERIGVNIGVGMPSLADVGDVSYSLYADpekvNYSRVNPLFVPK 181
Cdd:PTZ00050  72 KRESRATHFAMAAAREALADAKLD------ILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEK----GHSRVSPYFIPK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  182 ILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCTKYNGMP 261
Cdd:PTZ00050 142 ILGNMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNDDP 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  262 QEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEDGGNISI 341
Cdd:PTZ00050 222 QRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINI 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  342 NDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLH 420
Cdd:PTZ00050 302 NDVDYVNAHATSTpIGDKIELKAIKKVFGDSGA----PKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLE 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 71425875  421 APSAEGLerLQLVRGHAPLPFQG-DAVISTSFGFGGVNTALLFTRV 465
Cdd:PTZ00050 378 NPDAECD--LNLVQGKTAHPLQSiDAVLSTSFGFGGVNTALLFTKY 421
 
Name Accession Description Interval E-value
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
23-465 0e+00

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 662.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   23 AVTPLGLDVASTWAALCQGRSATRPLKEVPFFFPACIDsdcrltpaaRQKSHEQLLAKMPCQVAAPVLAPSGGPN-FTPT 101
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIP---------EQKALENLVAAMPCQIAAEVDQSEFDPSdFAPT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  102 LRETRATLFAYYAAEEALTHAKLLespakrILASFAKERIGVNIGVGMPSLADVGDVSYSLYADpekvNYSRVNPLFVPK 181
Cdd:PTZ00050  72 KRESRATHFAMAAAREALADAKLD------ILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEK----GHSRVSPYFIPK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  182 ILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCTKYNGMP 261
Cdd:PTZ00050 142 ILGNMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNDDP 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  262 QEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEDGGNISI 341
Cdd:PTZ00050 222 QRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINI 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  342 NDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLH 420
Cdd:PTZ00050 302 NDVDYVNAHATSTpIGDKIELKAIKKVFGDSGA----PKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLE 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 71425875  421 APSAEGLerLQLVRGHAPLPFQG-DAVISTSFGFGGVNTALLFTRV 465
Cdd:PTZ00050 378 NPDAECD--LNLVQGKTAHPLQSiDAVLSTSFGFGGVNTALLFTKY 421
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
14-462 1.37e-166

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: 475.49  E-value: 1.37e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKevpfFFPAcidsdcrltpaarqksheqllAKMPCQVAAPVLAPS 93
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPIT----RFDA---------------------SGFPSRIAGEVPDFD 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  94 GGPNFTP--TLRETRATLFAYYAAEEALTHAKLLEspakrilASFAKERIGVNIGVGMPSLADVGDVSYSLYADPekvnY 171
Cdd:cd00834  56 PEDYLDRkeLRRMDRFAQFALAAAEEALADAGLDP-------EELDPERIGVVIGSGIGGLATIEEAYRALLEKG----P 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 172 SRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMR 251
Cdd:cd00834 125 RRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALR 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 252 ALCTKYNgMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRS 331
Cdd:cd00834 205 ALSTRND-DPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRA 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 332 ALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGtssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYH 410
Cdd:cd00834 284 ALADAG-LSPEDIDYINAHGTSTpLNDAAESKAIKRVFGEHA-----KKVPVSSTKSMTGHLLGAAGAVEAIATLLALRD 357
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 71425875 411 QQAPPNINLHAPSAEglERLQLVRgHAPLPFQGDAVISTSFGFGGVNTALLF 462
Cdd:cd00834 358 GVLPPTINLEEPDPE--CDLDYVP-NEAREAPIRYALSNSFGFGGHNASLVF 406
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
14-465 1.23e-164

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: 470.35  E-value: 1.23e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPlkeVPFFFPAcidsdcrltpaarqksheqllaKMPCQVAAPVlaps 93
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRP---ITRFDAS----------------------GLPVRIAGEV---- 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  94 ggPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESPakrilasFAKERIGVNIGVGMPSLADVGDVSYSLYAD 165
Cdd:COG0304  52 --KDFDPEEyldrkelrRMDRFTQYALAAAREALADAGLDLDE-------VDPDRTGVIIGSGIGGLDTLEEAYRALLEK 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 166 pekvNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIA 245
Cdd:COG0304 123 ----GPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLA 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 246 GFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGA 325
Cdd:COG0304 199 GFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGA 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 326 QLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTSsrrrpVYVSSVKGGLGHLLGAAGSVEAIVA 404
Cdd:COG0304 278 ARAMRAALKDAG-LSPEDIDYINAHGTSTpLGDAAETKAIKRVFGDHAYK-----VPVSSTKSMTGHLLGAAGAIEAIAS 351
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71425875 405 IMSLYHQQAPPNINLHAPSAEglERLQLVRGHApLPFQGDAVISTSFGFGGVNTALLFTRV 465
Cdd:COG0304 352 VLALRDGVIPPTINLENPDPE--CDLDYVPNEA-REAKIDYALSNSFGFGGHNASLVFKRY 409
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
14-462 4.32e-147

beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 274452 [Multi-domain]  Cd Length: 407  Bit Score: 425.75  E-value: 4.32e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpffFPAcidsdcrltpaarqksheqllAKMPCQVAAPVlaps 93
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITR----FDA---------------------SDLPVKIAGEV---- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    94 ggPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESPAKRilasfakERIGVNIGVGMPSLADVGDVSYSLYad 165
Cdd:TIGR03150  52 --KDFDPEDyidkkearRMDRFIQYALAAAKEAVEDSGLDIEEEDA-------ERVGVIIGSGIGGLETIEEQHIVLL-- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   166 pEKvNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIA 245
Cdd:TIGR03150 121 -EK-GPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIA 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   246 GFSRMRALCTkYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGA 325
Cdd:TIGR03150 199 GFAAMKALST-RNDDPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGA 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   326 QLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGgdgtsSRRRPVYVSSVKGGLGHLLGAAGSVEAIVA 404
Cdd:TIGR03150 278 ARAMRAALKDAG-INPEDVDYINAHGTSTpLGDKAETKAIKKVFG-----DHAYKLAVSSTKSMTGHLLGAAGAIEAIFT 351
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 71425875   405 IMSLYHQQAPPNINLHAPSAEGleRLQLVRgHAPLPFQGDAVISTSFGFGGVNTALLF 462
Cdd:TIGR03150 352 VLAIRDGIVPPTINLDNPDPEC--DLDYVP-NEAREAKIDYALSNSFGFGGTNASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
14-292 4.26e-40

