|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-341 |
1.03e-157 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 447.70 E-value: 1.03e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 1 MARFAQYAMVASEEALKDSEWFPKkEEDlestvwRIRTlstralltsyqGVYMGSGIGSLDDVYNTTVAY-EKG------ 73
Cdd:PRK07314 69 MDRFIQYGIAAAKQAVEDAGLEIT-EEN------ADRI-----------GVIIGSGIGGLETIEEQHITLlEKGprrvsp 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 74 ----------------------GPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATD 131
Cdd:PRK07314 131 ffvpmaiinmaaghvsirygakGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 132 fNDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHA 211
Cdd:PRK07314 211 -NDDPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 212 GLKPSDVDYVNAHATSTPLGDAAENRAIKElLLGEdgktAASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPT 291
Cdd:PRK07314 290 GINPEDIDYINAHGTSTPAGDKAETQAIKR-VFGE----HAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPT 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 189207418 292 LNLNNPGdppEDFDCNYVAKSAQQYDVKVALSNSFGFGGTNASLCFRKVE 341
Cdd:PRK07314 365 INLDNPD---EECDLDYVPNEARERKIDYALSNSFGFGGTNASLVFKRYE 411
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
1-340 |
2.39e-154 |
|
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: 439.15 E-value: 2.39e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 1 MARFAQYAMVASEEALKDSEWfPKKEEDLEstvwriRTlstralltsyqGVYMGSGIGSLDDVYNTTVAY-EKG------ 73
Cdd:COG0304 68 MDRFTQYALAAAREALADAGL-DLDEVDPD------RT-----------GVIIGSGIGGLDTLEEAYRALlEKGprrvsp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 74 ----------------------GPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATD 131
Cdd:COG0304 130 ffvpmmmpnmaaghvsirfglkGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 132 fNDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHA 211
Cdd:COG0304 210 -NDDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 212 GLKPSDVDYVNAHATSTPLGDAAENRAIKElLLGEdgktAASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPT 291
Cdd:COG0304 289 GLSPEDIDYINAHGTSTPLGDAAETKAIKR-VFGD----HAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPT 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 189207418 292 LNLNNPgDPpeDFDCNYVAKSAQQYDVKVALSNSFGFGGTNASLCFRKV 340
Cdd:COG0304 364 INLENP-DP--ECDLDYVPNEAREAKIDYALSNSFGFGGHNASLVFKRY 409
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
1-338 |
7.74e-154 |
|
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: 437.69 E-value: 7.74e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 1 MARFAQYAMVASEEALKDSEWfPKKEEDLEstvwRIrtlstralltsyqGVYMGSGIGSLDDVYNTTVAY-EKG------ 73
Cdd:TIGR03150 68 MDRFIQYALAAAKEAVEDSGL-DIEEEDAE----RV-------------GVIIGSGIGGLETIEEQHIVLlEKGprrvsp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 74 ----------------------GPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATd 131
Cdd:TIGR03150 130 ffipmsiinmaagqisirygakGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALST- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 132 FNDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHA 211
Cdd:TIGR03150 209 RNDDPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 212 GLKPSDVDYVNAHATSTPLGDAAENRAIKElLLGEDgktaASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPT 291
Cdd:TIGR03150 289 GINPEDVDYINAHGTSTPLGDKAETKAIKK-VFGDH----AYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPT 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 189207418 292 LNLNNPGdppEDFDCNYVAKSAQQYDVKVALSNSFGFGGTNASLCFR 338
Cdd:TIGR03150 364 INLDNPD---PECDLDYVPNEAREAKIDYALSNSFGFGGTNASLVFK 407
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
1-337 |
5.89e-151 |
|
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: 430.42 E-value: 5.89e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 1 MARFAQYAMVASEEALKDSEWFPKKEEDlestvWRIrtlstralltsyqGVYMGSGIGSLDDVYNTTVAYEKGGPNHAAT 80
Cdd:cd00834 68 MDRFAQFALAAAEEALADAGLDPEELDP-----ERI-------------GVVIGSGIGGLATIEEAYRALLEKGPRRVSP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 81 TACTTGA-----------------------------HSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATD 131
Cdd:cd00834 130 FFVPMALpnmaagqvairlglrgpnytvstacasgaHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 132 FNDrPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHA 211
Cdd:cd00834 210 NDD-PEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 212 GLKPSDVDYVNAHATSTPLGDAAENRAIKELLLgedgkTAASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPT 291
