|
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 ... |
61-468 |
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: 608.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 61 KRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKFPTRFAGQIRGFNSEGYIDGKNDRRLDDCLRYCIVAGK 140
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 141 KALEDADLggdKLSKIDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIELGLMGPNYSI 220
Cdd:cd00834 81 EALADAGL---DPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 221 STACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLI 300
Cdd:cd00834 158 STACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 301 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEINAIK 380
Cdd:cd00834 238 LESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 381 KVFKNTLD-IKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVANEKQQHEVNVAISNSFGF 459
Cdd:cd00834 318 RVFGEHAKkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGF 397
|
....*....
gi 1269947445 460 GGHNSVVAF 468
Cdd:cd00834 398 GGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
61-471 |
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: 607.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 61 KRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKFPTRFAGQIRGFNSEGYIDGKNDRRLDDCLRYCIVAGK 140
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 141 KALEDADLGGDKLSKidmERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIELGLMGPNYSI 220
Cdd:COG0304 81 EALADAGLDLDEVDP---DRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 221 STACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLI 300
Cdd:COG0304 158 STACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 301 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEINAIK 380
Cdd:COG0304 238 LEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 381 KVFKNTLD-IKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVANEKQQHEVNVAISNSFGF 459
Cdd:COG0304 318 RVFGDHAYkVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGF 397
|
410
....*....|..
gi 1269947445 460 GGHNSVVAFSAF 471
Cdd:COG0304 398 GGHNASLVFKRY 409
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
61-468 |
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: 595.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 61 KRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKFPTRFAGQIRGFNSEGYIDGKNDRRLDDCLRYCIVAGK 140
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 141 KALEDADLggdKLSKIDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIELGLMGPNYSI 220
Cdd:TIGR03150 81 EAVEDSGL---DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 221 STACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLI 300
Cdd:TIGR03150 158 VTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 301 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEINAIK 380
Cdd:TIGR03150 238 LEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 381 KVFKN-TLDIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVANEKQQHEVNVAISNSFGF 459
Cdd:TIGR03150 318 KVFGDhAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGF 397
|
....*....
gi 1269947445 460 GGHNSVVAF 468
Cdd:TIGR03150 398 GGTNASLVF 406
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
14-472 |
0e+00 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 593.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 14 LNPLLKPNPNPHFPNVSRLPPRPTKKFSSITASSPT--VSAPKREKDPKKRVVITGMGLVSVFGNDVDAYYDKLLAGESG 91
Cdd:PLN02787 80 LSSLFGSNSVSLNRNQRRRNRAARSGKAMAVAVQPEkeVETKKKPLTKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 92 IGPIDRFDASKFPTRFAGQIRGFNSEGYIDGKNDRRLDDCLRYCIVAGKKALEDADLGGDKLSKIDMERAGVLVGTGMGG 171
Cdd:PLN02787 160 ISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAGKKALADGGITEDVMKELDKTKCGVLIGSAMGG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 172 LTVFSDGVQNLiEKGYRKISPFFIPYAITNMASALLAIELGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGT 251
Cdd:PLN02787 240 MKVFNDAIEAL-RISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGS 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 252 EAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMT 331
Cdd:PLN02787 319 DAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMT 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 332 DPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEINAIKKVFKNTLDIKINATKSMIGHCLGAAGGLEAI 411
Cdd:PLN02787 399 EPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPELRVNSTKSMIGHLLGAAGAVEAI 478
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1269947445 412 ATVKAITTGWLHPSINQFNPEPSVDFDT-VANEKQQHEVNVAISNSFGFGGHNSVVAFSAFK 472
Cdd:PLN02787 479 ATVQAIRTGWVHPNINLENPESGVDTKVlVGPKKERLDIKVALSNSFGFGGHNSSILFAPYK 540
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
59-473 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 580.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 59 PKKRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKFPTRFAGQIR--------GFNSEGYIDGKNDRRLDD 130
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlaedaeaGFDPDRYLDPKDQRKMDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 131 CLRYCIVAGKKALEDADLGGDKLSkiDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIE 210
Cdd:PRK06333 82 FILFAMAAAKEALAQAGWDPDTLE--DRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 211 LGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTASRPWDKDRDG 289
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 290 FVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTL 369
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 370 AGDLAEINAIKKVFKNTLDIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVD-FDTVANEKQQHE 448
Cdd:PRK06333 320 VGDLGEVAAIKKVFGHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
|
410 420
....*....|....*....|....*
gi 1269947445 449 VNVAISNSFGFGGHNSVVAFSAFKP 473
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRRWEP 424
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
60-468 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 580.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 60 KKRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKFPTRFAGQIRGFNSEGYIDGKNDRRLDDCLRYCIVAG 139
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 140 KKALEDADLggdKLSKIDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIELGLMGPNYS 219
Cdd:PRK07314 81 KQAVEDAGL---EITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 220 ISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVL 299
Cdd:PRK07314 158 IVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 300 IMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEINAI 379
Cdd:PRK07314 238 VLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 380 KKVFKNTL-DIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVANEKQQHEVNVAISNSFG 458
Cdd:PRK07314 318 KRVFGEHAyKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFG 397
|
410
....*....|
gi 1269947445 459 FGGHNSVVAF 468
Cdd:PRK07314 398 FGGTNASLVF 407
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
70-471 |
5.78e-146 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 423.72 E-value: 5.78e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 70 LVSVFGNDVDAYYDKLLAGESGIGPIDRFDA----------------SKFPTRFAGQIRG--FNSEGYIDGKNDrrlDDC 131
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDQseFDPSDFAPTKRE---SRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 132 LRYCIVAGKKALEDADLggDKLSKIDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIEL 211
Cdd:PTZ00050 78 THFAMAAAREALADAKL--DILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 212 GLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTASRPWDKDRDGF 290
Cdd:PTZ00050 156 KLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 291 VMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAG-VSPEEVNYINAHATSTL 369
Cdd:PTZ00050 236 VMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 370 AGDLAEINAIKKVFKNTLDIK--INATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVANEKQQH 447
Cdd:PTZ00050 316 IGDKIELKAIKKVFGDSGAPKlyVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHP 395
|
410 420
....*....|....*....|....*.