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: 144.70  E-value: 4.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKevpfffpacidsDCRLTPAARQKSHEQLLAKMPCQVAAPVlaps 93
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIP------------ADRWDPDKLYDPPSRIAGKIYTKWGGLD---- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    94 GGPNFTPTL-----RETRAT----LFAYYAAEEALTHAKLLEspakrilASFAKERIGVNIGVGMPSLADvgdvsysLYA 164
Cdd:pfam00109  65 DIFDFDPLFfgispREAERMdpqqRLLLEAAWEALEDAGITP-------DSLDGSRTGVFIGSGIGDYAA-------LLL 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   165 DPEKVNYSRVNPLFVPKIlGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSI 244
Cdd:pfam00109 131 LDEDGGPRRGSPFAVGTM-PSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGF 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 71425875   245 AGFSRMRALCTkyNGmPQEASRPFDKdrgGFVMGEGSGIIVLEHLEHA 292
Cdd:pfam00109 210 AGFSAAGMLSP--DG-PCKAFDPFAD---GFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
207-461 2.87e-23

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: 99.33  E-value: 2.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    207 ACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCtkyngmPQEASRPFDKDRGGFVMGEGSGIIVL 286
Cdd:smart00825  96 ACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGEGVGVVVL 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    287 EHLEHAMQRGAQIFAELRGFGISSDAHD--LAAPHPEgrgAQLclrsaledggnisindvayvnahatgtigddmelhal 364
Cdd:smart00825 170 KRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGP---AQL------------------------------------- 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    365 dkvlggdgtssrrrpvYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHAPS-----AEGleRLQLVRGHAPL 439
Cdd:smart00825 210 ----------------LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNphidlEES--PLRVPTELTPW 271
                          250       260
                   ....*....|....*....|....*
gi 71425875    440 PFQGD---AVIStSFGFGGVNTALL 461
Cdd:smart00825 272 PPPGRprrAGVS-SFGFGGTNAHVI 295
 
Name Accession Description Interval E-value
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
23-465 0e+00

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 662.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   23 AVTPLGLDVASTWAALCQGRSATRPLKEVPFFFPACIDsdcrltpaaRQKSHEQLLAKMPCQVAAPVLAPSGGPN-FTPT 101
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIP---------EQKALENLVAAMPCQIAAEVDQSEFDPSdFAPT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  102 LRETRATLFAYYAAEEALTHAKLLespakrILASFAKERIGVNIGVGMPSLADVGDVSYSLYADpekvNYSRVNPLFVPK 181
Cdd:PTZ00050  72 KRESRATHFAMAAAREALADAKLD------ILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEK----GHSRVSPYFIPK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  182 ILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCTKYNGMP 261
Cdd:PTZ00050 142 ILGNMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNDDP 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  262 QEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEDGGNISI 341
Cdd:PTZ00050 222 QRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINI 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  342 NDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLH 420
Cdd:PTZ00050 302 NDVDYVNAHATSTpIGDKIELKAIKKVFGDSGA----PKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLE 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 71425875  421 APSAEGLerLQLVRGHAPLPFQG-DAVISTSFGFGGVNTALLFTRV 465
Cdd:PTZ00050 378 NPDAECD--LNLVQGKTAHPLQSiDAVLSTSFGFGGVNTALLFTKY 421
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
14-462 1.37e-166

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: 475.49  E-value: 1.37e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKevpfFFPAcidsdcrltpaarqksheqllAKMPCQVAAPVLAPS 93
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPIT----RFDA---------------------SGFPSRIAGEVPDFD 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  94 GGPNFTP--TLRETRATLFAYYAAEEALTHAKLLEspakrilASFAKERIGVNIGVGMPSLADVGDVSYSLYADPekvnY 171
Cdd:cd00834  56 PEDYLDRkeLRRMDRFAQFALAAAEEALADAGLDP-------EELDPERIGVVIGSGIGGLATIEEAYRALLEKG----P 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 172 SRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMR 251
Cdd:cd00834 125 RRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALR 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 252 ALCTKYNgMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRS 331
Cdd:cd00834 205 ALSTRND-DPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRA 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 332 ALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGtssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYH 410
Cdd:cd00834 284 ALADAG-LSPEDIDYINAHGTSTpLNDAAESKAIKRVFGEHA-----KKVPVSSTKSMTGHLLGAAGAVEAIATLLALRD 357
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 71425875 411 QQAPPNINLHAPSAEglERLQLVRgHAPLPFQGDAVISTSFGFGGVNTALLF 462
Cdd:cd00834 358 GVLPPTINLEEPDPE--CDLDYVP-NEAREAPIRYALSNSFGFGGHNASLVF 406
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
14-465 1.23e-164

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: 470.35  E-value: 1.23e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPlkeVPFFFPAcidsdcrltpaarqksheqllaKMPCQVAAPVlaps 93
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRP---ITRFDAS----------------------GLPVRIAGEV---- 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  94 ggPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESPakrilasFAKERIGVNIGVGMPSLADVGDVSYSLYAD 165
Cdd:COG0304  52 --KDFDPEEyldrkelrRMDRFTQYALAAAREALADAGLDLDE-------VDPDRTGVIIGSGIGGLDTLEEAYRALLEK 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 166 pekvNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIA 245
Cdd:COG0304 123 ----GPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLA 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 246 GFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGA 325
Cdd:COG0304 199 GFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGA 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 326 QLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTSsrrrpVYVSSVKGGLGHLLGAAGSVEAIVA 404
Cdd:COG0304 278 ARAMRAALKDAG-LSPEDIDYINAHGTSTpLGDAAETKAIKRVFGDHAYK-----VPVSSTKSMTGHLLGAAGAIEAIAS 351
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71425875 405 IMSLYHQQAPPNINLHAPSAEglERLQLVRGHApLPFQGDAVISTSFGFGGVNTALLFTRV 465
Cdd:COG0304 352 VLALRDGVIPPTINLENPDPE--CDLDYVPNEA-REAKIDYALSNSFGFGGHNASLVFKRY 409
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
14-462 4.32e-147

beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 274452 [Multi-domain]  Cd Length: 407  Bit Score: 425.75  E-value: 4.32e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpffFPAcidsdcrltpaarqksheqllAKMPCQVAAPVlaps 93
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITR----FDA---------------------SDLPVKIAGEV---- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    94 ggPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESPAKRilasfakERIGVNIGVGMPSLADVGDVSYSLYad 165
Cdd:TIGR03150  52 --KDFDPEDyidkkearRMDRFIQYALAAAKEAVEDSGLDIEEEDA-------ERVGVIIGSGIGGLETIEEQHIVLL-- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   166 pEKvNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIA 245
Cdd:TIGR03150 121 -EK-GPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIA 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   246 GFSRMRALCTkYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGA 325
Cdd:TIGR03150 199 GFAAMKALST-RNDDPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGA 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   326 QLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGgdgtsSRRRPVYVSSVKGGLGHLLGAAGSVEAIVA 404
Cdd:TIGR03150 278 ARAMRAALKDAG-INPEDVDYINAHGTSTpLGDKAETKAIKKVFG-----DHAYKLAVSSTKSMTGHLLGAAGAIEAIFT 351
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 71425875   405 IMSLYHQQAPPNINLHAPSAEGleRLQLVRgHAPLPFQGDAVISTSFGFGGVNTALLF 462
Cdd:TIGR03150 352 VLAIRDGIVPPTINLDNPDPEC--DLDYVP-NEAREAKIDYALSNSFGFGGTNASLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
13-466 2.79e-145

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 421.50  E-value: 2.79e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   13 RRRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpfFFPAcidsdcrltpaarqksheqllaKMPCQVAAPVlap 92
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITH---FDTS----------------------DLAVKIAGEV--- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   93 sggPNFTPTL----RETRA----TLFAYYAAEEALTHAKLLESPAKRilasfakERIGVNIGVGMPSLADVGDVSYSLYa 164
Cdd:PRK07314  53 ---KDFNPDDymsrKEARRmdrfIQYGIAAAKQAVEDAGLEITEENA-------DRIGVIIGSGIGGLETIEEQHITLL- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  165 dpEKvNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSI 244
Cdd:PRK07314 122 --EK-GPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGI 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  245 AGFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRG 324
Cdd:PRK07314 199 AGFAAARALSTR-NDDPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEG 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  325 AQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTSsrrrpVYVSSVKGGLGHLLGAAGSVEAIV 403
Cdd:PRK07314 278 AARAMKLALKDAG-INPEDIDYINAHGTSTpAGDKAETQAIKRVFGEHAYK-----VAVSSTKSMTGHLLGAAGAVEAIF 351
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71425875  404 AIMSLYHQQAPPNINLHAPSAEGleRLQLVrGHAPLPFQGDAVISTSFGFGGVNTALLFTRVE 466
Cdd:PRK07314 352 SVLAIRDQVIPPTINLDNPDEEC--DLDYV-PNEARERKIDYALSNSFGFGGTNASLVFKRYE 411
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
9-465 1.46e-140

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 410.34  E-value: 1.46e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    9 PPFIRRRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpfffpacidSDCRLtPAARQKSHEQLLAKMPCQVAAP 88
Cdd:PLN02836   1 PPLPTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQ----------DDLKM-KSEDEETQLYTLDQLPSRVAAL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   89 VLAPSGGPNFTPTL-----RETRATLFAYYAAEEALTHAKLLESPAKRilasfaKERIGVNIGVGMPSLADVGDVSySLY 163
Cdd:PLN02836  70 VPRGTGPGDFDEELwlnsrSSSRFIGYALCAADEALSDARWLPSEDEA------KERTGVSIGGGIGSITDILEAA-QLI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  164 ADPEKvnySRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVS 243
Cdd:PLN02836 143 CEKRL---RRLSPFFVPRILINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALS 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  244 IAGFSRMRALCTKYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGR 323
Cdd:PLN02836 220 IAGFSRSRALSTKFNSCPTEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGR 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  324 GAQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTSSRrrpVYVSSVKGGLGHLLGAAGSVEAI 402
Cdd:PLN02836 300 GAVLAMTRALQQSG-LHPNQVDYVNAHATSTpLGDAVEARAIKTVFSEHATSGG---LAFSSTKGATGHLLGAAGAVEAI 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71425875  403 VAIMSLYHQQAPPNINLHAPSAEGLERLQLVRGHAPLPFQgdAVISTSFGFGGVNTALLFTRV 465
Cdd:PLN02836 376 FSVLAIHHGIAPPTLNLERPDPIFDDGFVPLTASKAMLIR--AALSNSFGFGGTNASLLFTSP 436
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
13-464 7.00e-133

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 390.13  E-value: 7.00e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   13 RRRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpffFPAcidsdcrltpaarqkshEQLLAKMPCQVaaPVLAP 92
Cdd:PRK06333   3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTD----FPV-----------------GDLATKIGGQV--PDLAE 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   93 SGGPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESPAKrilasfAKERIGVNIGVGM---PSLADVGDVSys 161
Cdd:PRK06333  60 DAEAGFDPDRyldpkdqrKMDRFILFAMAAAKEALAQAGWDPDTLE------DRERTATIIGSGVggfPAIAEAVRTL-- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  162 lyadpEKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITP 241
Cdd:PRK06333 132 -----DSRGPRRLSPFTIPSFLTNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDR 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  242 VSIAGFSRMRALCTKYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPE 321
Cdd:PRK06333 207 VSLAGFAAARALSTRFNDAPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPED 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  322 GRGAQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrrpVYVSSVKGGLGHLLGAAGSVE 400
Cdd:PRK06333 287 GEGARRAMLIALRQAG-IPPEEVQHLNAHATSTpVGDLGEVAAIKKVFGHVSG------LAVSSTKSATGHLLGAAGGVE 359
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71425875  401 AIVAIMSLYHQQAPPNINLHAPSAEGlERLQLVRGHApLPFQGDAVISTSFGFGGVNTALLFTR 464
Cdd:PRK06333 360 AIFTILALRDQIAPPTLNLENPDPAA-EGLDVVANKA-RPMDMDYALSNGFGFGGVNASILFRR 421
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
14-465 9.15e-94

