|
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 1393601517 23 AVTPLGLDVASTWAALCQGRSATRPLKEVPFFFPACIDsdcrltpaaRQKSHEQLLAKMPCQVAAPVLAPSGGPN-FTPT 101
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIP---------EQKALENLVAAMPCQIAAEVDQSEFDPSdFAPT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 102 LRETRATLFAYYAAEEALTHAKLLespakrILASFAKERIGVNIGVGMPSLADVGDVSYSLYADpekvNYSRVNPLFVPK 181
Cdd:PTZ00050 72 KRESRATHFAMAAAREALADAKLD------ILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEK----GHSRVSPYFIPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 182 ILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCTKYNGMP 261
Cdd:PTZ00050 142 ILGNMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNDDP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 262 QEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEDGGNISI 341
Cdd:PTZ00050 222 QRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 342 NDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLH 420
Cdd:PTZ00050 302 NDVDYVNAHATSTpIGDKIELKAIKKVFGDSGA----PKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLE 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKevpfFFPAcidsdcrltpaarqksheqllAKMPCQVAAPVLAPS 93
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPIT----RFDA---------------------SGFPSRIAGEVPDFD 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 GGPNFTP--TLRETRATLFAYYAAEEALTHAKLLEspakrilASFAKERIGVNIGVGMPSLADVGDVSYSLYADPekvnY 171
Cdd:cd00834 56 PEDYLDRkeLRRMDRFAQFALAAAEEALADAGLDP-------EELDPERIGVVIGSGIGGLATIEEAYRALLEKG----P 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 172 SRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMR 251
Cdd:cd00834 125 RRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 252 ALCTKYNgMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRS 331
Cdd:cd00834 205 ALSTRND-DPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 332 ALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGtssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYH 410
Cdd:cd00834 284 ALADAG-LSPEDIDYINAHGTSTpLNDAAESKAIKRVFGEHA-----KKVPVSSTKSMTGHLLGAAGAVEAIATLLALRD 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPlkeVPFFFPAcidsdcrltpaarqksheqllaKMPCQVAAPVlaps 93
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRP---ITRFDAS----------------------GLPVRIAGEV---- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 ggPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESPakrilasFAKERIGVNIGVGMPSLADVGDVSYSLYAD 165
Cdd:COG0304 52 --KDFDPEEyldrkelrRMDRFTQYALAAAREALADAGLDLDE-------VDPDRTGVIIGSGIGGLDTLEEAYRALLEK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 166 pekvNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIA 245
Cdd:COG0304 123 ----GPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 246 GFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGA 325
Cdd:COG0304 199 GFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 326 QLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTSsrrrpVYVSSVKGGLGHLLGAAGSVEAIVA 404
Cdd:COG0304 278 ARAMRAALKDAG-LSPEDIDYINAHGTSTpLGDAAETKAIKRVFGDHAYK-----VPVSSTKSMTGHLLGAAGAIEAIAS 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpffFPAcidsdcrltpaarqksheqllAKMPCQVAAPVlaps 93
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITR----FDA---------------------SDLPVKIAGEV---- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 ggPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESPAKRilasfakERIGVNIGVGMPSLADVGDVSYSLYad 165
Cdd:TIGR03150 52 --KDFDPEDyidkkearRMDRFIQYALAAAKEAVEDSGLDIEEEDA-------ERVGVIIGSGIGGLETIEEQHIVLL-- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 166 pEKvNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIA 245
Cdd:TIGR03150 121 -EK-GPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 246 GFSRMRALCTkYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGA 325
Cdd:TIGR03150 199 GFAAMKALST-RNDDPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 326 QLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGgdgtsSRRRPVYVSSVKGGLGHLLGAAGSVEAIVA 404
Cdd:TIGR03150 278 ARAMRAALKDAG-INPEDVDYINAHGTSTpLGDKAETKAIKKVFG-----DHAYKLAVSSTKSMTGHLLGAAGAIEAIFT 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKevpfffpacidsDCRLTPAARQKSHEQLLAKMPCQVAAPVlaps 93
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIP------------ADRWDPDKLYDPPSRIAGKIYTKWGGLD---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 GGPNFTPTL-----RETRAT----LFAYYAAEEALTHAKLLEspakrilASFAKERIGVNIGVGMPSLADvgdvsysLYA 164