gi 1269947445 448 EVNV--AISNSFGFGGHNSVVAFSAF 471
Cdd:PTZ00050 396 LQSIdaVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
60-471 |
1.13e-139 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 407.47 E-value: 1.13e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 60 KKRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKFPTRFAGQIRGFNSEGYIDGKNDRRLDDCLRYCIVAG 139
Cdd:PRK08722 3 KRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 140 KKALEDADLggdKLSKIDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIELGLMGPNYS 219
Cdd:PRK08722 83 IQALDDSGL---EVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 220 ISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVL 299
Cdd:PRK08722 160 ISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 300 IMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEINAI 379
Cdd:PRK08722 240 VLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 380 KKVF--KNTLDIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVANEKQQHE-VNVAISNS 456
Cdd:PRK08722 320 KRALgeAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNS 399
|
410
....*....|....*
gi 1269947445 457 FGFGGHNSVVAFSAF 471
Cdd:PRK08722 400 FGFGGTNGSLIFKKM 414
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
61-469 |
8.34e-136 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 397.18 E-value: 8.34e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 61 KRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKFPTRFAGQIRGFNSEGYIDGKNDRRLDDCLRYCIVAGK 140
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 141 KALEDADLGGDKlskIDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIELGLMGPNYSI 220
Cdd:PRK08439 82 EAMKDAGFLPEE---LDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 221 STACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLI 300
Cdd:PRK08439 159 VTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 301 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADglGVSSCIERCLEDAGVSpeEVNYINAHATSTLAGDLAEINAIK 380
Cdd:PRK08439 239 LEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNP--KIDYINAHGTSTPYNDKNETAALK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 381 KVFKNTLDI-KINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVANEKQQHEVNVAISNSFGF 459
Cdd:PRK08439 315 ELFGSKEKVpPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGF 394
|
410
....*....|
gi 1269947445 460 GGHNSVVAFS 469
Cdd:PRK08439 395 GGTNGVVIFK 404
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
59-470 |
8.30e-118 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 352.56 E-value: 8.30e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 59 PKKRVVITGMGLVSVFGNDVDAYYDKLLAGESGI--------------GPIDRFDASKFPTRFAGQI-RG-----FNSEG 118
Cdd:PLN02836 4 PTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVraltqddlkmksedEETQLYTLDQLPSRVAALVpRGtgpgdFDEEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 119 YIdgkNDRRLDDCLRYCIVAGKKALEDADLG-GDKLSKidmERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPY 197
Cdd:PLN02836 84 WL---NSRSSSRFIGYALCAADEALSDARWLpSEDEAK---ERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 198 AITNMASALLAIELGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQR-NDDP 276
Cdd:PLN02836 158 ILINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 277 QTASRPWDKDRDGFVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPE 356
Cdd:PLN02836 238 TEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 357 EVNYINAHATSTLAGDLAEINAIKKVFKN---TLDIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEP 433
Cdd:PLN02836 318 QVDYVNAHATSTPLGDAVEARAIKTVFSEhatSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDP 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 1269947445 434 SVD--FDTVANEKQQhEVNVAISNSFGFGGHNSVVAFSA 470
Cdd:PLN02836 398 IFDdgFVPLTASKAM-LIRAALSNSFGFGGTNASLLFTS 435
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
63-471 |
2.45e-97 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 299.34 E-value: 2.45e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 63 VVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKF--PTRFAGQIRGfNSEGYIDGKNDRRLDDCLRYCIVAGK 140
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEFdlPVRIGGHLLE-EFDHQLTRVELRRMSYLQRMSTVLGR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 141 KALEDADLggdklSKIDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIELGLMGPNYSI 220
Cdd:PRK07910 93 RVWENAGS-----PEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 221 STACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRA-LSQRNDDPQTASRPWDKDRDGFVMGEGAGVL 299
Cdd:PRK07910 168 VSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGALM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 300 IMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEINAI 379
Cdd:PRK07910 248 VIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 380 KKVFKNTlDIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVANEKQQHEVNVAISNSFGF 459
Cdd:PRK07910 328 NNALGGH-RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGF 406
|
410
....*....|..
