|
Name |
Accession |
Description |
Interval |
E-value |
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
1-336 |
7.11e-173 |
|
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: 485.06 E-value: 7.11e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:cd00751 49 MGNVLQAGEGQNPARQAALLAGLPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 81 -GGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPdVV 159
Cdd:cd00751 129 rLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 160 VKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIA 238
Cdd:cd00751 208 VDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 239 PVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GE 316
Cdd:cd00751 287 PVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGR 366
|
330 340
....*....|....*....|
gi 1897357996 317 YGLASICNGGGGASAMLIQK 336
Cdd:cd00751 367 YGLATMCIGGGQGAAMVIER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-337 |
4.21e-162 |
|
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: 457.99 E-value: 4.21e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:COG0183 53 LGCVLQAGQGQNPARQAALLAGLPESVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 81 GG-VKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQpDVV 159
Cdd:COG0183 133 RMnAKLVDPMINPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKG-EVV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 160 VKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIA 238
Cdd:COG0183 212 VDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 239 PVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GE 316
Cdd:COG0183 291 PVPATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGR 370
|
330 340
....*....|....*....|.
gi 1897357996 317 YGLASICNGGGGASAMLIQKL 337
Cdd:COG0183 371 YGLATMCIGGGQGIALIIERV 391
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
1-337 |
4.01e-156 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 443.00 E-value: 4.01e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGST 78
Cdd:PLN02644 52 FGNVLSANLGQAPARQAALGAGLPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 79 PYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV-KGQPD 157
Cdd:PLN02644 132 RLGHDTVVDGMLKDGLWDVYNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 158 VVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PLN02644 212 VIVDKDEGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTT 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--G 315
Cdd:PLN02644 292 APALAIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknG 371
|
330 340
....*....|....*....|..
gi 1897357996 316 EYGLASICNGGGGASAMLIQKL 337
Cdd:PLN02644 372 KYGVAGICNGGGGASAIVVELM 393
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
1-335 |
2.05e-144 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 412.78 E-value: 2.05e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTP- 79
Cdd:TIGR01930 48 FGNVLQAGEQQNIARQAALLAGLPESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWg 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 80 --YGGVKLEDLIVKDgLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPD 157
Cdd:TIGR01930 128 vkPGNAELEDARLKD-LTDANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 158 VVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:TIGR01930 207 TVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--G 315
Cdd:TIGR01930 286 GPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgG 365
|
330 340
....*....|....*....|
gi 1897357996 316 EYGLASICNGGGGASAMLIQ 335
Cdd:TIGR01930 366 RYGLATMCIGGGQGAAVILE 385
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-334 |
4.41e-141 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 404.53 E-value: 4.41e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN--RGST 78
Cdd:PRK05790 53 MGQVLQAGAGQNPARQAALKAGLPVEVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPgsRWGQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 79 PYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDV 158
Cdd:PRK05790 133 KMGDVELVDTMIHDGLTDAFNGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 159 VVKEDeEYKRVDFS--KVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFP 236
Cdd:PRK05790 213 VVDTD-EHPRPDTTaeSLAKLRPAF-DKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 237 IAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--Q 314
Cdd:PRK05790 291 IGPVPAIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKrrG 370
|
330 340
....*....|....*....|
gi 1897357996 315 GEYGLASICNGGGGASAMLI 334
Cdd:PRK05790 371 AKKGLATLCIGGGQGVALIV 390
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-335 |
9.67e-133 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 383.68 E-value: 9.67e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:PRK08235 53 MGTVLQGGQGQIPSRQAARAAGIPWEVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 81 --GGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVT-VKGQPD 157
Cdd:PRK08235 133 rmGDNEVIDLMVADGLTCAFSGVHMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPqRKGDPI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 158 VVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PRK08235 213 VVAKDEAPRKDTTIEKLAKLKPVFDKT-GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--G 315
Cdd:PRK08235 292 TPGYAINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrgG 371
|
330 340
....*....|....*....|
gi 1897357996 316 EYGLASICNGGGGASAMLIQ 335
Cdd:PRK08235 372 GIGIAAICSGGGQGDAVLIE 391
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-335 |
5.39e-106 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 315.68 E-value: 5.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGST 78
Cdd:PRK06954 58 MGCVLPAGQGQAPARQAALGAGLPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpkARGGM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 79 PYGGVKLEDLIVKDGLTDVYNKIH-MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQpD 157
