|
Name |
Accession |
Description |
Interval |
E-value |
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
65-472 |
0e+00 |
|
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: 604.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 65 KRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDASKFPTRFGGQIRGFDSQGYIDGKNDRRLDDCLRYCLVAGK 144
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 145 KALEDAGLggeNLSKLDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIELGLMGPNYSI 224
Cdd:cd00834 81 EALADAGL---DPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 225 STACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKERDGFVMGEGAGVLV 304
Cdd:cd00834 158 STACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 305 MESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDLAEVNAIK 384
Cdd:cd00834 238 LESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 385 KVFKN-TSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVANVKKQHEVNVAISNSFGF 463
Cdd:cd00834 318 RVFGEhAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGF 397
|
....*....
gi 1573240076 464 GGHNSVVVF 472
Cdd:cd00834 398 GGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
65-475 |
0e+00 |
|
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: 601.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 65 KRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDASKFPTRFGGQIRGFDSQGYIDGKNDRRLDDCLRYCLVAGK 144
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 145 KALEDAGLggeNLSKLDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIELGLMGPNYSI 224
Cdd:COG0304 81 EALADAGL---DLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 225 STACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKERDGFVMGEGAGVLV 304
Cdd:COG0304 158 STACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 305 MESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDLAEVNAIK 384
Cdd:COG0304 238 LEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 385 KVFKNT-SSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVANVKKQHEVNVAISNSFGF 463
Cdd:COG0304 318 RVFGDHaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGF 397
|
410
....*....|..
gi 1573240076 464 GGHNSVVVFSEF 475
Cdd:COG0304 398 GGHNASLVFKRY 409
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
63-477 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 593.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 63 PKKRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDASKFPTRFGGQIR--------GFDSQGYIDGKNDRRLDD 134
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlaedaeaGFDPDRYLDPKDQRKMDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 135 CLRYCLVAGKKALEDAGLGGENLSklDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIE 214
Cdd:PRK06333 82 FILFAMAAAKEALAQAGWDPDTLE--DRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 215 LGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTASRPWDKERDG 293
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 294 FVMGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTL 373
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 374 AGDLAEVNAIKKVFKNTSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVD-FDTVANVKKQHE 452
Cdd:PRK06333 320 VGDLGEVAAIKKVFGHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
|
410 420
....*....|....*....|....*
gi 1573240076 453 VNVAISNSFGFGGHNSVVVFSEFKP 477
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRRWEP 424
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
11-476 |
0e+00 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 591.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 11 VSPLESLRKQSPLLNNNNNVSNKNRSKLKRN-PSLVISASSKTSVNAPKREKDPKKRVVITGMGLVSVFGNDVDTYYERL 89
Cdd:PLN02787 74 SSGGNALSSLFGSNSVSLNRNQRRRNRAARSgKAMAVAVQPEKEVETKKKPLTKQRRVVVTGMGVVSPLGHDPDVFYNNL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 90 LAGESGISLIDRFDASKFPTRFGGQIRGFDSQGYIDGKNDRRLDDCLRYCLVAGKKALEDAGLGGENLSKLDKERGGVLV 169
Cdd:PLN02787 154 LEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAGKKALADGGITEDVMKELDKTKCGVLI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 170 GTGMGGLTVFSDGVQALiERGHRKITPFFIPYAITNMGSALLGIELGLMGPNYSISTACATSNYCFYAAANHIRRGEADL 249
Cdd:PLN02787 234 GSAMGGMKVFNDAIEAL-RISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 250 MIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKERDGFVMGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNC 329
Cdd:PLN02787 313 MLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTC 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 330 DAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDLAEVNAIKKVFKNTSSIKINATKSMIGHCLGAA 409
Cdd:PLN02787 393 DAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPELRVNSTKSMIGHLLGAA 472
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573240076 410 GGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVANVKKQH-EVNVAISNSFGFGGHNSVVVFSEFK 476
Cdd:PLN02787 473 GAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERlDIKVALSNSFGFGGHNSSILFAPYK 540
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
65-472 |
0e+00 |
|
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: 589.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 65 KRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDASKFPTRFGGQIRGFDSQGYIDGKNDRRLDDCLRYCLVAGK 144
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 145 KALEDAGLggeNLSKLDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIELGLMGPNYSI 224
Cdd:TIGR03150 81 EAVEDSGL---DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 225 STACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKERDGFVMGEGAGVLV 304
Cdd:TIGR03150 158 VTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 305 MESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDLAEVNAIK 384
Cdd:TIGR03150 238 LEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 385 KVFKN-TSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVANVKKQHEVNVAISNSFGF 463
Cdd:TIGR03150 318 KVFGDhAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGF 397
|
....*....