gi 1269947445 460 GGHNSVVAFSAF 471
Cdd:PRK07910 407 GGHNVALAFGRY 418
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
61-472 |
4.30e-92 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 285.41 E-value: 4.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 61 KRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKFPTRFAGQIRgFNSEGYIDGKNDRRLDDCLRYCIVAGK 140
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 141 KALEDADLGGDKLSKidmERAGVLVGTGmGGLTVF----SDGVQNliEKGYRKISPFFIPYAITNMASALLAIELGLMGP 216
Cdd:PRK07967 81 QAIADAGLSEEQVSN---PRTGLIAGSG-GGSTRNqveaADAMRG--PRGPKRVGPYAVTKAMASTVSACLATPFKIKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 217 NYSISTACATSNYCFYNAANHIRRGEAELMIAGGTE------AAIipiglggFVACRALS-QRNDDPQTASRPWDKDRDG 289
Cdd:PRK07967 155 NYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEeldwemSCL-------FDAMGALStKYNDTPEKASRAYDANRDG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 290 FVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGlgvsscIERCLEDA--GVSpEEVNYINAHATS 367
Cdd:PRK07967 228 FVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEG------AVRCMQMAlaTVD-TPIDYINTHGTS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 368 TLAGDLAEINAIKKVFKNTLDiKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSV-DFDTVANEKQQ 446
Cdd:PRK07967 301 TPVGDVKELGAIREVFGDKSP-AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVTETTDN 379
|
410 420
....*....|....*....|....*.
gi 1269947445 447 HEVNVAISNSFGFGGHNSVVAFSAFK 472
Cdd:PRK07967 380 AELTTVMSNSFGFGGTNATLVFRRYK 405
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
61-468 |
1.35e-85 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 268.39 E-value: 1.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 61 KRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDasKFP---TRFAGQIRGFNSEGYIDGKNDRRLDDCLRYCIV 137
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWD--RYDglnTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 138 AGKKALEDADLGGDKLskIDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIELGLMGPN 217
Cdd:PRK09116 80 ASELALEDAGLLGDPI--LTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 218 YSISTACATSNYCFYNAANHIRRGEAELMIAGG------TEAAIipiglggFVACRALSQRNDDPQTASRPWDKDRDGFV 291
Cdd:PRK09116 158 IPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGaeelcpTEAAV-------FDTLFATSTRNDAPELTPRPFDANRDGLV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 292 MGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVssCIERCLEDAGVSPEEVNYINAHATSTLAG 371
Cdd:PRK09116 231 IGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQI--AMELALKDAGLAPEDIGYVNAHGTATDRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 372 DLAEINAIKKVFKNTLdiKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSV-DFDTVANEKQQHEVN 450
Cdd:PRK09116 309 DIAESQATAAVFGARM--PISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTE 386
|
410
....*....|....*...