Cdd:cd00834 289 GLSPEDIDYINAHGTSTPLNDAAESKAIKRVFG-----EHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPT 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 189207418 292 LNLNNPgDPpeDFDCNYVAKSAQQYDVKVALSNSFGFGGTNASLCF 337
Cdd:cd00834 364 INLEEP-DP--ECDLDYVPNEAREAPIRYALSNSFGFGGHNASLVF 406
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2-337 |
4.12e-143 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 411.88 E-value: 4.12e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 2 ARFAQYAMVASEEALKDSEWFPKKEEDLESTvwrirtlstralltsyqGVYMGSGIGSLDDVY----------------- 64
Cdd:PLN02836 91 SRFIGYALCAADEALSDARWLPSEDEAKERT-----------------GVSIGGGIGSITDILeaaqlicekrlrrlspf 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 65 ------------NTTVAYEKGGPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATDF 132
Cdd:PLN02836 154 fvprilinmaagHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 133 NDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHAG 212
Cdd:PLN02836 234 NSCPTEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 213 LKPSDVDYVNAHATSTPLGDAAENRAIKElLLGEDGKTAAskINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTL 292
Cdd:PLN02836 314 LHPNQVDYVNAHATSTPLGDAVEARAIKT-VFSEHATSGG--LAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTL 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 189207418 293 NLNNPgDPPedFDCNYVAKSAQQYD-VKVALSNSFGFGGTNASLCF 337
Cdd:PLN02836 391 NLERP-DPI--FDDGFVPLTASKAMlIRAALSNSFGFGGTNASLLF 433
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-342 |
3.92e-135 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 390.90 E-value: 3.92e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 1 MARFAQYAMVASEEALKDSEWFPKKEEDLESTvwrirtlstralltsyqGVYMGSGIG---SLDDVYNTTVayEKG---- 73
Cdd:PRK06333 79 MDRFILFAMAAAKEALAQAGWDPDTLEDRERT-----------------ATIIGSGVGgfpAIAEAVRTLD--SRGprrl 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 74 ------------------------GPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLA 129
Cdd:PRK06333 140 spftipsfltnmaaghvsirygfkGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 130 TDFNDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALR 209
Cdd:PRK06333 220 TRFNDAPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 210 HAGLKPSDVDYVNAHATSTPLGDAAENRAIKElLLGEDGKTAaskinISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILP 289
Cdd:PRK06333 300 QAGIPPEEVQHLNAHATSTPVGDLGEVAAIKK-VFGHVSGLA-----VSSTKSATGHLLGAAGGVEAIFTILALRDQIAP 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 189207418 290 PTLNLNNPGDPPEDFDcnYVAKSAQQYDVKVALSNSFGFGGTNASLCFRKVEG 342
Cdd:PRK06333 374 PTLNLENPDPAAEGLD--VVANKARPMDMDYALSNGFGFGGVNASILFRRWEP 424
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
3-340 |
5.67e-135 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 390.59 E-value: 5.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 3 RFAQYAMVASEEALKDSEWFPKKEEDLESTvwrirtlstralltsyqGVYMGSGIGSLDDVY-NTTVAYEKG-------- 73
Cdd:PTZ00050 76 RATHFAMAAAREALADAKLDILSEKDQERI-----------------GVNIGSGIGSLADLTdEMKTLYEKGhsrvspyf 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 74 --------------------GPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATDFN 133
Cdd:PTZ00050 139 ipkilgnmaaglvaikhklkGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYN 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 134 DRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHAGL 213
Cdd:PTZ00050 219 DDPQRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 214 KP-SDVDYVNAHATSTPLGDAAENRAIKELLlgedGKTAASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTL 292
Cdd:PTZ00050 299 INiNDVDYVNAHATSTPIGDKIELKAIKKVF----GDSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTI 374
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 189207418 293 NLNNPgDPPEDFDCNYVAKSAQQYDVKVALSNSFGFGGTNASLCFRKV 340
Cdd:PTZ00050 375 NLENP-DAECDLNLVQGKTAHPLQSIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
3-340 |
3.58e-97 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 293.56 E-value: 3.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 3 RFAQYAMVASEEALKDSEwFPKKEEDLESTvwrirtlstralltsyqGVYMGSGIGSLDDV-YNTTVAYEKG-------- 73
Cdd:PRK08439 71 RFIQLGLKAAREAMKDAG-FLPEELDAERF-----------------GVSSASGIGGLPNIeKNSIICFEKGprkispff 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 74 --------------------GPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATdFN 133
Cdd:PRK08439 133 ipsalvnmlggfisiehglkGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALST-RN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 134 DRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDgqGPRLAMKHALRHAGL 213
Cdd:PRK08439 212 DDPKKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 214 KPsdVDYVNAHATSTPLGDAAENRAIKELLlgedgktaASKIN---ISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPP 290
Cdd:PRK08439 290 PK--IDYINAHGTSTPYNDKNETAALKELF--------GSKEKvppVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPP 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 189207418 291 TLNLNNPgDPPEDFDcnYVAKSAQQYDVKVALSNSFGFGGTNASLCFRKV 340
Cdd:PRK08439 360 TINQETP-DPECDLD--YIPNVARKAELNVVMSNSFGFGGTNGVVIFKKV 406
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
1-340 |
9.45e-96 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 290.37 E-value: 9.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 1 MARFAQYAMVASEEALKDSEWfpkkeEDLESTVWRIrtlstralltsyqGVYMGSGIGSLDDVYNTTVAY-EKG------ 73
Cdd:PRK08722 71 MDLFIQYGIAAGIQALDDSGL-----EVTEENAHRI-------------GVAIGSGIGGLGLIEAGHQALvEKGprkvsp 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 74 ----------------------GPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATD 131
Cdd:PRK08722 133 ffvpstivnmiagnlsimrglrGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 132 fNDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHA 211
Cdd:PRK08722 213 -NDEPQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 212 GLKPSDVDYVNAHATSTPLGDAAENRAIKELLlgedGKTAASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPT 291
Cdd:PRK08722 292 GVTGEQIGYVNAHGTSTPAGDVAEIKGIKRAL----GEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPT 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 189207418 292 LNLNnpgDPPEDFDCNYVAKSAQQYD-VKVALSNSFGFGGTNASLCFRKV 340
Cdd:PRK08722 368 INLD---DPEEGLDIDLVPHTARKVEsMEYAICNSFGFGGTNGSLIFKKM 414
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
65-339 |
1.75e-88 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 269.29 E-value: 1.75e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 65 NTTVAYEKGGPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATDFNDRPTESSRPFD 144
Cdd:PRK14691 73 HVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHFNSTPEKASRPFD 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 145 RARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYVNAH 224
Cdd:PRK14691 153 TARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAH 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 225 ATSTPLGDAAENRAIKElLLGEDGKTAaskinISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPgDPPEDf 304
Cdd:PRK14691 233 ATSTPVGDLGEINAIKH-LFGESNALA-----ITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENP-DPAAK- 304
|
250 260 270
....*....|....*....|....*....|....*
gi 189207418 305 DCNYVAKSAQQYDVKVALSNSFGFGGTNASLCFRK 339
Cdd:PRK14691 305 GLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
90-339 |
7.83e-82 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 254.65 E-value: 7.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 90 IGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATDFNDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKN 169
Cdd:PRK07910 178 IAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVIETEEHAKA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 170 RGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYVNAHATSTPLGDAAENRAIKELLLGEDGK 249
Cdd:PRK07910 258 RGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNALGGHRPA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 250 TAASkinisstKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPgDPPEDFDCnyVAKSAQQYDVKVALSNSFGFG 329
Cdd:PRK07910 338 VYAP-------KSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENL-DPEIDLDV--VAGEPRPGNYRYAINNSFGFG 407
|
250
....*....|
gi 189207418 330 GTNASLCFRK 339
Cdd:PRK07910 408 GHNVALAFGR 417
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
89-339 |
2.73e-79 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 246.89 E-value: 2.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 89 SIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATdfndrptESSRPFDRARNGFVIGEGAGVMVLEELEHAK 168
Cdd:PRK05952 152 AIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK-------TGAYPFDRQREGLVLGEGGAILVLESAELAQ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 169 NRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYVNAHATSTPLGDAAENRAIKELLlgedg 248
Cdd:PRK05952 225 KRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALF----- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 249 ktaASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPgdppeDFDCNYVaKSAQQYDVKVALSNSFGF 328
Cdd:PRK05952 300 ---PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEP-----EFDLNFV-RQAQQSPLQNVLCLSFGF 370
|
250
....*....|.