gi 1573240076 464 GGHNSVVVF 472
Cdd:TIGR03150 398 GGTNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
64-472 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 575.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 64 KKRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDASKFPTRFGGQIRGFDSQGYIDGKNDRRLDDCLRYCLVAG 143
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 144 KKALEDAGLggeNLSKLDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIELGLMGPNYS 223
Cdd:PRK07314 81 KQAVEDAGL---EITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 224 ISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKERDGFVMGEGAGVL 303
Cdd:PRK07314 158 IVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 304 VMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDLAEVNAI 383
Cdd:PRK07314 238 VLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 384 KKVFKN-TSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVANVKKQHEVNVAISNSFG 462
Cdd:PRK07314 318 KRVFGEhAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFG 397
|
410
....*....|
gi 1573240076 463 FGGHNSVVVF 472
Cdd:PRK07314 398 FGGTNASLVF 407
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
74-475 |
1.01e-142 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 415.63 E-value: 1.01e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 74 LVSVFGNDVDTYYERLLAGESGISLIDRFDA----------------SKFPTRFGGQIRG--FDSQGYIDGKNDrrlDDC 135
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDQseFDPSDFAPTKRE---SRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 136 LRYCLVAGKKALEDAGLggENLSKLDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIEL 215
Cdd:PTZ00050 78 THFAMAAAREALADAKL--DILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 216 GLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTASRPWDKERDGF 294
Cdd:PTZ00050 156 KLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 295 VMGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAG-VSPEEVNYINAHATSTL 373
Cdd:PTZ00050 236 VMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 374 AGDLAEVNAIKKVFKN--TSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVANvKKQH 451
Cdd:PTZ00050 316 IGDKIELKAIKKVFGDsgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQG-KTAH 394
|
410 420
....*....|....*....|....*..
gi 1573240076 452 E---VNVAISNSFGFGGHNSVVVFSEF 475
Cdd:PTZ00050 395 PlqsIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
65-475 |
7.32e-141 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 410.28 E-value: 7.32e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 65 KRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDASKFPTRFGGQIRGFDSQGYIDGKNDRRLDDCLRYCLVAGK 144
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 145 KALEDAGLGGEnlsKLDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIELGLMGPNYSI 224
Cdd:PRK08439 82 EAMKDAGFLPE---ELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 225 STACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKERDGFVMGEGAGVLV 304
Cdd:PRK08439 159 VTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 305 MESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADglGVSTCIEKSLEDAGVSpeEVNYINAHATSTLAGDLAEVNAIK 384
Cdd:PRK08439 239 LEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNP--KIDYINAHGTSTPYNDKNETAALK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 385 KVFKNTSSI-KINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVANVKKQHEVNVAISNSFGF 463
Cdd:PRK08439 315 ELFGSKEKVpPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGF 394
|
410
....*....|..
gi 1573240076 464 GGHNSVVVFSEF 475
Cdd:PRK08439 395 GGTNGVVIFKKV 406
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
64-475 |
6.14e-137 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 400.53 E-value: 6.14e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 64 KKRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDASKFPTRFGGQIRGFDSQGYIDGKNDRRLDDCLRYCLVAG 143
Cdd:PRK08722 3 KRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 144 KKALEDAGLggeNLSKLDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIELGLMGPNYS 223
Cdd:PRK08722 83 IQALDDSGL---EVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 224 ISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKERDGFVMGEGAGVL 303
Cdd:PRK08722 160 ISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 304 VMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDLAEVNAI 383
Cdd:PRK08722 240 VLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 384 KKVF--KNTSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVANVKKQHE-VNVAISNS 460
Cdd:PRK08722 320 KRALgeAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNS 399
|
410
....*....|....*
gi 1573240076 461 FGFGGHNSVVVFSEF 475
Cdd:PRK08722 400 FGFGGTNGSLIFKKM 414
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
63-473 |
1.29e-118 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 354.48 E-value: 1.29e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 63 PKKRVVITGMGLVSVFGNDVDTYYERLLAGESGI--------------SLIDRFDASKFPTRFGGQI-RG-----FDSQG 122
Cdd:PLN02836 4 PTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVraltqddlkmksedEETQLYTLDQLPSRVAALVpRGtgpgdFDEEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 123 YIdgkNDRRLDDCLRYCLVAGKKALEDAGLGGENlsKLDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYA 202
Cdd:PLN02836 84 WL---NSRSSSRFIGYALCAADEALSDARWLPSE--DEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 203 ITNMGSALLGIELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQR-NDDPQ 281
Cdd:PLN02836 159 LINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 282 TASRPWDKERDGFVMGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEE 361
Cdd:PLN02836 239 EASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 362 VNYINAHATSTLAGDLAEVNAIKKVFKN---TSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPA 438
Cdd:PLN02836 319 VDYVNAHATSTPLGDAVEARAIKTVFSEhatSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPI 398
|
410 420 430
....*....|....*....|....*....|....*..