Cdd:pfam00109 65 DIFDFDPLFfgispREAERMdpqqRLLLEAAWEALEDAGITP-------DSLDGSRTGVFIGSGIGDYAA-------LLL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 165 DPEKVNYSRVNPLFVPKIlGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSI 244
Cdd:pfam00109 131 LDEDGGPRRGSPFAVGTM-PSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGF 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1393601517 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 1393601517 207 ACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCtkyngmPQEASRPFDKDRGGFVMGEGSGIIVL 286
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGEGVGVVVL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 287 EHLEHAMQRGAQIFAELRGFGISSDAHD--LAAPHPEgrgAQLclrsaledggnisindvayvnahatgtigddmelhal 364
Cdd:smart00825 170 KRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGP---AQL------------------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 365 dkvlggdgtssrrrpvYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHAPS-----AEGleRLQLVRGHAPL 439
Cdd:smart00825 210 ----------------LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNphidlEES--PLRVPTELTPW 271
|
250 260
....*....|....*....|....*
gi 1393601517 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 1393601517 23 AVTPLGLDVASTWAALCQGRSATRPLKEVPFFFPACIDsdcrltpaaRQKSHEQLLAKMPCQVAAPVLAPSGGPN-FTPT 101
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIP---------EQKALENLVAAMPCQIAAEVDQSEFDPSdFAPT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 102 LRETRATLFAYYAAEEALTHAKLLespakrILASFAKERIGVNIGVGMPSLADVGDVSYSLYADpekvNYSRVNPLFVPK 181
Cdd:PTZ00050 72 KRESRATHFAMAAAREALADAKLD------ILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEK----GHSRVSPYFIPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 182 ILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCTKYNGMP 261
Cdd:PTZ00050 142 ILGNMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNDDP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 262 QEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEDGGNISI 341
Cdd:PTZ00050 222 QRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 342 NDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLH 420
Cdd:PTZ00050 302 NDVDYVNAHATSTpIGDKIELKAIKKVFGDSGA----PKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLE 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKevpfFFPAcidsdcrltpaarqksheqllAKMPCQVAAPVLAPS 93
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPIT----RFDA---------------------SGFPSRIAGEVPDFD 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 GGPNFTP--TLRETRATLFAYYAAEEALTHAKLLEspakrilASFAKERIGVNIGVGMPSLADVGDVSYSLYADPekvnY 171
Cdd:cd00834 56 PEDYLDRkeLRRMDRFAQFALAAAEEALADAGLDP-------EELDPERIGVVIGSGIGGLATIEEAYRALLEKG----P 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 172 SRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMR 251
Cdd:cd00834 125 RRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 252 ALCTKYNgMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRS 331
Cdd:cd00834 205 ALSTRND-DPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 332 ALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGtssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYH 410
Cdd:cd00834 284 ALADAG-LSPEDIDYINAHGTSTpLNDAAESKAIKRVFGEHA-----KKVPVSSTKSMTGHLLGAAGAVEAIATLLALRD 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPlkeVPFFFPAcidsdcrltpaarqksheqllaKMPCQVAAPVlaps 93
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRP---ITRFDAS----------------------GLPVRIAGEV---- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 ggPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESPakrilasFAKERIGVNIGVGMPSLADVGDVSYSLYAD 165
Cdd:COG0304 52 --KDFDPEEyldrkelrRMDRFTQYALAAAREALADAGLDLDE-------VDPDRTGVIIGSGIGGLDTLEEAYRALLEK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 166 pekvNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIA 245
Cdd:COG0304 123 ----GPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 246 GFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGA 325
Cdd:COG0304 199 GFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 326 QLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTSsrrrpVYVSSVKGGLGHLLGAAGSVEAIVA 404