gi 189207418 329 GGTNASLCFRK 339
Cdd:PRK05952 371 GGQNAAIALGK 381
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-342 |
4.92e-77 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 241.88 E-value: 4.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 1 MARFAQYAMVASEEALKDSEWfpkkeedLESTVWRIRTlstralltsyqGVYMGSGIGS-LDDVYNTTVAYEKGGP---- 75
Cdd:PRK07967 68 MGDASAYAYLAMEQAIADAGL-------SEEQVSNPRT-----------GLIAGSGGGStRNQVEAADAMRGPRGPkrvg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 76 -------------------------NHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISgFARARSLAT 130
Cdd:PRK07967 130 pyavtkamastvsaclatpfkikgvNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALST 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 131 DFNDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPreDGQGPRLAMKHALrh 210
Cdd:PRK07967 209 KYNDTPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAP--SGEGAVRCMQMAL-- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 211 AGLKpSDVDYVNAHATSTPLGDAAENRAIKElLLGEdgKTAAskinISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPP 290
Cdd:PRK07967 285 ATVD-TPIDYINTHGTSTPVGDVKELGAIRE-VFGD--KSPA----ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAP 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 189207418 291 TLNLNNPGdpPEDFDCNYVAKSAQQYDVKVALSNSFGFGGTNASLCFRKVEG 342
Cdd:PRK07967 357 SANIEELD--PQAAGMPIVTETTDNAELTTVMSNSFGFGGTNATLVFRRYKG 406
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1-338 |
8.32e-76 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 238.73 E-value: 8.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 1 MARFAQYAMVASEEALKDSewfpkkeedlestvwrirTLSTRALLTSYQ-GVYMGSGIGSLDDV---------------- 63
Cdd:PRK09116 70 MGRVSLMATRASELALEDA------------------GLLGDPILTDGRmGIAYGSSTGSTDPIgafgtmllegsmsgit 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 64 ---Y----------NTTVAYEKGGPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAEScihpLAISGFARARSL-A 129
Cdd:PRK09116 132 attYvrmmphttavNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE----LCPTEAAVFDTLfA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 130 TDF-NDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQgpRLAMKHAL 208
Cdd:PRK09116 208 TSTrNDAPELTPRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETM--QIAMELAL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 209 RHAGLKPSDVDYVNAHATSTPLGDAAENRAikelllgedgkTAA---SKINISSTKGAIGHLLGAAGSVEAIFTVLGMHH 285
Cdd:PRK09116 286 KDAGLAPEDIGYVNAHGTATDRGDIAESQA-----------TAAvfgARMPISSLKSYFGHTLGACGALEAWMSIEMMNE 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 189207418 286 NILPPTLNLNNPgDPpedfDC---NYVAKSAQQYDVKVALSNSFGFGGTNASLCFR 338
Cdd:PRK09116 355 GWFAPTLNLTQV-DP----ACgalDYIMGEAREIDTEYVMSNNFAFGGINTSLIFK 405
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
74-337 |
1.05e-75 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 242.58 E-value: 1.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 74 GPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATDfNDRPTESSRPFDRARNGFVIG 153
Cdd:PLN02787 282 GPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQR-NDDPTKASRPWDMNRDGFVMG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 154 EGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYVNAHATSTPLGDA 233
Cdd:PLN02787 361 EGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 234 AENRAIKELLlgedGKTAASKINisSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNpgdPPEDFDCN-YVAKS 312
Cdd:PLN02787 441 KEYQALMRCF----GQNPELRVN--STKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLEN---PESGVDTKvLVGPK 511
|
250 260
....*....|....*....|....*
gi 189207418 313 AQQYDVKVALSNSFGFGGTNASLCF 337
Cdd:PLN02787 512 KERLDIKVALSNSFGFGGHNSSILF 536
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
93-339 |
8.60e-72 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 228.76 E-value: 8.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 93 ASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATD-FNDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRG 171
Cdd:PRK07103 177 AARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDrFADEPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 172 AQIYAEVAGYGLSSDAYHMTAPREDGQGPrlAMKHALRHAGLKPSDVDYVNAHATSTPLGDAAENRAIKElllgedgkTA 251
Cdd:PRK07103 257 ARPYAKLLGWSMRLDANRGPDPSLEGEMR--VIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELAALFA--------SG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 252 ASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPGDPpedfDCNYVAKSAQQYDVKVALSNSFGFGGT 331
Cdd:PRK07103 327 LAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPIDE----RFRWVGSTAESARIRYALSLSFGFGGI 402
|
....*...
gi 189207418 332 NASLCFRK 339
Cdd:PRK07103 403 NTALVLER 410
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
90-337 |
2.16e-65 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 211.62 E-value: 2.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 90 IGDASRLIQFGDADIMIAGGAES-CIHPLaiSGFARARSLAtdfnDRPTessRPFDRARNGFVIGEGAGVMVLEelehak 168
Cdd:PRK09185 167 FASARRLLEAGLCDAAIVGGVDSlCRLTL--NGFNSLESLS----PQPC---RPFSANRDGINIGEAAAFFLLE------ 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 169 nRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYVNAHATSTPLGDAAENRAIKELLlgedg 248
Cdd:PRK09185 232 -REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVF----- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 249 ktaASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPgDPpeDFDCNYVAKSAQQYDVKVALSNSFGF 328
Cdd:PRK09185 306 ---GDGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQP-DP--ALPPLYLVENAQALAIRYVLSNSFAF 379
|
....*....