gi 1573240076 439 VD--FDTVANVKKQhEVNVAISNSFGFGGHNSVVVFS 473
Cdd:PLN02836 399 FDdgFVPLTASKAM-LIRAALSNSFGFGGTNASLLFT 434
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
67-472 |
1.53e-97 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 300.11 E-value: 1.53e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 67 VVITGMGLVSVFGNDVDTYYERLLAGESGI-----SLIDRFDaskFPTRFGGQI-RGFDSQgyIDGKNDRRLDDCLRYCL 140
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIrtlddPFVEEFD---LPVRIGGHLlEEFDHQ--LTRVELRRMSYLQRMST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 141 VAGKKALEDAGLggenlSKLDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIELGLMGP 220
Cdd:PRK07910 89 VLGRRVWENAGS-----PEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 221 NYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRA-LSQRNDDPQTASRPWDKERDGFVMGEG 299
Cdd:PRK07910 164 VITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 300 AGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDLAE 379
Cdd:PRK07910 244 GALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 380 VNAIKKVFKNTSSiKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVANVKKQHEVNVAISN 459
Cdd:PRK07910 324 GKAINNALGGHRP-AVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINN 402
|
410
....*....|...
gi 1573240076 460 SFGFGGHNSVVVF 472
Cdd:PRK07910 403 SFGFGGHNVALAF 415
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
65-476 |
8.87e-92 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 284.64 E-value: 8.87e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 65 KRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDASKFPTRFGGQIRgFDSQGYIDGKNDRRLDDCLRYCLVAGK 144
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 145 KALEDAGLGGENLSKldkERGGVLVGTGMGGLTVFSDGVQALIE-RGHRKITPFFIPYAITNMGSALLGIELGLMGPNYS 223
Cdd:PRK07967 81 QAIADAGLSEEQVSN---PRTGLIAGSGGGSTRNQVEAADAMRGpRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 224 ISTACATSNYCFYAAANHIRRGEADLMIAGGTE------AAIipiglggFVACRALS-QRNDDPQTASRPWDKERDGFVM 296
Cdd:PRK07967 158 ISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEeldwemSCL-------FDAMGALStKYNDTPEKASRAYDANRDGFVI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 297 GEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPraDGLGVSTCIEKSLedAGVSpEEVNYINAHATSTLAGD 376
Cdd:PRK07967 231 AGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAP--SGEGAVRCMQMAL--ATVD-TPIDYINTHGTSTPVGD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 377 LAEVNAIKKVFKNTSSiKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAV-DFDTVANVKKQHEVNV 455
Cdd:PRK07967 306 VKELGAIREVFGDKSP-AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVTETTDNAELTT 384
|
410 420
....*....|....*....|.
gi 1573240076 456 AISNSFGFGGHNSVVVFSEFK 476
Cdd:PRK07967 385 VMSNSFGFGGTNATLVFRRYK 405
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
65-472 |
1.74e-89 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 278.79 E-value: 1.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 65 KRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDasKFP---TRFGGQIRGFDSQGYIDGKNDRRLDDCLRYCLV 141
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWD--RYDglnTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 142 AGKKALEDAGLGGENLskLDKERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIELGLMGPN 221
Cdd:PRK09116 80 ASELALEDAGLLGDPI--LTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 222 YSISTACATSNYCFYAAANHIRRGEADLMIAGG------TEAAIipiglggFVACRALSQRNDDPQTASRPWDKERDGFV 295
Cdd:PRK09116 158 IPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGaeelcpTEAAV-------FDTLFATSTRNDAPELTPRPFDANRDGLV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 296 MGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVstCIEKSLEDAGVSPEEVNYINAHATSTLAG 375
Cdd:PRK09116 231 IGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQI--AMELALKDAGLAPEDIGYVNAHGTATDRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 376 DLAEVNAIKKVFKNtsSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAV-DFDTVANVKKQHEVN 454
Cdd:PRK09116 309 DIAESQATAAVFGA--RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTE 386
|
410
....*....|....*...
gi 1573240076 455 VAISNSFGFGGHNSVVVF 472
Cdd:PRK09116 387 YVMSNNFAFGGINTSLIF 404
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
61-473 |
8.36e-87 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 272.27 E-value: 8.36e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 61 KDPKKR--VVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDASKFPTRFGGQIRGFDSQGYIDGKNDRRLDDclry 138
Cdd:PRK06501 5 RDHLGRpiVAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDFLPESPFGASALSEALAR---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 139 clVAGKKALEDAGLGGENL----------SKLD-KERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAItnmg 207
Cdd:PRK06501 81 --LAAEEALAQAGIGKGDFpgplflaappVELEwPARFALAAAVGDNDAPSYDRLLRAARGGRFDALHERFQFGSI---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 208 SALLGIELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPW 287
Cdd:PRK06501 155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 288 DKERDGFVMGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINA 367
Cdd:PRK06501 235 SKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 368 HATSTLAGDLAEVNAIKKVF-KNTSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVAN 446
Cdd:PRK06501 315 HGTSTPENDKMEYLGLSAVFgERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPN 394
|
410 420
....*....|....*....|....*..