gi 1269947445 451 VAISNSFGFGGHNSVVAF 468
Cdd:PRK09116 387 YVMSNNFAFGGINTSLIF 404
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
159-466 |
3.36e-84 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 262.74 E-value: 3.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 159 ERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASALLAIELGLMGPNYSISTACATSNYCFYNAANHI 238
Cdd:PRK14691 26 ERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 239 RRGEAELMIAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTASRPWDKDRDGFVMGEGAGVLIMESLEHAMKRGAPIIAE 317
Cdd:PRK14691 106 RNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 318 YLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEINAIKKVFKNTLDIKINATKSM 397
Cdd:PRK14691 186 IVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNALAITSTKSA 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 398 IGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVD-FDTVANEKQQHEVNVAISNSFGFGGHNSVV 466
Cdd:PRK14691 266 TGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASI 335
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
57-470 |
9.79e-84 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 264.57 E-value: 9.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 57 KDPKKR--VVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKFPTRFAGQIRGFNSEGYIDGKNDRRLDDclry 134
Cdd:PRK06501 5 RDHLGRpiVAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDFLPESPFGASALSEALAR---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 135 ciVAGKKALEDADLG-GD-------KLSKIDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAITNMASAL 206
Cdd:PRK06501 81 --LAAEEALAQAGIGkGDfpgplflAAPPVELEWPARFALAAAVGDNDAPSYDRLLRAARGGRFDALHERFQFGSIADRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 207 lAIELGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKD 286
Cdd:PRK06501 159 -ADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 287 RDGFVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHAT 366
Cdd:PRK06501 238 RDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 367 STLAGDLAEINAIKKVFKNTL-DIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVANEKQ 445
Cdd:PRK06501 318 STPENDKMEYLGLSAVFGERLaSIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVAR 397
|
410 420
....*....|....*....|....*
gi 1269947445 446 QHEVNVAISNSFGFGGHNSVVAFSA 470
Cdd:PRK06501 398 DARVTAVLSNSFGFGGQNASLVLTA 422
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
62-466 |
4.73e-83 |
|
"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: 261.99 E-value: 4.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 62 RVVITGMGLVS---VFGNDVDAYYDKLLAGESGIGPIDRFDaSKFPTRFAGQIRGFNSEGYiDGKNDRRLDDCLRYCIVA 138
Cdd:cd00828 2 RVVITGIGVVSphgEGCDEVEEFWEALREGRSGIAPVARLK-SRFDRGVAGQIPTGDIPGW-DAKRTGIVDRTTLLALVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 139 GKKALEDADLggDKLSKIDMERAGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPFFIPYAitNMASALLAIELGLM-GPN 217
Cdd:cd00828 80 TEEALADAGI--TDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLSP--NTVAGWVNILLLSShGPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 218 YSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAaIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAG 297
Cdd:cd00828 156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 298 VLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPrADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEIN 377
Cdd:cd00828 235 VLVLERAELALARGAPIYGRVAGTASTTDGAGRSVP-AGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 378 AIKKVFKNTLD-IKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSIN--QFNPEPSVDFDTVANEKQQHEVNVAIS 454
Cdd:cd00828 314 AIAEVAGALGApLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANldDVDPDVEHLSVVGLSRDLNLKVRAALV 393
|
410
....*....|..
gi 1269947445 455 NSFGFGGHNSVV 466
Cdd:cd00828 394 NAFGFGGSNAAL 405
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
60-466 |
1.62e-75 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 242.63 E-value: 1.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 60 KKRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASK-------FPTRFAG-QIRGFNSEGYIDGKNDRRLDDC 131
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVpddagagLASAFIGaELDSLALPERLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 132 LRYCIVAGKKALEDADLGGdklskIDMERAGVLVGtgmgGLTVFSDGVQNLIEKgYRKISPFFIP-YAITNMASALLAI- 209
Cdd:PRK07103 81 AQAALAAAREAWRDAALGP-----VDPDRIGLVVG----GSNLQQREQALVHET-YRDRPAFLRPsYGLSFMDTDLVGLc 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 210 --ELGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRAL-SQRN-DDPQTASRPWDK 285
Cdd:PRK07103 151 seQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMgSDRFaDEPEAACRPFDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 286 DRDGFVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPraDGLGVSSCIERCLEDAGVSPEEVNYINAHA 365
Cdd:PRK07103 231 DRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPHG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 366 TSTLAGDLAEINAIkkvFKNTLD-IKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNP-EPSVDFdtVANE 443
Cdd:PRK07103 309 TGSPLGDETELAAL---FASGLAhAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERFRW--VGST 383
|
410 420
....*....|....*....|...
gi 1269947445 444 KQQHEVNVAISNSFGFGGHNSVV 466
Cdd:PRK07103 384 AESARIRYALSLSFGFGGINTAL 406
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
62-469 |
5.07e-68 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 222.23 E-value: 5.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 62 RVVITGMGLVSVFGnDVDAYYDKLLAGESGIGPIDRFdaSKFPTRFAGQIrgfnsegyidGKNDRRLDDCLRYCIVAgkk 141
Cdd:PRK05952 3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQPF--PELPPLPLGLI----------GNQPSSLEDLTKTVVTA--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 142 ALEDADLggdklsKIDMERAGVLVGTgmggltvfSDGVQNLIEKGYRKISPFFIPYAIT-----------NMASALLAIE 210
Cdd:PRK05952 67 ALKDAGL------TPPLTDCGVVIGS--------SRGCQGQWEKLARQMYQGDDSPDEEldlenwldtlpHQAAIAAARQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 211 LGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQrnddpqTASRPWDKDRDGF 290
Cdd:PRK05952 133 IGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREGL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 291 VMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLA 370
Cdd:PRK05952 207 VLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 371 GDLAEINAIKKVFKNtlDIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVAnekQQHEVN 450
Cdd:PRK05952 287 NDQREANLIQALFPH--RVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNFVRQA---QQSPLQ 361
|
410
....*....|....*....