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 289.71  E-value: 9.15e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSAtrpLKEVPFFFPAcidsdcrltpaarqksheqllaKMPCQVAAPVlaps 93
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECG---IKKITLFDAS----------------------DFPVQIAGEI---- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   94 ggPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESpakrilaSFAKERIGVNIGVGMPSLADVGDVSYSLyad 165
Cdd:PRK08439  53 --TDFDPTEvmdpkevkKADRFIQLGLKAAREAMKDAGFLPE-------ELDAERFGVSSASGIGGLPNIEKNSIIC--- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  166 pEKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIA 245
Cdd:PRK08439 121 -FEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIG 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  246 GFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEgrGA 325
Cdd:PRK08439 200 GFAAMKALSTR-NDDPKKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GP 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  326 QLCLRSALEDGGNISINdvaYVNAHATGT-IGDDMELHALDKVLGGDGTSSRrrpvyVSSVKGGLGHLLGAAGSVEAIVA 404
Cdd:PRK08439 277 LRAMKAALEMAGNPKID---YINAHGTSTpYNDKNETAALKELFGSKEKVPP-----VSSTKGQIGHCLGAAGAIEAVIS 348
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71425875  405 IMSLYHQQAPPNINLHAPSAE-GLERLQLVRGHAPLpfqgDAVISTSFGFGGVNTALLFTRV 465
Cdd:PRK08439 349 IMAMRDGILPPTINQETPDPEcDLDYIPNVARKAEL----NVVMSNSFGFGGTNGVVIFKKV 406
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
9-462 3.74e-87

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 276.86  E-value: 3.74e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    9 PPFIRRRVVVTGLGAVTPLGLDVASTWAALCQGRSAtrpLKEVPFFfpacidsDCrltpaarqksheqllAKMPCQVAAP 88
Cdd:PLN02787 124 PLTKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSG---ISEIERF-------DC---------------SQFPTRIAGE 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   89 VLAPSGGPNFTPTL--RETRATLFAYYAAEEALTHAKLLESpakrILASFAKERIGVNIGVGMPSLADVGDVSYSLyadp 166
Cdd:PLN02787 179 IKSFSTDGWVAPKLskRMDKFMLYLLTAGKKALADGGITED----VMKELDKTKCGVLIGSAMGGMKVFNDAIEAL---- 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  167 eKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAG 246
Cdd:PLN02787 251 -RISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGG 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  247 FSRMRALcTKYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQ 326
Cdd:PLN02787 330 FVACRAL-SQRNDDPTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVI 408
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  327 LCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrrpVYVSSVKGGLGHLLGAAGSVEAIVAI 405
Cdd:PLN02787 409 LCIEKALAQSG-VSKEDVNYINAHATSTkAGDLKEYQALMRCFGQNPE------LRVNSTKSMIGHLLGAAGAVEAIATV 481
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 71425875  406 MSLYHQQAPPNINLHAPsaEGLERLQLVRGHAPLPFQGDAVISTSFGFGGVNTALLF 462
Cdd:PLN02787 482 QAIRTGWVHPNINLENP--ESGVDTKVLVGPKKERLDIKVALSNSFGFGGHNSSILF 536
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
13-465 2.87e-85

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 268.02  E-value: 2.87e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   13 RRRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpffFPACIDSdCRLTPAARQKSHEQLLAKMPCQvaapvlap 92
Cdd:PRK08722   3 KRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEH----FDTTNFS-TRFAGLVKDFNCEEYMSKKDAR-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   93 sggpnftptlretRATLFAYYAAEEALthaKLLESPAKRILASFAkERIGVNIGVGMPSLADVGDVSYSLYADPEKvnys 172
Cdd:PRK08722  70 -------------KMDLFIQYGIAAGI---QALDDSGLEVTEENA-HRIGVAIGSGIGGLGLIEAGHQALVEKGPR---- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  173 RVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRA 252
Cdd:PRK08722 129 KVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKA 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  253 LCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSA 332
Cdd:PRK08722 209 LSTR-NDEPQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAA 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  333 LEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQ 411
Cdd:PRK08722 288 MRDAG-VTGEQIGYVNAHGTSTpAGDVAEIKGIKRALGEAGS----KQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQ 362
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71425875  412 QAPPNINLHAPSaEGLErLQLVRGHAPLPFQGDAVISTSFGFGGVNTALLFTRV 465
Cdd:PRK08722 363 IVPPTINLDDPE-EGLD-IDLVPHTARKVESMEYAICNSFGFGGTNGSLIFKKM 414
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
16-464 1.43e-75

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 243.10  E-value: 1.43e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   16 VVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvPFF----FPACI------DSDCRLTPAA-RQKSHEQllaKMPCQ 84
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDD-PFVeefdLPVRIgghlleEFDHQLTRVElRRMSYLQ---RMSTV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   85 VAAPVLAPSGGPNFTPtlretratlfayyaaeealthakllespakrilasfakERIGVNIGVGMPSLADVGDVsyslYA 164
Cdd:PRK07910  90 LGRRVWENAGSPEVDT--------------------------------------NRLMVSIGTGLGSAEELVFA----YD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  165 DPEKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSI 244
Cdd:PRK07910 128 DMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPI 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  245 AGFSRMRALCTKYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRG 324
Cdd:PRK07910 208 AGFAQMRIVMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGER 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  325 AQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDgtssrRRPVYVSsvKGGLGHLLGAAGSVEAIV 403
Cdd:PRK07910 288 AGHAMTRAIELAG-LTPGDIDHVNAHATGTsVGDVAEGKAINNALGGH-----RPAVYAP--KSALGHSVGAVGAVESIL 359
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71425875  404 AIMSLYHQQAPPNINLHAPSAEglERLQLVRGHaPLPFQGDAVISTSFGFGGVNTALLFTR 464
Cdd:PRK07910 360 TVLALRDGVIPPTLNLENLDPE--IDLDVVAGE-PRPGNYRYAINNSFGFGGHNVALAFGR 417
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
14-467 2.48e-74