gi 1573240076 447 VKKQHEVNVAISNSFGFGGHNSVVVFS 473
Cdd:PRK06501 395 VARDARVTAVLSNSFGFGGQNASLVLT 421
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
162-475 |
4.03e-84 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 262.74 E-value: 4.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 162 KERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAITNMGSALLGIELGLMGPNYSISTACATSNYCFYAAANH 241
Cdd:PRK14691 25 QERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 242 IRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTASRPWDKERDGFVMGEGAGVLVMESLEHAMKRGAPILA 320
Cdd:PRK14691 105 IRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 321 EYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDLAEVNAIKKVFKNTSSIKINATKS 400
Cdd:PRK14691 185 EIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNALAITSTKS 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1573240076 401 MIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVD-FDTVANVKKQHEVNVAISNSFGFGGHNSVVVFSEF 475
Cdd:PRK14691 265 ATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKRW 340
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
66-471 |
1.50e-78 |
|
"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: 250.43 E-value: 1.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 66 RVVITGMGLVS---VFGNDVDTYYERLLAGESGISLIDRFDaSKFPTRFGGQIRGFDSQGYiDGKNDRRLDDCLRYCLVA 142
Cdd:cd00828 2 RVVITGIGVVSphgEGCDEVEEFWEALREGRSGIAPVARLK-SRFDRGVAGQIPTGDIPGW-DAKRTGIVDRTTLLALVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 143 GKKALEDAGLGGEnlSKLDKERGGVLVGTGMGGLTVFSDGVQALiergHRKITPFFIPYAI--TNMGSALLGIELGLM-G 219
Cdd:cd00828 80 TEEALADAGITDP--YEVHPSEVGVVVGSGMGGLRFLRRGGKLD----ARAVNPYVSPKWMlsPNTVAGWVNILLLSShG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 220 PNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAaIIPIGLGGFVACRALSQRNDDPQTASRPWDKERDGFVMGEG 299
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 300 AGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPrADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDLAE 379
Cdd:cd00828 233 AGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVP-AGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 380 VNAIKKVFKN-TSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSIN--QFNPEPAVDFDTVANVKKQHEVNVA 456
Cdd:cd00828 312 SRAIAEVAGAlGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANldDVDPDVEHLSVVGLSRDLNLKVRAA 391
|
410
....*....|....*
gi 1573240076 457 ISNSFGFGGHNSVVV 471
Cdd:cd00828 392 LVNAFGFGGSNAALV 406
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
64-471 |
3.42e-78 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 249.56 E-value: 3.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 64 KKRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDR--------FDASKFPTRFGGQIRGFDSQGYIDGKNDRRLDDC 135
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRpgrqvpddAGAGLASAFIGAELDSLALPERLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 136 LRYCLVAGKKALEDAGLGGEnlsklDKERGGVLVGtgmgGLTVFSDgVQALIERGHRKiTPFFIP--YAITNMGSALLGI 213
Cdd:PRK07103 81 AQAALAAAREAWRDAALGPV-----DPDRIGLVVG----GSNLQQR-EQALVHETYRD-RPAFLRpsYGLSFMDTDLVGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 214 ---ELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRAL-SQRN-DDPQTASRPWD 288
Cdd:PRK07103 150 cseQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMgSDRFaDEPEAACRPFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 289 KERDGFVMGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPraDGLGVSTCIEKSLEDAGVSPEEVNYINAH 368
Cdd:PRK07103 230 QDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 369 ATSTLAGDLAEVNAIKKVfkNTSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPepaVD--FDTVAN 446
Cdd:PRK07103 308 GTGSPLGDETELAALFAS--GLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEP---IDerFRWVGS 382
|
410 420
....*....|....*....|....*
gi 1573240076 447 VKKQHEVNVAISNSFGFGGHNSVVV 471
Cdd:PRK07103 383 TAESARIRYALSLSFGFGGINTALV 407
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
66-471 |
6.18e-69 |
|
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: 225.90 E-value: 6.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 66 RVVITGMGLVsvF--GNDVDTYYERLLAGESGISLI--DRFDASKFP----------TRFGG---QIRGFDSQGY-IDGK 127
Cdd:cd00833 2 PIAIVGMACR--FpgAADPDEFWENLLEGRDAISEIpeDRWDADGYYpdpgkpgktyTRRGGfldDVDAFDAAFFgISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 128 NDRRLDDCLRYCLVAGKKALEDAGLGGEnlsKLDKERGGVLVGtgmggltVFSDGVQALIERGHRKITPFFIPYAITNMG 207
Cdd:cd00833 80 EAEAMDPQQRLLLEVAWEALEDAGYSPE---SLAGSRTGVFVG-------ASSSDYLELLARDPDEIDAYAATGTSRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 208 SALLGIELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSqrnDDPQtaSRPW 287
Cdd:cd00833 150 ANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS---PDGR--CRPF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 288 DKERDGFVMGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAH--HMTDPRADGLgvSTCIEKSLEDAGVSPEEVNYI 365
Cdd:cd00833 225 DADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEAQ--AALIRRAYARAGVDPSDIDYV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 366 NAHATSTLAGDLAEVNAIKKVFK----NTSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDF 441
Cdd:cd00833 303 EAHGTGTPLGDPIEVEALAKVFGgsrsADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDF 382
|
410 420 430
....*....|....*....|....*....|....*...