gi 189207418 329 GGTNASLCF 337
Cdd:PRK09185 380 GGNNCSLIF 388
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
97-335 |
4.37e-64 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 209.10 E-value: 4.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 97 IQFGDADIMIAGGAESCIHPLAISGFARARSLATDfNDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYA 176
Cdd:PRK06501 189 IRRGETDRALCIATDGSVSAEALIRFSLLSALSTQ-NDPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILG 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 177 EVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYVNAHATSTPLGDAAENRAIKElLLGEdgktAASKIN 256
Cdd:PRK06501 268 IVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSA-VFGE----RLASIP 342
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189207418 257 ISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPgDPPEDFDCnyVAKSAQQYDVKVALSNSFGFGGTNASL 335
Cdd:PRK06501 343 VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNP-DPAIPLDV--VPNVARDARVTAVLSNSFGFGGQNASL 418
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
93-335 |
1.44e-59 |
|
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: 197.40 E-value: 1.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 93 ASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLAtdfndrPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGA 172
Cdd:cd00833 180 ACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS------PDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 173 QIYAEVAGYGLSSDAY--HMTAPREDGQgpRLAMKHALRHAGLKPSDVDYVNAHATSTPLGDAAENRAIKELLlgEDGKT 250
Cdd:cd00833 254 RIYAVIRGSAVNQDGRtkGITAPSGEAQ--AALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVF--GGSRS 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 251 AASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPgDPPEDFD--CNYVAKSAQQYD----VKVALSN 324
Cdd:cd00833 330 ADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETP-NPKIDFEesPLRVPTEARPWPapagPRRAGVS 408
|
250
....*....|.
gi 189207418 325 SFGFGGTNASL 335
Cdd:cd00833 409 SFGFGGTNAHV 419
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
3-335 |
1.19e-56 |
|
"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: 189.19 E-value: 1.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 3 RFAQYAMVASEEALKDSEWFPKKEEDLESTvwrirtlstralltsyqGVYMGSGIGSLD--------------DVYNTTV 68
Cdd:cd00828 71 RTTLLALVATEEALADAGITDPYEVHPSEV-----------------GVVVGSGMGGLRflrrggkldaravnPYVSPKW 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 69 AYE--------------KGGPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAEScIHPLAISGFARARSLATDfND 134
Cdd:cd00828 134 MLSpntvagwvnilllsSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTA-EE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 135 RPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPReDGQGPRLAMKHALRHAGLK 214
Cdd:cd00828 212 EPEEMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 215 PSDVDYVNAHATSTPLGDAAENRAIKELLlgedgKTAASKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNL 294
Cdd:cd00828 291 LDDLDVISAHGTSTPANDVAESRAIAEVA-----GALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 189207418 295 NnpgDPPEDFDCNYVAKSAQ--QYDVKVALSNSFGFGGTNASL 335
Cdd:cd00828 366 D---DVDPDVEHLSVVGLSRdlNLKVRAALVNAFGFGGSNAAL 405
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
175-295 |
1.82e-45 |
|
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: 151.18 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 175 YAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYVNAHATSTPLGDAAENRAIKELLlgeDGKTAASK 254
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVF---GSGARKQP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 189207418 255 INISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLN 295
Cdd:pfam02801 78 LAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
100-333 |
1.89e-44 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 163.12 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 100 GDADIMIAGGAESCIHPLAISGFARARSLAtdfndrPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVA 179
Cdd:COG3321 191 GECDLALAGGVNLMLTPESFILFSKGGMLS------PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 180 GYGLSSD-AYH-MTAPREDGQgpRLAMKHALRHAGLKPSDVDYVNAHATSTPLGDAAENRAIKElLLGEDGkTAASKINI 257
Cdd:COG3321 265 GSAVNQDgRSNgLTAPNGPAQ--AAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTA-AFGQGR-PADQPCAI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 258 SSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPgdPPE-DFDcN---YVAKSAQQYDVK----VALSNSFGFG 329
Cdd:COG3321 341 GSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETP--NPHiDFE-NspfYVNTELRPWPAGggprRAGVSSFGFG 417
|
....
gi 189207418 330 GTNA 333
Cdd:COG3321 418 GTNA 421
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
73-335 |
1.10e-43 |
|
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: 153.18 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 73 GGPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLAtdfndrPTESSRPFDRARNGFVI 152
Cdd:cd00825 86 HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST------PEKASRTFDAAADGFVF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 153 GEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYVNAHATSTPLGD 232
Cdd:cd00825 160 GDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 233 AAENRAIKELLLGEdgktaasKINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPgdppeDFDCNYVAKS 312
Cdd:cd00825 240 VKELKLLRSEFGDK-------SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEEL-----DEAGLNIVTE 307
|
250 260
....*....|....*....|...