gi 1269947445 451 VAISNSFGFGGHNSVVAFS 469
Cdd:PRK05952 362 NVLCLSFGFGGQNAAIALG 380
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
62-464 |
4.30e-65 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 215.88 E-value: 4.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 62 RVVITGMGLVsvF--GNDVDAYYDKLLAGESGIGPI--DRFDASKFPTRFAGQIRGFNSE-GYIDGKND----------- 125
Cdd:cd00833 2 PIAIVGMACR--FpgAADPDEFWENLLEGRDAISEIpeDRWDADGYYPDPGKPGKTYTRRgGFLDDVDAfdaaffgispr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 126 --RRLDDCLRYCIVAGKKALEDADLGGDKLSKidmERAGVLVGtgmggltVFSDGVQNLIEKGYRKISPFFIPYAITNMA 203
Cdd:cd00833 80 eaEAMDPQQRLLLEVAWEALEDAGYSPESLAG---SRTGVFVG-------ASSSDYLELLARDPDEIDAYAATGTSRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 204 SALLAIELGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSqrnDDPQtaSRPW 283
Cdd:cd00833 150 ANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS---PDGR--CRPF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 284 DKDRDGFVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAY--HMTDPRADGLgvSSCIERCLEDAGVSPEEVNYI 361
Cdd:cd00833 225 DADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEAQ--AALIRRAYARAGVDPSDIDYV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 362 NAHATSTLAGDLAEINAIKKVFKNTLD----IKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDF 437
Cdd:cd00833 303 EAHGTGTPLGDPIEVEALAKVFGGSRSadqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDF 382
|
410 420 430
....*....|....*....|....*....|....*
gi 1269947445 438 D----TVANEKQQHEVNVAIS----NSFGFGGHNS 464
Cdd:cd00833 383 EesplRVPTEARPWPAPAGPRragvSSFGFGGTNA 417
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
61-307 |
9.55e-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: 206.72 E-value: 9.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 61 KRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPI--DRFDASKF---PTRFAGQIRG--------FNSEGYIDGKNDR- 126
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTkwgglddiFDFDPLFFGISPRe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 127 --RLDDCLRYCIVAGKKALEDADLGGDKLSKidmERAGVLVGTGMGGLtvfsDGVQNLIEKG-YRKISPFFIPYaITNMA 203
Cdd:pfam00109 81 aeRMDPQQRLLLEAAWEALEDAGITPDSLDG---SRTGVFIGSGIGDY----AALLLLDEDGgPRRGSPFAVGT-MPSVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 204 SALLAIELGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSQrnDDPQTASRPW 283
Cdd:pfam00109 153 AGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPF 230
|
250 260
....*....|....*....|....
gi 1269947445 284 DkdrDGFVMGEGAGVLIMESLEHA 307
Cdd:pfam00109 231 A---DGFVRGEGVGAVVLKRLSDA 251
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
61-466 |
2.69e-61 |
|
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: 205.29 E-value: 2.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 61 KRVVITGMGLVSVFGNDVDAYYDKLLAGESGIGPIDRFDASKFPTRFAGQIRGFNSEGYIDGKNDRRLDDCLRYCIVAGK 140
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 141 KALEDADLGGDKLSKIDMeraGVLVGTGMGGLTVFSDGVQNLIEKGYRKISPF-----FipYAITnmaSALLAIELGLMG 215
Cdd:cd00832 81 WALADAGVDPAALPPYDM---GVVTASAAGGFEFGQRELQKLWSKGPRHVSAYqsfawF--YAVN---TGQISIRHGMRG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 216 PNYSISTACATSNYCFYNAANHIRRGeAELMIAGGTEAAIIPIGLGGFVACRALSqRNDDPQTASRPWDKDRDGFVMGEG 295
Cdd:cd00832 153 PSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLS-TSDDPARAYLPFDAAAAGYVPGEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 296 AGVLIMESLEHAMKRGAPIIAEYLGGAVNcdayhMTDPRADGL--GVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDL 373
Cdd:cd00832 231 GAILVLEDAAAARERGARVYGEIAGYAAT-----FDPPPGSGRppGLARAIRLALADAGLTPEDVDVVFADAAGVPELDR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 374 AEINAIKKVFkNTLDIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPSVDFDTVANEKQQHEVNVAI 453
Cdd:cd00832 306 AEAAALAAVF-GPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTAL 384
|
410
....*....|...