Cdd:COG0304 278 ARAMRAALKDAG-LSPEDIDYINAHGTSTpLGDAAETKAIKRVFGDHAYK-----VPVSSTKSMTGHLLGAAGAIEAIAS 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpffFPAcidsdcrltpaarqksheqllAKMPCQVAAPVlaps 93
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITR----FDA---------------------SDLPVKIAGEV---- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 ggPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESPAKRilasfakERIGVNIGVGMPSLADVGDVSYSLYad 165
Cdd:TIGR03150 52 --KDFDPEDyidkkearRMDRFIQYALAAAKEAVEDSGLDIEEEDA-------ERVGVIIGSGIGGLETIEEQHIVLL-- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 166 pEKvNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIA 245
Cdd:TIGR03150 121 -EK-GPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 246 GFSRMRALCTkYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGA 325
Cdd:TIGR03150 199 GFAAMKALST-RNDDPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 326 QLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGgdgtsSRRRPVYVSSVKGGLGHLLGAAGSVEAIVA 404
Cdd:TIGR03150 278 ARAMRAALKDAG-INPEDVDYINAHGTSTpLGDKAETKAIKKVFG-----DHAYKLAVSSTKSMTGHLLGAAGAIEAIFT 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1393601517 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 1393601517 13 RRRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpfFFPAcidsdcrltpaarqksheqllaKMPCQVAAPVlap 92
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITH---FDTS----------------------DLAVKIAGEV--- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 93 sggPNFTPTL----RETRA----TLFAYYAAEEALTHAKLLESPAKRilasfakERIGVNIGVGMPSLADVGDVSYSLYa 164
Cdd:PRK07314 53 ---KDFNPDDymsrKEARRmdrfIQYGIAAAKQAVEDAGLEITEENA-------DRIGVIIGSGIGGLETIEEQHITLL- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 165 dpEKvNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSI 244
Cdd:PRK07314 122 --EK-GPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 245 AGFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRG 324
Cdd:PRK07314 199 AGFAAARALSTR-NDDPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 325 AQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTSsrrrpVYVSSVKGGLGHLLGAAGSVEAIV 403
Cdd:PRK07314 278 AARAMKLALKDAG-INPEDIDYINAHGTSTpAGDKAETQAIKRVFGEHAYK-----VAVSSTKSMTGHLLGAAGAVEAIF 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393601517 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 1393601517 9 PPFIRRRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpfffpacidSDCRLtPAARQKSHEQLLAKMPCQVAAP 88
Cdd:PLN02836 1 PPLPTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQ----------DDLKM-KSEDEETQLYTLDQLPSRVAAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 89 VLAPSGGPNFTPTL-----RETRATLFAYYAAEEALTHAKLLESPAKRilasfaKERIGVNIGVGMPSLADVGDVSySLY 163
Cdd:PLN02836 70 VPRGTGPGDFDEELwlnsrSSSRFIGYALCAADEALSDARWLPSEDEA------KERTGVSIGGGIGSITDILEAA-QLI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 164 ADPEKvnySRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVS 243
Cdd:PLN02836 143 CEKRL---RRLSPFFVPRILINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 244 IAGFSRMRALCTKYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGR 323
Cdd:PLN02836 220 IAGFSRSRALSTKFNSCPTEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 324 GAQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTSSRrrpVYVSSVKGGLGHLLGAAGSVEAI 402
Cdd:PLN02836 300 GAVLAMTRALQQSG-LHPNQVDYVNAHATSTpLGDAVEARAIKTVFSEHATSGG---LAFSSTKGATGHLLGAAGAVEAI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393601517 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 1393601517 13 RRRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpffFPAcidsdcrltpaarqkshEQLLAKMPCQVaaPVLAP 92
Cdd:PRK06333 3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTD----FPV-----------------GDLATKIGGQV--PDLAE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 93 SGGPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESPAKrilasfAKERIGVNIGVGM---PSLADVGDVSys 161
Cdd:PRK06333 60 DAEAGFDPDRyldpkdqrKMDRFILFAMAAAKEALAQAGWDPDTLE------DRERTATIIGSGVggfPAIAEAVRTL-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 162 lyadpEKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITP 241
Cdd:PRK06333 132 -----DSRGPRRLSPFTIPSFLTNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 242 VSIAGFSRMRALCTKYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPE 321
Cdd:PRK06333 207 VSLAGFAAARALSTRFNDAPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPED 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 322 GRGAQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrrpVYVSSVKGGLGHLLGAAGSVE 400