gi 189207418 313 AQQYDVKVALSNSFGFGGTNASL 335
Cdd:cd00825 308 TTPRELRTALLNGFGLGGTNATL 330
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
100-332 |
1.68e-33 |
|
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: 131.28 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 100 GDADIMIAGGAESCIHPLAISGFARARSLATDfndrptESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVA 179
Cdd:TIGR02813 223 GRSEMMITGGVCTDNSPFMYMSFSKTPAFTTN------EDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 180 GYGLSSDAYHMT--APREDGQGPrlAMKHALRHAGLKPSDVDYVNAHATSTPLGDAAENRAIKELLlgEDGKTAASKINI 257
Cdd:TIGR02813 297 GVGASSDGKFKSiyAPRPEGQAK--ALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVF--SQDNDQKQHIAL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 258 SSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPgDPPEDFDCN--YVAKSAQQYDVKV------ALSNSFGFG 329
Cdd:TIGR02813 373 GSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQP-NPKLDIENSpfYLNTETRPWMQREdgtprrAGISSFGFG 451
|
...
gi 189207418 330 GTN 332
Cdd:TIGR02813 452 GTN 454
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
89-335 |
5.82e-33 |
|
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: 126.32 E-value: 5.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 89 SIGDASRLIQFGdADIMIAGGAESCIHPLAISGFARARSLATDfnDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAK 168
Cdd:cd00832 167 ALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTS--DDPARAYLPFDAAAAGYVPGEGGAILVLEDAAAAR 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 169 NRGAQIYAEVAGYGLSsdayhMTAPREDGQGPRL--AMKHALRHAGLKPSDVDYVNAHATSTPLGDAAENRAIKElLLGE 246
Cdd:cd00832 244 ERGARVYGEIAGYAAT-----FDPPPGSGRPPGLarAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAA-VFGP 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 247 DGktaaskINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLnnpGDPPEDFDCNYVAKSAQQYDVKVALSNSF 326
Cdd:cd00832 318 RG------VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNV---TDVPPAYGLDLVTGRPRPAALRTALVLAR 388
|
....*....
gi 189207418 327 GFGGTNASL 335
Cdd:cd00832 389 GRGGFNSAL 397
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
72-336 |
1.07e-31 |
|
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: 119.47 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 72 KGGPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCihplaisgfararslatdfndrptessrpfdrarngfV 151
Cdd:cd00327 57 SGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF-------------------------------------V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 152 IGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSD-AYHMTAPREDGQGPrlAMKHALRHAGLKPSDVDYVNAHATSTPL 230
Cdd:cd00327 100 FGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVSGEGLAR--AARKALEGAGLTPSDIDYVEAHGTGTPI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 231 GDAAEnraiKELLLGEDGKTAaskINISSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTlnlnnpGDPPedfdcnyva 310
Cdd:cd00327 178 GDAVE----LALGLDPDGVRS---PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT------PREP--------- 235
|
250 260
....*....|....*....|....*.
gi 189207418 311 ksaqqydvKVALSNSFGFGGTNASLC 336
Cdd:cd00327 236 --------RTVLLLGFGLGGTNAAVV 253
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
93-335 |
5.59e-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: 107.80 E-value: 5.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 93 ASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLAtdfndrPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGA 172
Cdd:smart00825 107 ACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 173 QIYAEVAGYGLSSDAYH--MTAPREDGQgprlamkhalrhaglkpsdvdyvnahatstplgdaaenraikeLLLGedgkt 250
Cdd:smart00825 181 PILAVIRGSAVNQDGRSngITAPSGPAQ-------------------------------------------LLIG----- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 251 aaskinisSTKGAIGHLLGAAGSVEAIFTVLGMHHNILPPTLNLNNPGdPPEDFDCN--YVAKSAQQYD----VKVALSN 324
Cdd:smart00825 213 --------SVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPN-PHIDLEESplRVPTELTPWPppgrPRRAGVS 283
|
250
....*....|.