gi 1573240076 442 D----TVANVKKQHEVNVAIS----NSFGFGGHNSVVV 471
Cdd:cd00833 383 EesplRVPTEARPWPAPAGPRragvSSFGFGGTNAHVI 420
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
66-473 |
5.53e-67 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 219.54 E-value: 5.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 66 RVVITGMGLVSVFGNDVDTYyERLLAGESGISLIDRF-DASKFPtrfggqirgfdsQGYIdGKNDRRLDDCLRYCLVAgk 144
Cdd:PRK05952 3 KVVVTGIGLVSALGDLEQSW-QRLLQGKSGIKLHQPFpELPPLP------------LGLI-GNQPSSLEDLTKTVVTA-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 145 kALEDAGLggenlsKLDKERGGVLVGTgmggltvfSDGVQALIERGHRKITPFFIPYAIT-----------NMGSALLGI 213
Cdd:PRK05952 67 -ALKDAGL------TPPLTDCGVVIGS--------SRGCQGQWEKLARQMYQGDDSPDEEldlenwldtlpHQAAIAAAR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 214 ELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQrnddpqTASRPWDKERDG 293
Cdd:PRK05952 132 QIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 294 FVMGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTL 373
Cdd:PRK05952 206 LVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 374 AGDLAEVNAIKKVFknTSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVAnvkKQHEV 453
Cdd:PRK05952 286 LNDQREANLIQALF--PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNFVRQA---QQSPL 360
|
410 420
....*....|....*....|
gi 1573240076 454 NVAISNSFGFGGHNSVVVFS 473
Cdd:PRK05952 361 QNVLCLSFGFGGQNAAIALG 380
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
65-311 |
4.64e-64 |
|
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: 207.87 E-value: 4.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 65 KRVVITGMGLVSVFGNDVDTYYERLLAGESGISLI--DRFDASKF---PTRFGGQIRG----------FDSQgyIDGKND 129
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTkwgglddifdFDPL--FFGISP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 130 R---RLDDCLRYCLVAGKKALEDAGLGGENLsklDKERGGVLVGTGMGGLtvfsDGVQALIERG-HRKITPFFIPYaITN 205
Cdd:pfam00109 79 ReaeRMDPQQRLLLEAAWEALEDAGITPDSL---DGSRTGVFIGSGIGDY----AALLLLDEDGgPRRGSPFAVGT-MPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 206 MGSALLGIELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSQrnDDPQTASR 285
Cdd:pfam00109 151 VIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFD 228
|
250 260
....*....|....*....|....*.
gi 1573240076 286 PWDkerDGFVMGEGAGVLVMESLEHA 311
Cdd:pfam00109 229 PFA---DGFVRGEGVGAVVLKRLSDA 251
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
65-471 |
2.04e-59 |
|
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: 200.28 E-value: 2.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 65 KRVVITGMGLVSVFGNDVDTYYERLLAGESGISLIDRFDASKFPTRFGGQIRGFDSQGYIDGKNDRRLDDCLRYCLVAGK 144
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 145 KALEDAGLGGENLSKLDKergGVLVGTGMGGLTVFSDGVQALIERGHRKITPF-----FipYAITnmgSALLGIELGLMG 219
Cdd:cd00832 81 WALADAGVDPAALPPYDM---GVVTASAAGGFEFGQRELQKLWSKGPRHVSAYqsfawF--YAVN---TGQISIRHGMRG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 220 PNYSISTACATSNYCFYAAANHIRRGeADLMIAGGTEAAIIPIGLGGFVACRALSqRNDDPQTASRPWDKERDGFVMGEG 299
Cdd:cd00832 153 PSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLS-TSDDPARAYLPFDAAAAGYVPGEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 300 AGVLVMESLEHAMKRGAPILAEYLGGAVNcdahhMTDPRADGL--GVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDL 377
Cdd:cd00832 231 GAILVLEDAAAARERGARVYGEIAGYAAT-----FDPPPGSGRppGLARAIRLALADAGLTPEDVDVVFADAAGVPELDR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 378 AEVNAIKKVFkNTSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDFDTVANVKKQHEVNVAI 457
Cdd:cd00832 306 AEAAALAAVF-GPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTAL 384
|
410
....*....|....