Cdd:PRK06333 287 GEGARRAMLIALRQAG-IPPEEVQHLNAHATSTpVGDLGEVAAIKKVFGHVSG------LAVSSTKSATGHLLGAAGGVE 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSAtrpLKEVPFFFPAcidsdcrltpaarqksheqllaKMPCQVAAPVlaps 93
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECG---IKKITLFDAS----------------------DFPVQIAGEI---- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 ggPNFTPTL--------RETRATLFAYYAAEEALTHAKLLESpakrilaSFAKERIGVNIGVGMPSLADVGDVSYSLyad 165
Cdd:PRK08439 53 --TDFDPTEvmdpkevkKADRFIQLGLKAAREAMKDAGFLPE-------ELDAERFGVSSASGIGGLPNIEKNSIIC--- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 166 pEKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIA 245
Cdd:PRK08439 121 -FEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 246 GFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEgrGA 325
Cdd:PRK08439 200 GFAAMKALSTR-NDDPKKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 326 QLCLRSALEDGGNISINdvaYVNAHATGT-IGDDMELHALDKVLGGDGTSSRrrpvyVSSVKGGLGHLLGAAGSVEAIVA 404
Cdd:PRK08439 277 LRAMKAALEMAGNPKID---YINAHGTSTpYNDKNETAALKELFGSKEKVPP-----VSSTKGQIGHCLGAAGAIEAVIS 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393601517 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 1393601517 9 PPFIRRRVVVTGLGAVTPLGLDVASTWAALCQGRSAtrpLKEVPFFfpacidsDCrltpaarqksheqllAKMPCQVAAP 88
Cdd:PLN02787 124 PLTKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSG---ISEIERF-------DC---------------SQFPTRIAGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 89 VLAPSGGPNFTPTL--RETRATLFAYYAAEEALTHAKLLESpakrILASFAKERIGVNIGVGMPSLADVGDVSYSLyadp 166
Cdd:PLN02787 179 IKSFSTDGWVAPKLskRMDKFMLYLLTAGKKALADGGITED----VMKELDKTKCGVLIGSAMGGMKVFNDAIEAL---- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 167 eKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAG 246
Cdd:PLN02787 251 -RISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 247 FSRMRALcTKYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQ 326
Cdd:PLN02787 330 FVACRAL-SQRNDDPTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVI 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 327 LCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrrpVYVSSVKGGLGHLLGAAGSVEAIVAI 405
Cdd:PLN02787 409 LCIEKALAQSG-VSKEDVNYINAHATSTkAGDLKEYQALMRCFGQNPE------LRVNSTKSMIGHLLGAAGAVEAIATV 481
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393601517 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 1393601517 13 RRRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpffFPACIDSdCRLTPAARQKSHEQLLAKMPCQvaapvlap 92
Cdd:PRK08722 3 KRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEH----FDTTNFS-TRFAGLVKDFNCEEYMSKKDAR-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 93 sggpnftptlretRATLFAYYAAEEALthaKLLESPAKRILASFAkERIGVNIGVGMPSLADVGDVSYSLYADPEKvnys 172
Cdd:PRK08722 70 -------------KMDLFIQYGIAAGI---QALDDSGLEVTEENA-HRIGVAIGSGIGGLGLIEAGHQALVEKGPR---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 173 RVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRA 252
Cdd:PRK08722 129 KVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 253 LCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSA 332
Cdd:PRK08722 209 LSTR-NDEPQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 333 LEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGTssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQ 411
Cdd:PRK08722 288 MRDAG-VTGEQIGYVNAHGTSTpAGDVAEIKGIKRALGEAGS----KQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQ 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1393601517 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 1393601517 16 VVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvPFF----FPACI------DSDCRLTPAA-RQKSHEQllaKMPCQ 84
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDD-PFVeefdLPVRIgghlleEFDHQLTRVElRRMSYLQ---RMSTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 85 VAAPVLAPSGGPNFTPtlretratlfayyaaeealthakllespakrilasfakERIGVNIGVGMPSLADVGDVsyslYA 164
Cdd:PRK07910 90 LGRRVWENAGSPEVDT--------------------------------------NRLMVSIGTGLGSAEELVFA----YD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 165 DPEKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSI 244
Cdd:PRK07910 128 DMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 245 AGFSRMRALCTKYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRG 324