Cdd:PRK06954 138 RMGHGQVLDHMFLDGLEDAYDKGRlMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKG-D 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 158 VVVKEDEEYKRVDFSKVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PRK06954 217 TVIDRDEQPFKANPEKIPTLKPAFSK-TGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--G 315
Cdd:PRK06954 296 APVGAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRArgG 375
|
330 340
....*....|....*....|
gi 1897357996 316 EYGLASICNGGGGASAMLIQ 335
Cdd:PRK06954 376 KRGVASLCIGGGEATAMGIE 395
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
15-337 |
2.70e-99 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 298.41 E-value: 2.70e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 15 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVkD 92
Cdd:PRK09051 69 RVAAINAGVPQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpaARWGARMGDAKLVDMMV-G 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 93 GLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV-TVKGqpDVVVKEDEEYKR-VD 170
Cdd:PRK09051 148 ALHDPFGTIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIkTRKG--EVVFDTDEHVRAdTT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 171 FSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDV 250
Cdd:PRK09051 226 LEDLAKLKPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 251 GLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGG 328
Cdd:PRK09051 306 GLTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQriGGRYALVTMCIGGGQ 385
|
....*....
gi 1897357996 329 ASAMLIQKL 337
Cdd:PRK09051 386 GIAAIFERL 394
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-336 |
3.27e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 285.63 E-value: 3.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGST 78
Cdd:PRK05656 53 LGQVLTAGAGQNPARQAAIKAGLPHSVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLpgARTGL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 79 PYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV-TVKGQPD 157
Cdd:PRK05656 133 RMGHAQLVDSMITDGLWDAFNDYHMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIpQRKGEPL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 158 VVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PRK05656 213 AFATDEQPRAGTTAESLAKLKPAFKKD-GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQG 315
Cdd:PRK05656 292 GPVSATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMirRDA 371
|
330 340
....*....|....*....|.
gi 1897357996 316 EYGLASICNGGGGASAMLIQK 336
Cdd:PRK05656 372 KKGLATLCIGGGQGVALAIER 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-335 |
1.28e-92 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 281.53 E-value: 1.28e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS---NVPYVmnRGS 77
Cdd:PRK06633 54 LGQVITGGSGQNPARQTLIHAGIPKEVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI--RAG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 78 TPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPD 157
Cdd:PRK06633 132 AKFGDIKMVDLMQYDGLTDVFSGVFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 158 VVVKEDEEYKRVDFSKVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PRK06633 212 LFDHDETVRPDTSLEILSKLRPAFDK-NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QG 315
Cdd:PRK06633 291 APVPASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRraKA 370
|
330 340
....*....|....*....|
gi 1897357996 316 EYGLASICNGGGGASAMLIQ 335
Cdd:PRK06633 371 KKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
15-337 |
2.47e-91 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 278.38 E-value: 2.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 15 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYG-GVKLEDL----- 88
Cdd:PRK09050 69 RMSALLAGLPVSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSrQAEIFDTtigwr 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 89 IVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEeYKR 168
Cdd:PRK09050 149 FVNPLMKAQYGVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDE-HPR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 169 VDFS--KVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMV 246
Cdd:PRK09050 228 PETTleALAKLKPVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 247 LKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEI--DPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASI 322
Cdd:PRK09050 307 LARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTM 386
|
330
....*....|....*
gi 1897357996 323 CNGGGGASAMLIQKL 337
Cdd:PRK09050 387 CIGVGQGIALAIERV 401
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
1-209 |
2.48e-91 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 273.41 E-value: 2.48e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN---RGS 77
Cdd:pfam00108 50 VGNVLQAGEGQNPARQAALKAGIPDSAPAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 78 TPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPD 157
Cdd:pfam00108 130 LKHGDEKKHDLLIPDGLTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1897357996 158 VVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTAD 209
Cdd:pfam00108 210 TVDKDEGIRPPTTAEPLAKLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-335 |
1.73e-83 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 258.02 E-value: 1.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNR----- 75
Cdd:PRK06366 53 MGNVIQAGVGQNPAGQAAYHAGLPFGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSdlrwg 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 76 -GSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvkg 154
Cdd:PRK06366 133 pKHLLHKNYKIDDAMLVDGLIDAFYFEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND---- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 155 qpdvvVKEDEEYKRVDFSKVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPID 234
Cdd:PRK06366 209 -----LDRDEGIRKTTMEDLAKLPPAFDK-NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 235 FPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ 314
Cdd:PRK06366 283 FVEAPIPATRKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKT 362
|
330 340
....*....|....*....|...