gi 1573240076 458 SNSFGFGGHNSVVV 471
Cdd:cd00832 385 VLARGRGGFNSALV 398
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
137-471 |
3.06e-54 |
|
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: 184.76 E-value: 3.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 137 RYCLVAGKKALEDAGLGGENLSKldkERGGVLVGTGMGGLTVFSDGVQALIERGHRKITPFFIPYAitnmgSALLGIELG 216
Cdd:cd00825 13 ILGFEAAERAIADAGLSREYQKN---PIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGA-----SGQIATPLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 217 LMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSqrnddPQTASRPWDKERDGFVM 296
Cdd:cd00825 85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 297 GEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGD 376
Cdd:cd00825 160 GDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 377 LAEVNAIKKVFKNtSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPavDFDTVANVKKQHEVNVA 456
Cdd:cd00825 240 VKELKLLRSEFGD-KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTA 316
|
330
....*....|....*
gi 1573240076 457 ISNSFGFGGHNSVVV 471
Cdd:cd00825 317 LLNGFGLGGTNATLV 331
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
67-473 |
7.79e-50 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 174.65 E-value: 7.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 67 VVITGMGLVSVFGNDVDTYYERLLAG-ESGISLIDRFDASkFPTRFGG-----------QIRGFDSqgyidgKNDRRLDD 134
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRAGrASGMRPCDFWLVD-LPTWVGEvvgvelpalpaALAAFDC------RNNRLALL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 135 CLRyclvAGKKALEDAglggenLSKLDKERGGVLVGTGMGGLtvfSDGVQALIER-GHRKITPFFIPYAITNMGSA--LL 211
Cdd:PRK09185 77 ALQ----QIEPAVEAA------IARYGADRIGVVLGTSTSGI---LEGELAYRRRdPAHGALPADYHYAQQELGSLadFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 212 GIELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGG-------TeaaiipigLGGFVACRALSQrnddpqTAS 284
Cdd:PRK09185 144 RAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGvdslcrlT--------LNGFNSLESLSP------QPC 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 285 RPWDKERDGFVMGEGAGVLVMEslehamkRGAPILAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNY 364
Cdd:PRK09185 210 RPFSANRDGINIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 365 INAHATSTLAGDLAEVNAIKKVFKNT---SSikinaTKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFNPEPAVDF 441
Cdd:PRK09185 283 INLHGTATPLNDAMESRAVAAVFGDGvpcSS-----TKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPP 357
|
410 420 430
....*....|....*....|....*....|..
gi 1573240076 442 DTVANVKKQHEVNVAISNSFGFGGHNSVVVFS 473
Cdd:PRK09185 358 LYLVENAQALAIRYVLSNSFAFGGNNCSLIFG 389
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
67-474 |
8.51e-50 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 183.15 E-value: 8.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 67 VVITGMGlvSVF--GNDVDTYYERLLAGESGISLI--DRFDASKF-----------PTRFGG---QIRGFDSQGY-IDGK 127
Cdd:COG3321 6 IAIIGMA--CRFpgADDPEEFWRNLRAGRDAITEVpaDRWDADAYydpdpdapgktYVRWGGfldDVDEFDALFFgISPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 128 NDRRLDDCLRYCLVAGKKALEDAGLGGEnlsKLDKERGGVLVGTGMGGLTVFSDGVQALIErghrkitpffiPYAIT-NM 206
Cdd:COG3321 84 EAEAMDPQQRLLLEVAWEALEDAGYDPE---SLAGSRTGVFVGASSNDYALLLLADPEAID-----------AYALTgNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 207 GSALLG-I--ELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTeAAIIPIGLG-GFVACRALSqrnddPQT 282
Cdd:COG3321 150 KSVLAGrIsyKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGV-NLMLTPESFiLFSKGGMLS-----PDG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 283 ASRPWDKERDGFVMGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHH--MTDPRadGLGVSTCIEKSLEDAGVSPE 360
Cdd:COG3321 224 RCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSngLTAPN--GPAQAAVIRRALADAGVDPA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 361 EVNYINAHATSTLAGDLAEVNAIKKVFKNTSSIK----INATKSMIGHCLGAAG--GLeaIATVKAINTGWLHPSINQFN 434
Cdd:COG3321 302 TVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPADqpcaIGSVKSNIGHLEAAAGvaGL--IKAVLALRHGVLPPTLHFET 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1573240076 435 PEPAVDFDTvANVK----------KQHEVNVAISnSFGFGGHNSVVVFSE 474
Cdd:COG3321 380 PNPHIDFEN-SPFYvntelrpwpaGGGPRRAGVS-SFGFGGTNAHVVLEE 427
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
319-431 |
7.07e-42 |
|
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: 145.02 E-value: 7.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 319 LAEYLGGAVNCDAHHMTDPRADGLGVSTCIEKSLEDAGVSPEEVNYINAHATSTLAGDLAEVNAIKKVF---KNTSSIKI 395
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFgsgARKQPLAI 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1573240076 396 NATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSIN 431
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLN 116
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
67-474 |
9.45e-27 |