Cdd:PRK07910 208 AGFAQMRIVMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGER 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 325 AQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDgtssrRRPVYVSsvKGGLGHLLGAAGSVEAIV 403
Cdd:PRK07910 288 AGHAMTRAIELAG-LTPGDIDHVNAHATGTsVGDVAEGKAINNALGGH-----RPAVYAP--KSALGHSVGAVGAVESIL 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRplkevpfffpacidsdcrltpaarqKSHEQLLAKMPCQVA-APVLAP 92
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGIT-------------------------FSPEFAEMGMRSQVWgNVKLDP 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 93 SGGPNFTPTLRETRATLFAYYAAEEALTHAKLLESpakrilaSFAKERIGVNIGVGMPS---LADVGDVSYslyadpEKV 169
Cdd:PRK07967 57 TGLIDRKVMRFMGDASAYAYLAMEQAIADAGLSEE-------QVSNPRTGLIAGSGGGStrnQVEAADAMR------GPR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 170 NYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAgFSR 249
Cdd:PRK07967 124 GPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 250 MRALCTKYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAphPEGRGAQLCL 329
Cdd:PRK07967 203 MGALSTKYNDTPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCM 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 330 RSALEDGGnisiNDVAYVNAHATGT-IGDDMELHALDKVLgGDGTSSrrrpvyVSSVKGGLGHLLGAAGSVEAIVAIMSL 408
Cdd:PRK07967 281 QMALATVD----TPIDYINTHGTSTpVGDVKELGAIREVF-GDKSPA------ISATKSLTGHSLGAAGVQEAIYSLLMM 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393601517 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 1393601517 118 ALTHAKLLESPAKrilasfAKERIGVNIGvGMPSLADVgdVSYSLYADPEkvnysRVNPLFVPKILGNMVTGLTAMKYGI 197
Cdd:PRK14691 15 SLTHADNTEKQER------TATIIGAGIG-GFPAIAHA--VRTSDSRGPK-----RLSPFTVPSFLVNLAAGHVSIKHHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 198 MGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCTKYNGMPQEASRPFDKDRGGFVM 277
Cdd:PRK14691 81 KGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHFNSTPEKASRPFDTARDGFVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 278 GEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEDGGnISINDVAYVNAHATGT-IG 356
Cdd:PRK14691 161 GEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAG-ITPEQVQHLNAHATSTpVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 357 DDMELHALDKVLGgdgtssRRRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHA--PSAEGlerLQLVR 434
Cdd:PRK14691 240 DLGEINAIKHLFG------ESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENpdPAAKG---LNIIA 310
|
330 340 350
....*....|....*....|....*....|
gi 1393601517 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 1393601517 11 FIRRRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEvpffFPAcidsdcrltpaarqkshEQLLAKMpcqvaapvl 90
Cdd:PRK06501 8 LGRPIVAVTGMGVVTSLGQGKADNWAALTAGESGIHTITR----FPT-----------------EGLRTRI--------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 91 apSGGPNFTPTLRETRATL---FAYYAAEEALTHAKL-----------------LESPAKRILAsfakERIGVNIGVGmp 150
Cdd:PRK06501 58 --AGTVDFLPESPFGASALseaLARLAAEEALAQAGIgkgdfpgplflaappveLEWPARFALA----AAVGDNDAPS-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 151 sladvgdvsyslYADPEKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMG-PVGSSvAACATGAHCIGEAAEWIRGGRADI 229
Cdd:PRK06501 130 ------------YDRLLRAARGGRFDALHERFQFGSIADRLADRFGTRGlPISLS-TACASGATAIQLGVEAIRRGETDR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 230 VVCGGTEACITPVSIAGFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGIS 309
Cdd:PRK06501 197 ALCIATDGSVSAEALIRFSLLSALSTQ-NDPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 310 SDAHDLAAPHPEGRGAQLCLRSALEDGGnISINDVAYVNAHATGTIGDD-MELHALDKVLGgdgtsSRRRPVYVSSVKGG 388
Cdd:PRK06501 276 ADSFHRTRSSPDGSPAIGAIRAALADAG-LTPEQIDYINAHGTSTPENDkMEYLGLSAVFG-----ERLASIPVSSNKSM 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLG---LDVASTWAALCQGRSATRPLKEVPFFFPAcidsdcrltPAARQKSHEQLLAKMPCQvaapvl 90
Cdd:cd00828 1 SRVVITGIGVVSPHGegcDEVEEFWEALREGRSGIAPVARLKSRFDR---------GVAGQIPTGDIPGWDAKR------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 91 apsggpnftpTLRETRATLFAYYAAEEALTHAKLleSPAKRILASfakeRIGVNIGVGMPSLADVGDVSYSLYadpekvn 170
Cdd:cd00828 66 ----------TGIVDRTTLLALVATEEALADAGI--TDPYEVHPS----EVGVVVGSGMGGLRFLRRGGKLDA------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 171 ySRVNPLFVPK--ILGNMVTGLTAMKYGIM-GPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEAcITPVSIAGF 247