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 239.19  E-value: 2.48e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRplkevpfffpacidsdcrltpaarqKSHEQLLAKMPCQVA-APVLAP 92
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGIT-------------------------FSPEFAEMGMRSQVWgNVKLDP 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   93 SGGPNFTPTLRETRATLFAYYAAEEALTHAKLLESpakrilaSFAKERIGVNIGVGMPS---LADVGDVSYslyadpEKV 169
Cdd:PRK07967  57 TGLIDRKVMRFMGDASAYAYLAMEQAIADAGLSEE-------QVSNPRTGLIAGSGGGStrnQVEAADAMR------GPR 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  170 NYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAgFSR 249
Cdd:PRK07967 124 GPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDA 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  250 MRALCTKYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAphPEGRGAQLCL 329
Cdd:PRK07967 203 MGALSTKYNDTPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCM 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  330 RSALEDGGnisiNDVAYVNAHATGT-IGDDMELHALDKVLgGDGTSSrrrpvyVSSVKGGLGHLLGAAGSVEAIVAIMSL 408
Cdd:PRK07967 281 QMALATVD----TPIDYINTHGTSTpVGDVKELGAIREVF-GDKSPA------ISATKSLTGHSLGAAGVQEAIYSLLMM 349
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71425875  409 YHQQAPPNINLHA--PSAEGLERLQLVRGHAPLpfqgDAVISTSFGFGGVNTALLFTRVEK 467
Cdd:PRK07967 350 EHGFIAPSANIEEldPQAAGMPIVTETTDNAEL----TTVMSNSFGFGGTNATLVFRRYKG 406
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
118-464 9.76e-74

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 235.78  E-value: 9.76e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  118 ALTHAKLLESPAKrilasfAKERIGVNIGvGMPSLADVgdVSYSLYADPEkvnysRVNPLFVPKILGNMVTGLTAMKYGI 197
Cdd:PRK14691  15 SLTHADNTEKQER------TATIIGAGIG-GFPAIAHA--VRTSDSRGPK-----RLSPFTVPSFLVNLAAGHVSIKHHF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  198 MGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCTKYNGMPQEASRPFDKDRGGFVM 277
Cdd:PRK14691  81 KGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHFNSTPEKASRPFDTARDGFVM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  278 GEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEDGGnISINDVAYVNAHATGT-IG 356
Cdd:PRK14691 161 GEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAG-ITPEQVQHLNAHATSTpVG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  357 DDMELHALDKVLGgdgtssRRRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHA--PSAEGlerLQLVR 434
Cdd:PRK14691 240 DLGEINAIKHLFG------ESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENpdPAAKG---LNIIA 310
                        330       340       350
                 ....*....|....*....|....*....|
gi 71425875  435 GHAPlPFQGDAVISTSFGFGGVNTALLFTR 464
Cdd:PRK14691 311 GNAQ-PHDMTYALSNGFGFAGVNASILLKR 339
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
11-468 1.08e-67

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 222.58  E-value: 1.08e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   11 FIRRRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpffFPAcidsdcrltpaarqkshEQLLAKMpcqvaapvl 90
Cdd:PRK06501   8 LGRPIVAVTGMGVVTSLGQGKADNWAALTAGESGIHTITR----FPT-----------------EGLRTRI--------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   91 apSGGPNFTPTLRETRATL---FAYYAAEEALTHAKL-----------------LESPAKRILAsfakERIGVNIGVGmp 150
Cdd:PRK06501  58 --AGTVDFLPESPFGASALseaLARLAAEEALAQAGIgkgdfpgplflaappveLEWPARFALA----AAVGDNDAPS-- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  151 sladvgdvsyslYADPEKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMG-PVGSSvAACATGAHCIGEAAEWIRGGRADI 229
Cdd:PRK06501 130 ------------YDRLLRAARGGRFDALHERFQFGSIADRLADRFGTRGlPISLS-TACASGATAIQLGVEAIRRGETDR 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  230 VVCGGTEACITPVSIAGFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGIS 309
Cdd:PRK06501 197 ALCIATDGSVSAEALIRFSLLSALSTQ-NDPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEK 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  310 SDAHDLAAPHPEGRGAQLCLRSALEDGGnISINDVAYVNAHATGTIGDD-MELHALDKVLGgdgtsSRRRPVYVSSVKGG 388
Cdd:PRK06501 276 ADSFHRTRSSPDGSPAIGAIRAALADAG-LTPEQIDYINAHGTSTPENDkMEYLGLSAVFG-----ERLASIPVSSNKSM 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  389 LGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHAPSAEGLerLQLVRGHAPlPFQGDAVISTSFGFGGVNTALLFTRvEKA 468
Cdd:PRK06501 350 IGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIP--LDVVPNVAR-DARVTAVLSNSFGFGGQNASLVLTA-EPA 425
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
14-461 2.54e-67

"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: 221.16  E-value: 2.54e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  14 RRVVVTGLGAVTPLG---LDVASTWAALCQGRSATRPLKEVPFFFPAcidsdcrltPAARQKSHEQLLAKMPCQvaapvl 90
Cdd:cd00828   1 SRVVITGIGVVSPHGegcDEVEEFWEALREGRSGIAPVARLKSRFDR---------GVAGQIPTGDIPGWDAKR------ 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  91 apsggpnftpTLRETRATLFAYYAAEEALTHAKLleSPAKRILASfakeRIGVNIGVGMPSLADVGDVSYSLYadpekvn 170
Cdd:cd00828  66 ----------TGIVDRTTLLALVATEEALADAGI--TDPYEVHPS----EVGVVVGSGMGGLRFLRRGGKLDA------- 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 171 ySRVNPLFVPK--ILGNMVTGLTAMKYGIM-GPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEAcITPVSIAGF 247
Cdd:cd00828 123 -RAVNPYVSPKwmLSPNTVAGWVNILLLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGF 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 248 SRMRALCTKYNGmPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPeGRGAQL 327
Cdd:cd00828 201 ANMGALSTAEEE-PEEMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIAR 278
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 328 CLRSALeDGGNISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGtssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIM 406
Cdd:cd00828 279 AIRTAL-AKAGLSLDDLDVISAHGTSTpANDVAESRAIAEVAGALG-----APLPVTAQKALFGHSKGAAGALQLIGALQ 352
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71425875 407 SLYHQQAPPNINLHAPsAEGLERLQLVRGHAPLPFQGDAVISTSFGFGGVNTALL 461
Cdd:cd00828 353 SLEHGLIPPTANLDDV-DPDVEHLSVVGLSRDLNLKVRAALVNAFGFGGSNAALV 406
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
14-462 6.14e-66