gi 1269947445 454 SNSFGFGGHNSVV 466
Cdd:cd00832 385 VLARGRGGFNSAL 397
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
133-467 |
8.53e-53 |
|
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: 180.91 E-value: 8.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 133 RYCIVAGKKALEDADLGGDKLSKidmERAGVLVGTGMGGltvfsDGVQNLIEKGYRKISPFFIPYAITNMASALLAIELG 212
Cdd:cd00825 13 ILGFEAAERAIADAGLSREYQKN---PIVGVVVGTGGGS-----PRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 213 LMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSqrnddPQTASRPWDKDRDGFVM 292
Cdd:cd00825 85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 293 GEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGD 372
Cdd:cd00825 160 GDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 373 LAEINAIKKVFKNTlDIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPEPsvDFDTVANEKQQHEVNVA 452
Cdd:cd00825 240 VKELKLLRSEFGDK-SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTA 316
|
330
....*....|....*
gi 1269947445 453 ISNSFGFGGHNSVVA 467
Cdd:cd00825 317 LLNGFGLGGTNATLV 331
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
63-463 |
1.68e-48 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 171.18 E-value: 1.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 63 VVITGMGLVSVFGNDVDAYYDKLLAGESG---------------IGPIDRFDASKFPTRFAGQirgfnsegyiDGKNDRR 127
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRAGRASgmrpcdfwlvdlptwVGEVVGVELPALPAALAAF----------DCRNNRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 128 LDDCLRYCIVAGKKALedADLGGDklskidmeRAGVLVGTGMGGLtvfSDGvqnliEKGYRKISPF---FIP---YAITN 201
Cdd:PRK09185 74 ALLALQQIEPAVEAAI--ARYGAD--------RIGVVLGTSTSGI---LEG-----ELAYRRRDPAhgaLPAdyhYAQQE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 202 M--ASALLAIELGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGG-------TeaaiipigLGGFVACRALSQr 272
Cdd:PRK09185 136 LgsLADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGvdslcrlT--------LNGFNSLESLSP- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 273 nddpqTASRPWDKDRDGFVMGEGAGVLIMEslehamkRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAG 352
Cdd:PRK09185 207 -----QPCRPFSANRDGINIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 353 VSPEEVNYINAHATSTLAGDLAEINAIKKVFKNTLdiKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSINQFNPE 432
Cdd:PRK09185 275 LAPADIGYINLHGTATPLNDAMESRAVAAVFGDGV--PCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPD 352
|
410 420 430
....*....|....*....|....*....|.
gi 1269947445 433 PSVDFDTVANEKQQHEVNVAISNSFGFGGHN 463
Cdd:PRK09185 353 PALPPLYLVENAQALAIRYVLSNSFAFGGNN 383
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
63-463 |
2.98e-45 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 169.67 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 63 VVITGMGlvSVF--GNDVDAYYDKLLAGESGIGPI--DRFDASKF-----------PTRFAG---QIRGFNSEGY-IDGK 123
Cdd:COG3321 6 IAIIGMA--CRFpgADDPEEFWRNLRAGRDAITEVpaDRWDADAYydpdpdapgktYVRWGGfldDVDEFDALFFgISPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 124 NDRRLDDCLRYCIVAGKKALEDADLGGDKLSKidmERAGVLVGTGMGGLTVFSDGVQNLIEkgyrkispffiPYAIT--- 200
Cdd:COG3321 84 EAEAMDPQQRLLLEVAWEALEDAGYDPESLAG---SRTGVFVGASSNDYALLLLADPEAID-----------AYALTgna 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 201 -NMASALLAIELGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTeAAIIPIGLG-GFVACRALSqrnddPQT 278
Cdd:COG3321 150 kSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGV-NLMLTPESFiLFSKGGMLS-----PDG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 279 ASRPWDKDRDGFVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCD-AYH-MTDPRadGLGVSSCIERCLEDAGVSPE 356
Cdd:COG3321 224 RCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgRSNgLTAPN--GPAQAAVIRRALADAGVDPA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 357 EVNYINAHATSTLAGDLAEINAIKKVFKNTLDIK----INATKSMIGHCLGAAG--GLeaIATVKAITTGWLHPSINQFN 430
Cdd:COG3321 302 TVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPADqpcaIGSVKSNIGHLEAAAGvaGL--IKAVLALRHGVLPPTLHFET 379
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1269947445 431 PEPSVDFDT----VANE-----KQQHEVNVAISnSFGFGGHN 463
Cdd:COG3321 380 PNPHIDFENspfyVNTElrpwpAGGGPRRAGVS-SFGFGGTN 420
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
316-427 |
1.46e-41 |
|
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: 143.86 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 316 AEYLGGAVNCDAYHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEINAIKKVF---KNTLDIKIN 392
Cdd:pfam02801 2 AVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFgsgARKQPLAIG 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1269947445 393 ATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSIN 427