|
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: 109.34 E-value: 9.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 67 VVITGMGLVsvF--GNDVDTYYERLLAGESGIsliDRFDASKFptrfggqirgfdsqgyidGKNDR---RLDDCLRYCLV 141
Cdd:smart00825 1 IAIVGMSCR--FpgADDPEEFWDLLLAGLDDV---DLFDAAFF------------------GISPReaeAMDPQQRLLLE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 142 AGKKALEDAGLggeNLSKLDKERGGVLVGTGMGGltvfsdgvqalierghrkitpffipYAITnmgsallgielglmgpn 221
Cdd:smart00825 58 VAWEALEDAGI---DPESLRGSRTGVFVGVSSSD-------------------------YSVT----------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 222 ysISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRALSqrnddPQTASRPWDKERDGFVMGEGAG 301
Cdd:smart00825 93 --VDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 302 VLVMESLEHAMKRGAPILAEYLGGAVNCDAhhmtdpRADGLGVstcieksledagvsPeevnyinaHATSTLAgdlaevn 381
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSAVNQDG------RSNGITA--------------P--------SGPAQLL------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 382 aikkvfkntssikINATKSMIGHCLGAAG--GLeaIATVKAINTGWLHPSINQFNPEPAVDFDTvANVKKQHEV------ 453
Cdd:smart00825 211 -------------IGSVKSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPHIDLEE-SPLRVPTELtpwppp 274
|
410 420
....*....|....*....|....*
gi 1573240076 454 ----NVAIsNSFGFGGHNSVVVFSE 474
Cdd:smart00825 275 grprRAGV-SSFGFGGTNAHVILEE 298
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
140-477 |
2.13e-26 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 113.56 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 140 LVAGKKALEDAGLGgenlSKLDKERGGVLVGTGMG-----GLT----------VF-SDGV-----QALIERG-----HRK 193
Cdd:TIGR02813 98 LVVAKEVLNDAGLP----DGYDRDKIGITLGVGGGqkqssSLNarlqypvlkkVFkASGVededsEMLIKKFqdqyiHWE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 194 ITPFfiPYAITNMGSALLGIELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAAIIPIGLGGFVACRAL 273
Cdd:TIGR02813 174 ENSF--PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 274 SQRNDdpqtaSRPWDKERDGFVMGEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCDAHHMT--DPRADGLgvSTCIEKS 351
Cdd:TIGR02813 252 TTNED-----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSiyAPRPEGQ--AKALKRA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 352 LEDAGVSPEEVNYINAHATSTLAGDLAEVNAIKKVFKNTSS----IKINATKSMIGHCLGAAGGLEAIATVKAINTGWLH 427
Cdd:TIGR02813 325 YDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLP 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 428 PSINQFNPEPAVDFD-------TVANVKKQHEVNV---AISNSFGFGGHNSVVVFSEFKP 477
Cdd:TIGR02813 405 PTINVDQPNPKLDIEnspfylnTETRPWMQREDGTprrAGISSFGFGGTNFHMVLEEYSP 464
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
137-471 |
2.26e-26 |
|
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: 107.14 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 137 RYCLVAGKKALEDAGLGGEnlskldkERGGVLVGTGMGGLTVFSDGVQALIERGhrkitpffipyaitnmgsallgielG 216
Cdd:cd00327 9 ELGFEAAEQAIADAGLSKG-------PIVGVIVGTTGGSGEFSGAAGQLAYHLG-------------------------I 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 217 LMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAaiipiglggfvacralsqrnddpqtasrpwdkerdgFVM 296
Cdd:cd00327 57 SGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVF 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 297 GEGAGVLVMESLEHAMKRGAPILAEYLGGAVNCD-AHHMTDPRADGLgvSTCIEKSLEDAGVSPEEVNYINAHATSTLAG 375
Cdd:cd00327 101 GDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVSGEGL--ARAARKALEGAGLTPSDIDYVEAHGTGTPIG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 376 DLAEVNAIKKVFkNTSSIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSinqfnPEPAvdfdtvanvkkqhevNV 455
Cdd:cd00327 179 DAVELALGLDPD-GVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT-----PREP---------------RT 237
|
330
....*....|....*.
gi 1573240076 456 AISNSFGFGGHNSVVV 471
Cdd:cd00327 238 VLLLGFGLGGTNAAVV 253
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
67-414 |
1.68e-06 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 49.95 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 67 VVITGMGLVSVFGNDVDTYYERLLAGEsgisLIDRFDASKF---PTRFGGQIrGFDSQgyIDGKND-RRLDDCLRYCLVA 142
Cdd:PRK06519 8 VVITGIGLVSSLGEGLDAHWNALSAGR----PQPNVDTETFapyPVHPLPEI-DWSQQ--IPKRGDqRQMETWQRLGTYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 143 GKKALEDAGLGG--ENLSKLDkerggVLVGTGmGG---LTVFSDGVQALIERGHRkitpffipyaitnmGSAL---LGIE 214
Cdd:PRK06519 81 AGLALDDAGIKGneELLSTMD-----MIVAAG-GGerdIAVDTAILNEARKRNDR--------------GVLLnerLMTE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 215 L----------GLMGPNYSISTACATSNYCFYA-----------AANHIRRGEADLMIAGGTEAA-----IIPIGLGGFV 268
Cdd:PRK06519 141 LrptlflaqlsNLLAGNISIVHKVTGSSRTFMGeesagvsaieiAFARIASGQSDHALVGGAYNAerpdmLLLYELGGLL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 269 AcralsqrnddpQTASRP-WDKERD---GFVMGEGAGVLVMESLEHAMKRGAPILAEyLGGAVNCDAhhmtdPRADGlGV 344