Cdd:cd00828 123 -RAVNPYVSPKwmLSPNTVAGWVNILLLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 248 SRMRALCTKYNGmPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPeGRGAQL 327
Cdd:cd00828 201 ANMGALSTAEEE-PEEMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIAR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 328 CLRSALeDGGNISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGtssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIM 406
Cdd:cd00828 279 AIRTAL-AKAGLSLDDLDVISAHGTSTpANDVAESRAIAEVAGALG-----APLPVTAQKALFGHSKGAAGALQLIGALQ 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKEVPFFfpacidsdcrltpaarqkshEQLLAKMpcqvAAPVlaps 93
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRY--------------------DGLNTRL----AAPI---- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 ggPNFTP----TLRETRA----TLFAYYAAEEALTHAKLLESPakrilaSFAKERIGVNIGVGMPSLADVGDVsyslyad 165
Cdd:PRK09116 54 --DDFELpahyTRKKIRSmgrvSLMATRASELALEDAGLLGDP------ILTDGRMGIAYGSSTGSTDPIGAF------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 166 pekvnysrvnplfvpkilGNMVT-----GLTAMKY----------------GIMGPVGSSVAACATGAHCIGEAAEWIRG 224
Cdd:PRK09116 119 ------------------GTMLLegsmsGITATTYvrmmphttavnvglffGLKGRVIPTSSACTSGSQGIGYAYEAIKY 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 225 GRADIVVCGGTEAcITPVSIAGFSRMRALCTKyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELR 304
Cdd:PRK09116 181 GYQTVMLAGGAEE-LCPTEAAVFDTLFATSTR-NDAPELTPRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 305 GFGISSDAHDLAAPHPEgrGAQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGgdgtssRRRPvyVS 383
Cdd:PRK09116 259 GFGTNSDGAHVTQPQAE--TMQIAMELALKDAG-LAPEDIGYVNAHGTATdRGDIAESQATAAVFG------ARMP--IS 327
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393601517 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 1393601517 15 RVVVTGLGAVTPLGlDVASTWAALCQGRSATRPLKEVPFFFPacidsdcrlTPAArqksheqLLAKMPCQVaapvlapsg 94
Cdd:PRK05952 3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQPFPELPP---------LPLG-------LIGNQPSSL--------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 95 gpnftPTLRETratlfayyAAEEALTHAKLleSPAkriLASfakerIGVNIGVGMPSLADVGDVSYSLYADPEKVNYSRV 174
Cdd:PRK05952 57 -----EDLTKT--------VVTAALKDAGL--TPP---LTD-----CGVVIGSSRGCQGQWEKLARQMYQGDDSPDEELD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 175 NPLFVpKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALC 254
Cdd:PRK05952 114 LENWL-DTLPHQAAIAAARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 255 tkyngmpQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALE 334
Cdd:PRK05952 193 -------KTGAYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 335 DGGnISINDVAYVNAHATGTIGDDMELHALDKVLGGDGtssrrrpVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAP 414
Cdd:PRK05952 266 RSG-LTPEDIDYIHAHGTATRLNDQREANLIQALFPHR-------VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLP 337
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1393601517 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 1393601517 15 RVVVTGLGAVTPLGLDVASTWAALCQGRSATRplkEVPFffpacidsdcRLTPAARQKSHEQLLAKMPCQVAAPVLAPSG 94
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAIS---EIPE----------DRWDADGYYPDPGKPGKTYTRRGGFLDDVDA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 95 GPN--FTPTLRETRAT-----LF---AYyaaeEALTHAKLlespakrILASFAKERIGVNIGVgmpsladvgdvSYSLYA 164
Cdd:cd00833 69 FDAafFGISPREAEAMdpqqrLLlevAW----EALEDAGY-------SPESLAGSRTGVFVGA-----------SSSDYL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 165 DPEKVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPvgsSV---AACATGAHCIGEAAEWIRGGRADIVVCGGTEACITP 241
Cdd:cd00833 127 ELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGP---SLtvdTACSSSLVALHLACQSLRSGECDLALVGGVNLILSP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 242 VSIAGFSRMRALCtkyngmPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPE 321
Cdd:cd00833 204 DMFVGFSKAGMLS------PDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 322 GRGAQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDgtSSRRRPVYVSSVKGGLGHLLGAAGSVE 400
Cdd:cd00833 278 GEAQAALIRRAYARAG-VDPSDIDYVEAHGTGTpLGDPIEVEALAKVFGGS--RSADQPLLIGSVKSNIGHLEAAAGLAG 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393601517 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 1393601517 15 RVVVTGLGAVTPLGLDVASTWAALCQGRSATRplkevpfffpacidsdcRLTPAARQKSHEQLLAKMPCQVAAPVLAPSG 94