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 217.55  E-value: 6.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEVPFFfpacidsdcrltpaarqkshEQLLAKMpcqvAAPVlaps 93
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRY--------------------DGLNTRL----AAPI---- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   94 ggPNFTP----TLRETRA----TLFAYYAAEEALTHAKLLESPakrilaSFAKERIGVNIGVGMPSLADVGDVsyslyad 165
Cdd:PRK09116  54 --DDFELpahyTRKKIRSmgrvSLMATRASELALEDAGLLGDP------ILTDGRMGIAYGSSTGSTDPIGAF------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  166 pekvnysrvnplfvpkilGNMVT-----GLTAMKY----------------GIMGPVGSSVAACATGAHCIGEAAEWIRG 224
Cdd:PRK09116 119 ------------------GTMLLegsmsGITATTYvrmmphttavnvglffGLKGRVIPTSSACTSGSQGIGYAYEAIKY 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  225 GRADIVVCGGTEAcITPVSIAGFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELR 304
Cdd:PRK09116 181 GYQTVMLAGGAEE-LCPTEAAVFDTLFATSTR-NDAPELTPRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIV 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  305 GFGISSDAHDLAAPHPEgrGAQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGgdgtssRRRPvyVS 383
Cdd:PRK09116 259 GFGTNSDGAHVTQPQAE--TMQIAMELALKDAG-LAPEDIGYVNAHGTATdRGDIAESQATAAVFG------ARMP--IS 327
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71425875  384 SVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHAPSAEgLERLQLVRGhAPLPFQGDAVISTSFGFGGVNTALLF 462
Cdd:PRK09116 328 SLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPA-CGALDYIMG-EAREIDTEYVMSNNFAFGGINTSLIF 404
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
15-460 2.47e-65

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 215.30  E-value: 2.47e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   15 RVVVTGLGAVTPLGlDVASTWAALCQGRSATRPLKEVPFFFPacidsdcrlTPAArqksheqLLAKMPCQVaapvlapsg 94
Cdd:PRK05952   3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQPFPELPP---------LPLG-------LIGNQPSSL--------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   95 gpnftPTLRETratlfayyAAEEALTHAKLleSPAkriLASfakerIGVNIGVGMPSLADVGDVSYSLYADPEKVNYSRV 174
Cdd:PRK05952  57 -----EDLTKT--------VVTAALKDAGL--TPP---LTD-----CGVVIGSSRGCQGQWEKLARQMYQGDDSPDEELD 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  175 NPLFVpKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALC 254
Cdd:PRK05952 114 LENWL-DTLPHQAAIAAARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  255 tkyngmpQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALE 334
Cdd:PRK05952 193 -------KTGAYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLA 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  335 DGGnISINDVAYVNAHATGTIGDDMELHALDKVLGGDGtssrrrpVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAP 414
Cdd:PRK05952 266 RSG-LTPEDIDYIHAHGTATRLNDQREANLIQALFPHR-------VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLP 337
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 71425875  415 PNINLHAPSAEglerLQLVRghAPLPFQGDAVISTSFGFGGVNTAL 460
Cdd:PRK05952 338 PCVGLQEPEFD----LNFVR--QAQQSPLQNVLCLSFGFGGQNAAI 377
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
15-461 5.56e-54

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: 186.22  E-value: 5.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  15 RVVVTGLGAVTPLGLDVASTWAALCQGRSATRplkEVPFffpacidsdcRLTPAARQKSHEQLLAKMPCQVAAPVLAPSG 94
Cdd:cd00833   2 PIAIVGMACRFPGAADPDEFWENLLEGRDAIS---EIPE----------DRWDADGYYPDPGKPGKTYTRRGGFLDDVDA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  95 GPN--FTPTLRETRAT-----LF---AYyaaeEALTHAKLlespakrILASFAKERIGVNIGVgmpsladvgdvSYSLYA 164
Cdd:cd00833  69 FDAafFGISPREAEAMdpqqrLLlevAW----EALEDAGY-------SPESLAGSRTGVFVGA-----------SSSDYL 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 165 DPEKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPvgsSV---AACATGAHCIGEAAEWIRGGRADIVVCGGTEACITP 241
Cdd:cd00833 127 ELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGP---SLtvdTACSSSLVALHLACQSLRSGECDLALVGGVNLILSP 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 242 VSIAGFSRMRALCtkyngmPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPE 321
Cdd:cd00833 204 DMFVGFSKAGMLS------PDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPS 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 322 GRGAQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDgtSSRRRPVYVSSVKGGLGHLLGAAGSVE 400
Cdd:cd00833 278 GEAQAALIRRAYARAG-VDPSDIDYVEAHGTGTpLGDPIEVEALAKVFGGS--RSADQPLLIGSVKSNIGHLEAAAGLAG 354
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71425875 401 AIVAIMSLYHQQAPPNINLHAPSAE-GLERLQLVRGHAPLPFQGD-----AVIStSFGFGGVNTALL 461
Cdd:cd00833 355 LIKVVLALEHGVIPPNLHFETPNPKiDFEESPLRVPTEARPWPAPagprrAGVS-SFGFGGTNAHVI 420
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
15-464 7.30e-53