gi 189207418 325 SFGFGGTNASL 335
Cdd:smart00825 284 SFGFGGTNAHV 294
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
1-167 |
6.35e-22 |
|
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: 93.08 E-value: 6.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 1 MARFAQYAMVASEEALKDSEWFPKKEEDLESTVW---RIRTLSTRALLTSYQGVYMGS--GIGSLDDVYNTTVAYEKG-- 73
Cdd:pfam00109 84 MDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFigsGIGDYAALLLLDEDGGPRRGSpfAVGTMPSVIAGRISYFLGlr 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 74 GPNHAATTACTTGAHSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATDfndrptESSRPFDRARNGFVIG 153
Cdd:pfam00109 164 GPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD------GPCKAFDPFADGFVRG 237
|
170
....*....|....
gi 189207418 154 EGAGVMVLEELEHA 167
Cdd:pfam00109 238 EGVGAVVLKRLSDA 251
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
146-282 |
4.40e-08 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 54.33 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 146 ARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYGlssDAYHmtAPREDGQGPRLAMKHALRHAGLKPSDVDY--VNA 223
Cdd:PLN02644 244 AGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYA---DAAQ--APELFTTAPALAIPKALKHAGLEASQVDYyeINE 318
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 189207418 224 HATSTPLGDaaenraikELLLGEDgktaASKINISSTKGAIGHLLGAAGSvEAIFTVLG 282
Cdd:PLN02644 319 AFSVVALAN--------QKLLGLD----PEKVNVHGGAVSLGHPIGCSGA-RILVTLLG 364
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
155-273 |
4.72e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 50.88 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 155 GAGVMVLEELEHAKNRGAQIYAEVAGYGLSS-DAYHMtapredGQGPRLAMKHALRHAGLKPSDVDY--VNAHATSTPLg 231
Cdd:PRK06445 254 GASYVLLMSKKAVKKYGLKPMAKIRSFGFAGvPPAIM------GKGPVPASKKALEKAGLSVKDIDLweINEAFAVVVL- 326
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 189207418 232 daaenRAIKELLLGEDgktaasKINISSTKGAIGHLLGAAGS 273
Cdd:PRK06445 327 -----YAIKELGLDPE------TVNIKGGAIAIGHPLGATGA 357
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
120-272 |
6.03e-06 |
|
nondecarboxylating condensing enzymes; In general, thiolases 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. 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: 238422 [Multi-domain] Cd Length: 393 Bit Score: 47.49 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 120 SGFARARSLATDFNDRPTESSRPFDRARNGFVIGEGAGVMVLEELEHAKNRGAQIYA-EVAGYGLSSDayhMTAPRED-- 196
Cdd:cd00826 185 IQFGDEASLDEIAKLRPAFDKEDFLTAGNACGLNDGAAAAILMSEAEAQKHGLQSKArEIQALEMITD---MASTFEDkk 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 197 ------GQGPRLAMKHALRHAGLKPSDVDYVNAH--------ATSTPLGDAAENRAIKELLLGEDGKTAASKINISSTKG 262
Cdd:cd00826 262 vikmvgGDGPIEAARKALEKAGLGIGDLDLIEAHdafaanacATNEALGLCPEGQGGALVDRGDNTYGGKSIINPNGGAI 341
|
170
....*....|
gi 189207418 263 AIGHLLGAAG 272
Cdd:cd00826 342 AIGHPIGASG 351
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
88-221 |
8.25e-06 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 46.94 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 88 HSIGDASRLIQFGDADIMIAGGAESCIHPLAISGFARARSLATdfndrpteSSRPfdrarNGFVIGEGAGVMVLEELEHA 167
Cdd:PRK06147 138 VALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLT--------SQNS-----NGFIPGEAAAAVLLGRPAGG 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 189207418 168 KNRGAQIYaevaGYGLSSDAYHMTAPRE---DGQGPRLAMKHALRHAGLKPSDVDYV 221
Cdd:PRK06147 205 EAPGLPLL----GLGLGREPAPVGESEDlplRGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
155-273 |
1.75e-05 |
|
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: 45.93 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 155 GAGVMVLEELEHAKNRGAQIYAEVAGYglssdAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYV---NAHAtSTPLG 231
Cdd:cd00751 247 GAAAVLLMSEEKAKELGLKPLARIVGY-----AVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIeinEAFA-AQALA 320
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 189207418 232 daaenrAIKELLLGEDgktaasKINISstKGAI--GHLLGAAGS 273
Cdd:cd00751 321 ------CLKELGLDPE------KVNVN--GGAIalGHPLGASGA 350
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
152-272 |
3.76e-05 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 45.14 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 152 IGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSS--DAYhMtapredGQGPRLAMKHALRHAGLKPSDVDYVNAhatstp 229
Cdd:PRK05790 250 INDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGvdPAI-M------GIGPVPAIRKALEKAGWSLADLDLIEI------ 316
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 189207418 230 lgdaaeNRA--------IKEllLGEDgktaASKINISSTKGAIGHLLGAAG 272
Cdd:PRK05790 317 ------NEAfaaqalavEKE--LGLD----PEKVNVNGGAIALGHPIGASG 355
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
193-273 |
6.42e-05 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 41.86 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 193 PREDGQGPRLAMKHALRHAGLKPSDVDYVNAHatstplgdaaENRAIKELLLGEDGKTAASKINISSTKGAIGHLLGAAG 272
Cdd:pfam02803 17 PAIMGIGPAYAIPKALKKAGLTVNDIDLFEIN----------EAFAAQALAVAKDLGIDPEKVNVNGGAIALGHPLGASG 86
|
.