gi 1897357996 315 G--EYGLASICNGGGGASAMLIQ 335
Cdd:PRK06366 363 RhmKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
8-327 |
4.91e-83 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 257.22 E-value: 4.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 8 GEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN--RGSTPYGGVKL 85
Cdd:PRK06205 60 GEAPAIGRVAALDAGLPVTVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 86 EDLIVKDGLT---DVYNKIH-MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVK 161
Cdd:PRK06205 140 HDRLARGRETaggRRFPVPGgMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 162 EDEEYkRVDFS--KVPKLKTVFQK--ENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PRK06205 220 RDEHP-RADTTleSLAKLRPIMGKqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQ---KVNINGGAVSLGHPIGMSGARIVGHLTHALK- 313
Cdd:PRK06205 299 GPVPATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQr 378
|
330
....*....|....*
gi 1897357996 314 -QGEYGLASICNGGG 327
Cdd:PRK06205 379 rQARYGLETMCIGGG 393
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
15-336 |
3.92e-82 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 254.65 E-value: 3.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 15 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGL 94
Cdd:PRK06445 74 RHPIFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNPKLLTDPKYIEYDL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 95 TDVYNkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKV 174
Cdd:PRK06445 154 TTGYV---MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 175 PKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKK 254
Cdd:PRK06445 231 AKLPPAF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 255 EDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAM 332
Cdd:PRK06445 310 KDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLqiKGKDYGVATLCVGGGQGGAV 389
|
....
gi 1897357996 333 LIQK 336
Cdd:PRK06445 390 VLER 393
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
15-337 |
3.79e-79 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 246.84 E-value: 3.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 15 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGS-TPYGGVKLEDLIVKDG 93
Cdd:PRK09052 74 RIGALLAGLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSmSPAIFARDENVGIAYG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 94 ltdvynkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKgQPD-----VVVKEDE---- 164
Cdd:PRK09052 154 ---------MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITER-FPDlatgeVDVKTRTvdld 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 165 EYKRVDFS--KVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYA 242
Cdd:PRK09052 224 EGPRADTSleGLAKLKPVFANK-GSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 243 ASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLA 320
Cdd:PRK09052 303 IPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMV 382
|
330
....*....|....*..
gi 1897357996 321 SICNGGGGASAMLIQKL 337
Cdd:PRK09052 383 TMCVGTGMGAAGIFERL 399
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
6-337 |
2.92e-77 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 241.98 E-value: 2.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 6 QGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGstpyggvKL 85
Cdd:PRK07108 60 EGATGANIARQIALRAGLPVTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRH-------ML 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 86 EDLIVKDGLTDVYnkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQ---------P 156
Cdd:PRK07108 133 REGWLVEHKPEIY--WSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVAdkatgrlftK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 157 DVVVKEDEEYkRVDFSK--VPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPID 234
Cdd:PRK07108 211 EVTVSADEGI-RPDTTLegVSKIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 235 FPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGhltHALKQ 314
Cdd:PRK07108 288 MGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTG---HALIE 364
|
330 340
....*....|....*....|....*...