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 183.31  E-value: 7.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   15 RVVVTGLGAVTPLGLDVASTWAALCQGRSATRplkevpfffpacidsdcRLTPAARQKSHEQLLAKMPCQVAAPVLAPSG 94
Cdd:PRK07103   3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFG-----------------VMRRPGRQVPDDAGAGLASAFIGAELDSLAL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   95 GPNFTPTLR-----ETRATLFAyyaAEEALTHAKLLESPakrilasfaKERIGVNIG---VGMPSLADVgdvsYSLYADp 166
Cdd:PRK07103  66 PERLDAKLLrraslSAQAALAA---AREAWRDAALGPVD---------PDRIGLVVGgsnLQQREQALV----HETYRD- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  167 ekvnysrvNPLFVPK--ILGNMVT---GLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITP 241
Cdd:PRK07103 129 --------RPAFLRPsyGLSFMDTdlvGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSY 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  242 VSIAGFSRMRALCT-KYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHP 320
Cdd:PRK07103 201 WECQALRSLGAMGSdRFADEPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSL 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  321 EGRGAqlCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDkvlggdgtSSRRRPVYVSSVKGGLGHLLGAAGSV 399
Cdd:PRK07103 281 EGEMR--VIRAALRRAG-LGPEDIDYVNPHGTGSpLGDETELAALF--------ASGLAHAWINATKSLTGHGLSAAGIV 349
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71425875  400 EAIVAIMSLYHQQAPPNINLHAPSAeglERLQLVRGHaPLPFQGDAVISTSFGFGGVNTALLFTR 464
Cdd:PRK07103 350 ELIATLLQMRAGFLHPSRNLDEPID---ERFRWVGST-AESARIRYALSLSFGFGGINTALVLER 410
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
16-464 1.17e-47

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 168.87  E-value: 1.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   16 VVVTGLGAVTPLGLDVASTWAALCQGRSA-----TRPLKEVPFFFPACIDSDCRLTPAArqksheqlLAKMPCqvaapvl 90
Cdd:PRK09185   4 VYISAFGATSALGRGLDAILAALRAGRASgmrpcDFWLVDLPTWVGEVVGVELPALPAA--------LAAFDC------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   91 apsggpnftptlRETRATLFAYYAAEEALTHAKllespakrilASFAKERIGVNIGVGMPSLADvGDVSYSLY-----AD 165
Cdd:PRK09185  69 ------------RNNRLALLALQQIEPAVEAAI----------ARYGADRIGVVLGTSTSGILE-GELAYRRRdpahgAL 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  166 PEKVNYSRVNPLFVPKILGNmVTGLTAMKYGImgpvgSSvaACATGAHCIGEAAEWIRGGRADIVVCGGTEA-CITPVSi 244
Cdd:PRK09185 126 PADYHYAQQELGSLADFLRA-YLGLSGPAYTI-----ST--ACSSSAKVFASARRLLEAGLCDAAIVGGVDSlCRLTLN- 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  245 aGFSRMRALCTkyngmpqEASRPFDKDRGGFVMGEGSGIIVLEhlehamqRGAQIFAELRGFGISSDAHDLAAPHPEGRG 324
Cdd:PRK09185 197 -GFNSLESLSP-------QPCRPFSANRDGINIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLG 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  325 AQLCLRSALEDGGnISINDVAYVNAHATGTIGDD-MELHALDKVLGGDgtssrrrpVYVSSVKGGLGHLLGAAGSVEAIV 403
Cdd:PRK09185 262 AILAMQQALADAG-LAPADIGYINLHGTATPLNDaMESRAVAAVFGDG--------VPCSSTKGLTGHTLGAAGAVEAAI 332
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71425875  404 AIMSLYHQQAPPNINLHAPSAEgLERLQLVRGHAPLPFQgdAVISTSFGFGGVNTALLFTR 464
Cdd:PRK09185 333 CWLALRHGLPPHGWNTGQPDPA-LPPLYLVENAQALAIR--YVLSNSFAFGGNNCSLIFGR 390
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
105-461 5.37e-44

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: 157.41  E-value: 5.37e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 105 TRATLFAYYAAEEALTHAKLLESPAKrilasfaKERIGVNIGVGMPSladvgdvsySLYADPEKVNYSRVNPLFVPKILG 184
Cdd:cd00825   9 SYVSILGFEAAERAIADAGLSREYQK-------NPIVGVVVGTGGGS---------PRFQVFGADAMRAVGPYVVTKAMF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 185 NMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALctkyngMPQEA 264
Cdd:cd00825  73 PGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALS------TPEKA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 265 SRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEdGGNISINDV 344
Cdd:cd00825 147 SRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALA-VAGLTVWDI 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 345 AYVNAHATGT-IGDDMELHALDKVLGGdgtssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLhaps 423
Cdd:cd00825 226 DYLVAHGTGTpIGDVKELKLLRSEFGD-------KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHI---- 294
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 71425875 424 aEGLERLQLVRGHAPLPFQGDAVISTSFGFGGVNTALL 461
Cdd:cd00825 295 -EELDEAGLNIVTETTPRELRTALLNGFGLGGTNATLV 331
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
134-457 6.38e-42

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 159.65  E-value: 6.38e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  134 ASFAKERIGVNIGVGMpsladvGDVSYSLYADPEKVNysrvnPLFVPKILGNMVTGLTAMKYGIMGPvgsSVA---ACAT 210
Cdd:COG3321  111 ESLAGSRTGVFVGASS------NDYALLLLADPEAID-----AYALTGNAKSVLAGRISYKLDLRGP---SVTvdtACSS 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  211 GAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCtkyngmPQEASRPFDKDRGGFVMGEGSGIIVLEHLE 290
Cdd:COG3321  177 SLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS------PDGRCRAFDADADGYVRGEGVGVVVLKRLS 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  291 HAMQRGAQIFAELRGFGISSDAHD--LAAPHPEGRgaQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKV 367
Cdd:COG3321  251 DALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQ--AAVIRRALADAG-VDPATVDYVEAHGTGTpLGDPIEAAALTAA 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  368 LGGDGtsSRRRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHAPS-----AEGleRLQLVRGHAPLPFQ 442
Cdd:COG3321  328 FGQGR--PADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNphidfENS--PFYVNTELRPWPAG 403
                        330
                 ....*....|....*...
gi 71425875  443 GD---AVIStSFGFGGVN 457
Cdd:COG3321  404 GGprrAGVS-SFGFGGTN 420
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
14-292 4.26e-40