gi 189207418 273 S 273
Cdd:pfam02803 87 A 87
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
155-272 |
1.03e-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: 43.90 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 155 GAGVMVLEELEHAKNRGAQIYAEVAGYglssdAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYV---NAHAtSTPLG 231
Cdd:COG0183 251 GAAALLLMSEEAAKELGLKPLARIVAY-----AVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIeinEAFA-AQVLA 324
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 189207418 232 daaenrAIKEllLGEDgktaASKINIsstKG---AIGHLLGAAG 272
Cdd:COG0183 325 ------VLRE--LGLD----PDKVNV---NGgaiALGHPLGASG 353
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
146-272 |
2.24e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 42.57 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 146 ARNGFVIGEGAGVMVLEELEHAKNRGAQIYAEVAGYglssdAYHMTAPREDGQGPRLAMKHALRHAGLKPSDVDYVNAHa 225
Cdd:PRK05656 244 AGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAY-----ANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEAN- 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 189207418 226 tstplgdaaENRAIKELLLGEDGKTAASKINISSTKGAIGHLLGAAG 272
Cdd:PRK05656 318 ---------EAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASG 355
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
151-283 |
2.60e-04 |
|
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: 42.64 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 151 VIGEGAGVMVLEELEHAKNRGAQiYAEVAGYGLSSDAYHMTApREDGQGP---RLAMKHALRHAGLKPSDVDYVNAHATS 227
Cdd:cd00829 203 PVSDGAAAVVLASEERARELTDR-PVWILGVGAASDTPSLSE-RDDFLSLdaaRLAARRAYKMAGITPDDIDVAELYDCF 280
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189207418 228 TP--------LGDAAENRAIKELllgEDGKTAAS---KINISStkGAI--GHLLGAAGSVEAIFTVLGM 283
Cdd:cd00829 281 TIaellaledLGFCEKGEGGKLV---REGDTAIGgdlPVNTSG--GLLskGHPLGATGLAQAVEAVRQL 344
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
97-180 |
3.98e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 41.86 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 97 IQFGDADIMIAGGAESCIHPLAISGFARARSLATDfNDRPTESSRPFDRArnGFVIGEGAGVMVLEELEHAKNRGAQIYA 176
Cdd:PRK06519 189 IASGQSDHALVGGAYNAERPDMLLLYELGGLLLKG-GWAPVWSRGGEDGG--GFILGSGGAFLVLESREHAEARGARPYA 265
|
....
gi 189207418 177 EVAG 180
Cdd:PRK06519 266 RISG 269
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
141-273 |
5.00e-03 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 38.41 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 141 RP-FDRArNGFV-------IGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSS-DAYHMtapredGQGPRLAMKHALRHA 211
Cdd:PRK08947 223 RPaFDPV-NGTVtagtssaLSDGASAMLVMSESRAKELGLKPRARIRSMAVAGcDPSIM------GYGPVPATQKALKRA 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189207418 212 GLKPSDVDYVNAH----ATSTPLgdaaenraIKELLLGEdgkTAASKINISSTKGAIGHLLGAAGS 273
Cdd:PRK08947 296 GLSISDIDVFELNeafaAQSLPC--------LKDLGLLD---KMDEKVNLNGGAIALGHPLGCSGA 350
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
152-272 |
5.46e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 38.29 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189207418 152 IGEGAGVMVLEELEHAKNRGAQIYAEVAGYGLSSDAYHMTApREDGQG---PRLAMKHALRHAGLKPSDVDYVNAHATST 228
Cdd:PRK12578 209 ISDGSATAIFASEEKVKELKIDSPVWITGIGYANDYAYVAR-RGEWVGfkaTQLAARQAYNMAKVTPNDIEVATVHDAFT 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 189207418 229 --------PLGDAAENRAIKELLLGEDGKTAASKINISSTKGAIGHLLGAAG 272
Cdd:PRK12578 288 iaeimgyeDLGFTEKGKGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATG 339
|
|
| |