Cdd:PRK06519 221 L-----------KGGWAPvWSRGGEdggGFILGSGGAFLVLESREHAEARGARPYAR-ISGVESDRA-----RRAPG-DL 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 345 STCIEKSLEDAGVSPEEVNYINAhatSTLAGDLAEvnAIKKVFKNTSSIKINATKSMIGHclgaagGLEA 414
Cdd:PRK06519 283 EASLERLLKPAGGLAAPTAVISG---ATGAHPATA--EEKAALEAALAGPVRGIGTLFGH------TMEA 341
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
142-368 |
5.54e-05 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 45.33 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 142 AGKKALEDAGLGGenlskldKERGGVLVGTGMGGLTVFsdgvqalierghrkitpffipyaitnMGSALLGIELGLMG-P 220
Cdd:cd00829 23 AARAALDDAGLEP-------ADIDAVVVGNAAGGRFQS--------------------------FPGALIAEYLGLLGkP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 221 NYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEA--------------------------AIIPIGLGGF------- 267
Cdd:cd00829 70 ATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKmsdvptgdeaggrasdlewegpeppgGLTPPALYALaarrymh 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 268 -------------VACRALSQRNDDPQT----------ASRP-WD--KERDGFVMGEGAGVLVMESLEHAMKRGAPiLAE 321
Cdd:cd00829 150 rygttredlakvaVKNHRNAARNPYAQFrkpitvedvlNSRMiADplRLLDCCPVSDGAAAVVLASEERARELTDR-PVW 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1573240076 322 YLGGAVNCDAHHMTDPRADGL--GVSTCIEKSLEDAGVSPEEVNYINAH 368
Cdd:cd00829 229 ILGVGAASDTPSLSERDDFLSldAARLAARRAYKMAGITPDDIDVAELY 277
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
220-300 |
2.00e-04 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 43.52 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 220 PNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAA-IIPIGLGGFVACRALSQRNDDPQTASRPWDkERDGFVMGE 298
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMsRAPMLLPKARWGYRMNAKLVDPMINPGLTD-PYTGLSMGE 158
|
..
gi 1573240076 299 GA 300
Cdd:COG0183 159 TA 160
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
298-410 |
2.12e-04 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 43.60 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 298 EGAGVLVMESLEHAMKRGAPILAEYLG-GAVNCdahhmtDPRADGLGVSTCIEKSLEDAGVSPEEVnyinahatstlagD 376
Cdd:PLN02287 292 DGAGAVLLMKRSVAMQKGLPILGVFRSfAAVGV------DPAVMGIGPAVAIPAAVKAAGLELDDI-------------D 352
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1573240076 377 LAEVN---------AIKKVFKNTSSIKINATKSMIGHCLGAAG 410
Cdd:PLN02287 353 LFEINeafasqfvyCCKKLGLDPEKVNVNGGAIALGHPLGATG 395
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
142-256 |
4.73e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 39.11 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 142 AGKKALEDAGLGGENLSKLdkerggvLVGTGMGGLtvFSDgvQALIerghrkitpffipyaitnmgSALLGIELGLMG-P 220
Cdd:PRK06064 29 AGLEALEDAGIDGKDIDAM-------YVGNMSAGL--FVS--QEHI--------------------AALIADYAGLAPiP 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 1573240076 221 NYSISTACATSNYCFYAAANHIRRGEADLMIAGGTE 256
Cdd:PRK06064 78 ATRVEAACASGGAALRQAYLAVASGEADVVLAAGVE 113
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
209-300 |
5.86e-03 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 38.75 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 209 ALLGIELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEA-AIIPIGLGGFVACRALSQRNDDPQTASRPW 287
Cdd:TIGR01930 64 AALLAGLPESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESmSRVPYGVPRSLRWGVKPGNAELEDARLKDL 143
|
90
....*....|...
gi 1573240076 288 DKERDGFVMGEGA 300
Cdd:TIGR01930 144 TDANTGLPMGVTA 156
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
300-422 |
7.60e-03 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 38.61 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 300 AGVLVMeSLEHAMKRGAPILAEYLGGAVN-CDAHHMtdpradGLGVSTCIEKSLEDAGVSPEEVNYI---NAHATSTLA- 374
Cdd:cd00751 249 AAVLLM-SEEKAKELGLKPLARIVGYAVAgVDPAIM------GIGPVPAIPKALKRAGLTLDDIDLIeinEAFAAQALAc 321
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1573240076 375 -----GDLAEVNAikkvfkNTSSIkinAtksmIGHCLGAAGgleAIATVKAIN 422
Cdd:cd00751 322 lkelgLDPEKVNV------NGGAI---A----LGHPLGASG---ARIVVTLLH 358
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
220-300 |
7.94e-03 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 38.61 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573240076 220 PNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTEAA-IIPIGLGGfvacRALSQRNDDPQTASRPWDKERDGFV--- 295
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMsRAPYLLPK----ARRGGRLGLNTLDGMLDDGLTDPFTgls 151
|
....*
gi 1573240076 296 MGEGA 300
Cdd:cd00751 152 MGITA 156
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
209-265 |
8.35e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 38.34 E-value: 8.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1573240076 209 ALLGIELGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMIAGGTE-AAIIPIGLG 265
Cdd:PRK09268 74 CVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDtTSDAPIAVN 131
|
|
| |