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFG-----------------VMRRPGRQVPDDAGAGLASAFIGAELDSLAL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 95 GPNFTPTLR-----ETRATLFAyyaAEEALTHAKLLESPakrilasfaKERIGVNIG---VGMPSLADVgdvsYSLYADp 166
Cdd:PRK07103 66 PERLDAKLLrraslSAQAALAA---AREAWRDAALGPVD---------PDRIGLVVGgsnLQQREQALV----HETYRD- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 167 ekvnysrvNPLFVPK--ILGNMVT---GLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITP 241
Cdd:PRK07103 129 --------RPAFLRPsyGLSFMDTdlvGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSY 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 242 VSIAGFSRMRALCT-KYNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHP 320
Cdd:PRK07103 201 WECQALRSLGAMGSdRFADEPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 321 EGRGAqlCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDkvlggdgtSSRRRPVYVSSVKGGLGHLLGAAGSV 399
Cdd:PRK07103 281 EGEMR--VIRAALRRAG-LGPEDIDYVNPHGTGSpLGDETELAALF--------ASGLAHAWINATKSLTGHGLSAAGIV 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393601517 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 1393601517 16 VVVTGLGAVTPLGLDVASTWAALCQGRSA-----TRPLKEVPFFFPACIDSDCRLTPAArqksheqlLAKMPCqvaapvl 90
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRAGRASgmrpcDFWLVDLPTWVGEVVGVELPALPAA--------LAAFDC------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 91 apsggpnftptlRETRATLFAYYAAEEALTHAKllespakrilASFAKERIGVNIGVGMPSLADvGDVSYSLY-----AD 165
Cdd:PRK09185 69 ------------RNNRLALLALQQIEPAVEAAI----------ARYGADRIGVVLGTSTSGILE-GELAYRRRdpahgAL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 166 PEKVNYSRVNPLFVPKILGNmVTGLTAMKYGImgpvgSSvaACATGAHCIGEAAEWIRGGRADIVVCGGTEA-CITPVSi 244
Cdd:PRK09185 126 PADYHYAQQELGSLADFLRA-YLGLSGPAYTI-----ST--ACSSSAKVFASARRLLEAGLCDAAIVGGVDSlCRLTLN- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 245 aGFSRMRALCTkyngmpqEASRPFDKDRGGFVMGEGSGIIVLEhlehamqRGAQIFAELRGFGISSDAHDLAAPHPEGRG 324
Cdd:PRK09185 197 -GFNSLESLSP-------QPCRPFSANRDGINIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 325 AQLCLRSALEDGGnISINDVAYVNAHATGTIGDD-MELHALDKVLGGDgtssrrrpVYVSSVKGGLGHLLGAAGSVEAIV 403
Cdd:PRK09185 262 AILAMQQALADAG-LAPADIGYINLHGTATPLNDaMESRAVAAVFGDG--------VPCSSTKGLTGHTLGAAGAVEAAI 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393601517 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 1393601517 105 TRATLFAYYAAEEALTHAKLLESPAKrilasfaKERIGVNIGVGMPSladvgdvsySLYADPEKVNYSRVNPLFVPKILG 184
Cdd:cd00825 9 SYVSILGFEAAERAIADAGLSREYQK-------NPIVGVVVGTGGGS---------PRFQVFGADAMRAVGPYVVTKAMF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 185 NMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALctkyngMPQEA 264
Cdd:cd00825 73 PGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALS------TPEKA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 265 SRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEdGGNISINDV 344
Cdd:cd00825 147 SRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALA-VAGLTVWDI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 345 AYVNAHATGT-IGDDMELHALDKVLGGdgtssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLhaps 423
Cdd:cd00825 226 DYLVAHGTGTpIGDVKELKLLRSEFGD-------KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHI---- 294
|
330 340 350
....*....|....*....|....*....|....*...
gi 1393601517 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 1393601517 134 ASFAKERIGVNIGVGMpsladvGDVSYSLYADPEKVNysrvnPLFVPKILGNMVTGLTAMKYGIMGPvgsSVA---ACAT 210
Cdd:COG3321 111 ESLAGSRTGVFVGASS------NDYALLLLADPEAID-----AYALTGNAKSVLAGRISYKLDLRGP---SVTvdtACSS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 211 GAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCtkyngmPQEASRPFDKDRGGFVMGEGSGIIVLEHLE 290
Cdd:COG3321 177 SLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS------PDGRCRAFDADADGYVRGEGVGVVVLKRLS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 291 HAMQRGAQIFAELRGFGISSDAHD--LAAPHPEGRgaQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKV 367
Cdd:COG3321 251 DALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQ--AAVIRRALADAG-VDPATVDYVEAHGTGTpLGDPIEAAALTAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 368 LGGDGtsSRRRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHAPS-----AEGleRLQLVRGHAPLPFQ 442
Cdd:COG3321 328 FGQGR--PADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNphidfENS--PFYVNTELRPWPAG 403
|
330
....*....|....*...