Cdd:pfam02801 82 SVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLN 116
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
136-473 |
5.81e-27 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 115.10 E-value: 5.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 136 IVAGKKALEDADLGGDklskIDMERAGVLVGTGMG-----GLT----------VF-SDGVQN-----LIEK------GYR 188
Cdd:TIGR02813 98 LVVAKEVLNDAGLPDG----YDRDKIGITLGVGGGqkqssSLNarlqypvlkkVFkASGVEDedsemLIKKfqdqyiHWE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 189 KISpffIPYAITNMASALLAIELGLMGPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRA 268
Cdd:TIGR02813 174 ENS---FPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 269 LSQRNDdpqtaSRPWDKDRDGFVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAYHMT--DPRADGLgvSSCIER 346
Cdd:TIGR02813 251 FTTNED-----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSiyAPRPEGQ--AKALKR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 347 CLEDAGVSPEEVNYINAHATSTLAGDLAEINAIKKVFKNTLD----IKINATKSMIGHCLGAAGGLEAIATVKAITTGWL 422
Cdd:TIGR02813 324 AYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVL 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1269947445 423 HPSINQFNPEPSVDFD-------TVANEKQQHEVNV---AISNSFGFGGHNSVVAFSAFKP 473
Cdd:TIGR02813 404 PPTINVDQPNPKLDIEnspfylnTETRPWMQREDGTprrAGISSFGFGGTNFHMVLEEYSP 464
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
203-466 |
1.24e-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: 107.92 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 203 ASALLAIELGLM-GPNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAaiipiglggfvacralsqrnddpqtasr 281
Cdd:cd00327 46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 282 pwdkdrdgFVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCD-AYHMTDPRADGLgvSSCIERCLEDAGVSPEEVNY 360
Cdd:cd00327 98 --------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVSGEGL--ARAARKALEGAGLTPSDIDY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 361 INAHATSTLAGDLAEINAIKKVFKNTlDIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPSinqfnpepsvdfdtv 440
Cdd:cd00327 168 VEAHGTGTPIGDAVELALGLDPDGVR-SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT--------------- 231
|
250 260
....*....|....*....|....*.
gi 1269947445 441 anekqQHEVNVAISNSFGFGGHNSVV 466
Cdd:cd00327 232 -----PREPRTVLLLGFGLGGTNAAV 252
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
212-463 |
1.53e-24 |
|
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: 103.18 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 212 GLMGPNYSIS--TACATSNYCFYNAANHIRRGEAELMIAGGTEAAIIPIGLGGFVACRALSqrnddPQTASRPWDKDRDG 289
Cdd:smart00825 83 GVSSSDYSVTvdTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 290 FVMGEGAGVLIMESLEHAMKRGAPIIAEYLGGAVNCDAyhmtdpRADGLGVSSCIERCLedagvspeevnyinahatstl 369
Cdd:smart00825 158 YVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDG------RSNGITAPSGPAQLL--------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 370 agdlaeinaikkvfkntldikINATKSMIGHCLGAAG--GLeaIATVKAITTGWLHPSINQFNPEPSVDFDT----VANE 443
Cdd:smart00825 211 ---------------------IGSVKSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPHIDLEEsplrVPTE 267
|
250 260
....*....|....*....|....*
gi 1269947445 444 KQQHEVN-----VAIsNSFGFGGHN 463
Cdd:smart00825 268 LTPWPPPgrprrAGV-SSFGFGGTN 291
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
63-443 |
6.79e-10 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 60.74 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 63 VVITGMGLVSVFGNDVDAYYDKLLAGEsgigPIDRFDASKF---------PTRFAGQI--RGfnsegyidgkNDRRLDDC 131
Cdd:PRK06519 8 VVITGIGLVSSLGEGLDAHWNALSAGR----PQPNVDTETFapypvhplpEIDWSQQIpkRG----------DQRQMETW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 132 LRYCIVAGKKALEDADLGGDK--LSKIDMeragvLVGTGmGG---LTVfsDGvqnLIEKGYRKispffipyaiTNMASAL 206
Cdd:PRK06519 74 QRLGTYAAGLALDDAGIKGNEelLSTMDM-----IVAAG-GGerdIAV--DT---AILNEARK----------RNDRGVL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 207 LAIEL--------------GLMGPNYSISTACATSNYCFY-----------NAANHIRRGEAELMIAGGTEAA-----II 256
Cdd:PRK06519 133 LNERLmtelrptlflaqlsNLLAGNISIVHKVTGSSRTFMgeesagvsaieIAFARIASGQSDHALVGGAYNAerpdmLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 257 PIGLGGFVA---CRALSQRNDDpqtasrpwdkDRDGFVMGEGAGVLIMESLEHAMKRGAPIIAEyLGGAVNCDAyhmtdP 333
Cdd:PRK06519 213 LYELGGLLLkggWAPVWSRGGE----------DGGGFILGSGGAFLVLESREHAEARGARPYAR-ISGVESDRA-----R 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 334 RADGlGVSSCIERCLEDAGVSPEEVNYINAhatSTLAGDLAEinAIKKVFKNTLDIKINATKSMIGHC------LGAAgg 407
Cdd:PRK06519 277 RAPG-DLEASLERLLKPAGGLAAPTAVISG---ATGAHPATA--EEKAALEAALAGPVRGIGTLFGHTmeaqfpLGLA-- 348
|
410 420 430
....*....|....*....|....*....|....*.