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: 144.70  E-value: 4.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKevpfffpacidsDCRLTPAARQKSHEQLLAKMPCQVAAPVlaps 93
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIP------------ADRWDPDKLYDPPSRIAGKIYTKWGGLD---- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    94 GGPNFTPTL-----RETRAT----LFAYYAAEEALTHAKLLEspakrilASFAKERIGVNIGVGMPSLADvgdvsysLYA 164
Cdd:pfam00109  65 DIFDFDPLFfgispREAERMdpqqRLLLEAAWEALEDAGITP-------DSLDGSRTGVFIGSGIGDYAA-------LLL 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   165 DPEKVNYSRVNPLFVPKIlGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSI 244
Cdd:pfam00109 131 LDEDGGPRRGSPFAVGTM-PSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGF 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 71425875   245 AGFSRMRALCTkyNGmPQEASRPFDKdrgGFVMGEGSGIIVLEHLEHA 292
Cdd:pfam00109 210 AGFSAAGMLSP--DG-PCKAFDPFAD---GFVRGEGVGAVVLKRLSDA 251
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
300-420 4.92e-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: 123.83  E-value: 4.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875   300 FAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGtssRRR 378
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAG-VDPEDVDYVEAHGTGTpLGDPIEAEALKRVFGSGA---RKQ 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 71425875   379 PVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLH 420
Cdd:pfam02801  77 PLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
107-457 7.43e-31

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: 127.04  E-value: 7.43e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    107 ATLFAYYAAEEALTHAKLLESpakrilasFAKERIGVNIGVG--------------MPSLADVGDVSYSLYADPE----- 167
Cdd:TIGR02813   93 SQLLSLVVAKEVLNDAGLPDG--------YDRDKIGITLGVGggqkqssslnarlqYPVLKKVFKASGVEDEDSEmlikk 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    168 -KVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAG 246
Cdd:TIGR02813  165 fQDQYIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMS 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    247 FSRMRALCTkyngmpQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAH--DLAAPHPEGRG 324
Cdd:TIGR02813  245 FSKTPAFTT------NEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQA 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    325 AqlCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDgtSSRRRPVYVSSVKGGLGHLLGAAGSVEAIV 403
Cdd:TIGR02813  319 K--ALKRAYDDAG-FAPHTCGLIEAHGTGTaAGDVAEFGGLVSVFSQD--NDQKQHIALGSVKSQIGHTKSTAGTAGMIK 393
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71425875    404 AIMSLYHQQAPPNINLHAPSAE-GLERLQLVRGHAPLPFQG-------DAVIStSFGFGGVN 457
Cdd:TIGR02813  394 AVLALHHKVLPPTINVDQPNPKlDIENSPFYLNTETRPWMQredgtprRAGIS-SFGFGGTN 454
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
14-461 8.22e-27

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: 111.68  E-value: 8.22e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKevpfffpacidsdcRLTPAARqksheqllakmPCQVAAPVlaps 93
Cdd:cd00832   1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPIT--------------RFDPSGY-----------PARLAGEV---- 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875  94 ggPNFTPT-------LRET-RATLFAYYAAEEALTHAKLleSPAKriLASFakerigvniGVGMPSLADVGDVSYS---- 161
Cdd:cd00832  52 --PDFDAAehlpgrlLPQTdRMTRLALAAADWALADAGV--DPAA--LPPY---------DMGVVTASAAGGFEFGqrel 116
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 162 --LYAD-PEKVN-------YSRVNplfvpkilgnmvTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGrADIVV 231
Cdd:cd00832 117 qkLWSKgPRHVSayqsfawFYAVN------------TGQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRG-TPLVV 183
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 232 CGGTEACITPVSIAGFSRMRALCTkyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSD 311
Cdd:cd00832 184 SGGVDSALCPWGWVAQLSSGRLST--SDDPARAYLPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFD 261
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 312 ahdlAAPHPeGRGAQL--CLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGgdgtssrRRPVYVSSVKGG 388
Cdd:cd00832 262 ----PPPGS-GRPPGLarAIRLALADAG-LTPEDVDVVFADAAGVpELDRAEAAALAAVFG-------PRGVPVTAPKTM 328
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71425875 389 LGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHAPSAEglERLQLVRGhAPLPFQGDAVISTSFGFGGVNTALL 461
Cdd:cd00832 329 TGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPA--YGLDLVTG-RPRPAALRTALVLARGRGGFNSALV 398
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
187-461 4.06e-24

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: 100.98  E-value: 4.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 187 VTGLTAMKYGIM-GPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITpvsiagfsrmralctkyngmpqeas 265
Cdd:cd00327  46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEFVF------------------------- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 266 rpfdkdrggfvmGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDlAAPHPEGRGAQLCLRSALEdGGNISINDVA 345
Cdd:cd00327 101 ------------GDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGAS-MVPAVSGEGLARAARKALE-GAGLTPSDID 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875 346 YVNAHATGT-IGDDMELHALDKVLGGdgtssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHqqappninlhapsa 424
Cdd:cd00327 167 YVEAHGTGTpIGDAVELALGLDPDGV-------RSPAVSATLIMTGHPLGAAGLAILDELLLMLEH-------------- 225
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71425875 425 eglerlqlvRGHAPLPFQGDAVISTSFGFGGVNTALL 461
Cdd:cd00327 226 ---------EFIPPTPREPRTVLLLGFGLGGTNAAVV 253
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
207-461 2.87e-23

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: 99.33  E-value: 2.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    207 ACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCtkyngmPQEASRPFDKDRGGFVMGEGSGIIVL 286
Cdd:smart00825  96 ACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGEGVGVVVL 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    287 EHLEHAMQRGAQIFAELRGFGISSDAHD--LAAPHPEgrgAQLclrsaledggnisindvayvnahatgtigddmelhal 364
Cdd:smart00825 170 KRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGP---AQL------------------------------------- 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71425875    365 dkvlggdgtssrrrpvYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHAPS-----AEGleRLQLVRGHAPL 439
Cdd:smart00825 210 ----------------LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNphidlEES--PLRVPTELTPW 271
                          250       260
                   ....*....|....*....|....*
gi 71425875    440 PFQGD---AVIStSFGFGGVNTALL 461
Cdd:smart00825 272 PPPGRprrAGVS-SFGFGGTNAHVI 295
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
271-303 4.06e-03

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 39.55  E-value: 4.06e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 71425875  271 DRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAEL 303
Cdd:PRK06519 235 DGGGFILGSGGAFLVLESREHAEARGARPYARI 267
 
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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