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKevpfffpacidsDCRLTPAARQKSHEQLLAKMPCQVAAPVlaps 93
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIP------------ADRWDPDKLYDPPSRIAGKIYTKWGGLD---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 GGPNFTPTL-----RETRAT----LFAYYAAEEALTHAKLLEspakrilASFAKERIGVNIGVGMPSLADvgdvsysLYA 164
Cdd:pfam00109 65 DIFDFDPLFfgispREAERMdpqqRLLLEAAWEALEDAGITP-------DSLDGSRTGVFIGSGIGDYAA-------LLL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 165 DPEKVNYSRVNPLFVPKIlGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSI 244
Cdd:pfam00109 131 LDEDGGPRRGSPFAVGTM-PSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGF 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1393601517 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 1393601517 300 FAELRGFGISSDAHDLAAPHPEGRGAQLCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDGtssRRR 378
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAG-VDPEDVDYVEAHGTGTpLGDPIEAEALKRVFGSGA---RKQ 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1393601517 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 1393601517 107 ATLFAYYAAEEALTHAKLLESpakrilasFAKERIGVNIGVG--------------MPSLADVGDVSYSLYADPE----- 167
Cdd:TIGR02813 93 SQLLSLVVAKEVLNDAGLPDG--------YDRDKIGITLGVGggqkqssslnarlqYPVLKKVFKASGVEDEDSEmlikk 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 168 -KVNYSRVNPLFVPKILGNMVTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAG 246
Cdd:TIGR02813 165 fQDQYIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 247 FSRMRALCTkyngmpQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAH--DLAAPHPEGRG 324
Cdd:TIGR02813 245 FSKTPAFTT------NEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 325 AqlCLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGGDgtSSRRRPVYVSSVKGGLGHLLGAAGSVEAIV 403
Cdd:TIGR02813 319 K--ALKRAYDDAG-FAPHTCGLIEAHGTGTaAGDVAEFGGLVSVFSQD--NDQKQHIALGSVKSQIGHTKSTAGTAGMIK 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393601517 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 1393601517 14 RRVVVTGLGAVTPLGLDVASTWAALCQGRSATRPLKevpfffpacidsdcRLTPAARqksheqllakmPCQVAAPVlaps 93
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPIT--------------RFDPSGY-----------PARLAGEV---- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 94 ggPNFTPT-------LRET-RATLFAYYAAEEALTHAKLleSPAKriLASFakerigvniGVGMPSLADVGDVSYS---- 161
Cdd:cd00832 52 --PDFDAAehlpgrlLPQTdRMTRLALAAADWALADAGV--DPAA--LPPY---------DMGVVTASAAGGFEFGqrel 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 162 --LYAD-PEKVN-------YSRVNplfvpkilgnmvTGLTAMKYGIMGPVGSSVAACATGAHCIGEAAEWIRGGrADIVV 231
Cdd:cd00832 117 qkLWSKgPRHVSayqsfawFYAVN------------TGQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRG-TPLVV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 232 CGGTEACITPVSIAGFSRMRALCTkyNGMPQEASRPFDKDRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSD 311
Cdd:cd00832 184 SGGVDSALCPWGWVAQLSSGRLST--SDDPARAYLPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 312 ahdlAAPHPeGRGAQL--CLRSALEDGGnISINDVAYVNAHATGT-IGDDMELHALDKVLGgdgtssrRRPVYVSSVKGG 388
Cdd:cd00832 262 ----PPPGS-GRPPGLarAIRLALADAG-LTPEDVDVVFADAAGVpELDRAEAAALAAVFG-------PRGVPVTAPKTM 328
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393601517 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 1393601517 187 VTGLTAMKYGIM-GPVGSSVAACATGAHCIGEAAEWIRGGRADIVVCGGTEACITpvsiagfsrmralctkyngmpqeas 265
Cdd:cd00327 46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEFVF------------------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 266 rpfdkdrggfvmGEGSGIIVLEHLEHAMQRGAQIFAELRGFGISSDAHDlAAPHPEGRGAQLCLRSALEdGGNISINDVA 345
Cdd:cd00327 101 ------------GDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGAS-MVPAVSGEGLARAARKALE-GAGLTPSDID 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 346 YVNAHATGT-IGDDMELHALDKVLGGdgtssrrRPVYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHqqappninlhapsa 424
Cdd:cd00327 167 YVEAHGTGTpIGDAVELALGLDPDGV-------RSPAVSATLIMTGHPLGAAGLAILDELLLMLEH-------------- 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 1393601517 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 1393601517 207 ACATGAHCIGEAAEWIRGGRADIVVCGGTEACITPVSIAGFSRMRALCtkyngmPQEASRPFDKDRGGFVMGEGSGIIVL 286
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGEGVGVVVL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 287 EHLEHAMQRGAQIFAELRGFGISSDAHD--LAAPHPEgrgAQLclrsaledggnisindvayvnahatgtigddmelhal 364
Cdd:smart00825 170 KRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGP---AQL------------------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393601517 365 dkvlggdgtssrrrpvYVSSVKGGLGHLLGAAGSVEAIVAIMSLYHQQAPPNINLHAPS-----AEGleRLQLVRGHAPL 439
Cdd:smart00825 210 ----------------LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNphidlEES--PLRVPTELTPW 271
|
250 260
....*....|....*....|....*
gi 1393601517 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 1393601517 271 DRGGFVMGEGSGIIVLEHLEHAMQRGAQIFAEL 303
Cdd:PRK06519 235 DGGGFILGSGGAFLVLESREHAEARGARPYARI 267
|
|
| |