gi 1269947445 408 LEAIatvkAITTGWLHPSinqFNPEPSVDFDTVANE 443
Cdd:PRK06519 349 LAAL----SVSKGALFPP---FDASGEKPMSGAARE 377
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
218-260 |
1.27e-04 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 44.20 E-value: 1.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1269947445 218 YSISTACATSNYCFYNAANHIRRGEAELMIAGGTE-AAIIPIGL 260
Cdd:PRK08963 85 YSVSRACATSFQAVANVAESIMAGTIDIGIAGGADsSSVLPIGV 128
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
216-296 |
2.25e-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: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 216 PNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAA-IIPIGLGGFVACRALSQRNDDPQTASRPWDkDRDGFVMGE 294
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMsRAPMLLPKARWGYRMNAKLVDPMINPGLTD-PYTGLSMGE 158
|
..
gi 1269947445 295 GA 296
Cdd:COG0183 159 TA 160
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
135-361 |
3.18e-03 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 39.45 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 135 CIVAGKKALEDAdlgGDKLSKIDMeragVLVGTgmggltvfsdgvqnliekgyrkISPFFIPYAItnmaSALLAIELGLM 214
Cdd:cd00830 54 AVEAAKKALEDA---GIDADDIDL----IIVAT----------------------STPDYLFPAT----ACLVQARLGAK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 215 G-PNYSISTACATSNYCFYNAANHIRRGEAE--LMIAGGTeaaiipiglggfvacraLSQRNDdpqtasrpWDkDRDG-F 290
Cdd:cd00830 101 NaAAFDINAACSGFLYGLSTAAGLIRSGGAKnvLVVGAET-----------------LSRILD--------WT-DRSTaV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 291 VMGEGAGVLIMESLEHAMKrgapIIAEYLG------GAVNCDAYHMTDPRADGLG-------------------VSSCIE 345
Cdd:cd00830 155 LFGDGAGAVVLEATEEDPG----ILDSVLGsdgsgaDLLTIPAGGSRSPFEDAEGgdpylvmdgrevfkfavrlMPESIE 230
|
250
....*....|....*.
gi 1269947445 346 RCLEDAGVSPEEVNYI 361
Cdd:cd00830 231 EALEKAGLTPDDIDWF 246
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
294-406 |
4.08e-03 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 39.36 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 294 EGAGVLIMESLEHAMKRGAPIIAEYLG-GAVNCdayhmtDPRADGLGVSSCIERCLEDAGVSPEEVnyinahatstlagD 372
Cdd:PLN02287 292 DGAGAVLLMKRSVAMQKGLPILGVFRSfAAVGV------DPAVMGIGPAVAIPAAVKAAGLELDDI-------------D 352
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1269947445 373 LAEIN---------AIKKVFKNTLDIKINATKSMIGHCLGAAG 406
Cdd:PLN02287 353 LFEINeafasqfvyCCKKLGLDPEKVNVNGGAIALGHPLGATG 395
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
292-406 |
5.60e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 39.10 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 292 MGEGAGVLIMESLEHAMKRGAPI---IAEYLGGAVncdayhmtDPRADGLGVSSCIERCLEDAGVSPEEVNYINAH---- 364
Cdd:PRK05656 250 LNDGAAAVLLMSAAKAKALGLPVlakIAAYANAGV--------DPAIMGIGPVSATRRCLDKAGWSLAELDLIEANeafa 321
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1269947445 365 ATSTLAGDLAEINAIKkvfkntldIKINATKSMIGHCLGAAG 406
Cdd:PRK05656 322 AQSLAVGKELGWDAAK--------VNVNGGAIALGHPIGASG 355
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
216-296 |
7.71e-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: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 216 PNYSISTACATSNYCFYNAANHIRRGEAELMIAGGTEAA-IIPIGLGGfvacRALSQRNDDPQTASRPWDKDRDGFV--- 291
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMsRAPYLLPK----ARRGGRLGLNTLDGMLDDGLTDPFTgls 151
|
....*
gi 1269947445 292 MGEGA 296
Cdd:cd00751 152 MGITA 156
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
296-407 |
9.59e-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: 38.23 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269947445 296 AGVLIMeSLEHAMKRGAPIIAEYLGGAVncdayHMTDPRADGLGVSSCIERCLEDAGVSPEEVnyinahatstlagDLAE 375
Cdd:cd00751 249 AAVLLM-SEEKAKELGLKPLARIVGYAV-----AGVDPAIMGIGPVPAIPKALKRAGLTLDDI-------------DLIE 309
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1269947445 376 IN----AIKKVFKNTLDI---KINATKSMI--GHCLGAAGG 407
Cdd:cd00751 310 INeafaAQALACLKELGLdpeKVNVNGGAIalGHPLGASGA 350
|
|
| |