gi 1897357996 315 GE-----YGLASICNGGGGASAMLIQKL 337
Cdd:PRK07108 365 GKrrgakYVVVTMCIGGGQGAAGLFEVL 392
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-337 |
5.38e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 239.53 E-value: 5.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:PRK08170 54 LGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRW 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 81 ---------GGVKLEDL-------------IVKdGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEA 138
Cdd:PRK08170 134 lagwyaaksIGQKLAALgklrpsylapvigLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 139 GKFGnEVIPVtVTVKGQpdvvVKEDEEYKRVDFS--KVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNV 216
Cdd:PRK08170 213 GRLK-EVVPL-FDRDGK----FYDHDDGVRPDSSmeKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 217 TPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EI 279
Cdd:PRK08170 287 PPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWadeeycreqlgldgalgEL 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 280 DPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK08170 367 DRERLNVDGGAIALGHPVGASGARIVLHLLHALKRrgTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-337 |
8.21e-75 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 235.39 E-value: 8.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGE-GQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMNRGSTp 79
Cdd:PRK06504 53 MGCVSQVGEqATNVARNAVLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP--MGSPST- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 80 yggvkledLIVKDGLTDV--------YNKIH----MGscAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIP 147
Cdd:PRK06504 130 --------LPAKNGLGHYkspgmeerYPGIQfsqfTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 148 VTVTVKGQPDVVVKEDEEYkRVDFS--KVPKLKTVfqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAF 225
Cdd:PRK06504 200 LEITRADGSGEMHTVDEGI-RFDATleGIAGVKLI--AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHM 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 226 ADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIV 305
Cdd:PRK06504 277 TVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLM 356
|
330 340 350
....*....|....*....|....*....|....
gi 1897357996 306 GHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK06504 357 TTLVHALKQrgKRYGLQTMCEGGGMANVTIVERL 390
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-336 |
1.43e-74 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 235.44 E-value: 1.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGE-GQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTP 79
Cdd:PRK08131 53 LGCTNQAGEdSRNVARNALLLAGLPVTVPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 80 YGgvklEDLIVKDG----------LTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVT 149
Cdd:PRK08131 133 FS----RDAKVFDTtigarfpnpkIVAQYGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 150 V-TVKGQPDVVVKEDEEYK-RVDFSKVPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFAD 227
Cdd:PRK08131 209 VpQGRKLPPKLVAEDEHPRpSSTVEALTKLKPLF--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 228 AAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEI--DPQKVNINGGAVSLGHPIGMSGARIV 305
Cdd:PRK08131 287 AGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLA 366
|
330 340 350
....*....|....*....|....*....|...
gi 1897357996 306 GHLTHALK--QGEYGLASICNGGGGASAMLIQK 336
Cdd:PRK08131 367 LTAARELQrrGKRYAVVSLCIGVGQGLAMVIER 399
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
21-331 |
1.62e-73 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 232.33 E-value: 1.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 21 AGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVmnrgstpyGGVKLEDLIVKDGLTDVYnk 100
Cdd:PRK07661 75 AGLPYTVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--------GHVVRPNPRLVEAAPEYY-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 101 IHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV-------KGQPDVVVKEDEEYKRVDFSK 173
Cdd:PRK07661 145 MGMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLrtvgennKLQEETITFSQDEGVRADTTL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 174 --VPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVG 251
Cdd:PRK07661 225 eiLGKLRPAFNV-KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 252 LKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK-QGE-YGLASICNGGGGA 329
Cdd:PRK07661 304 LELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKrRNEqFGIVTMCIGGGMG 383
|
..
gi 1897357996 330 SA 331
Cdd:PRK07661 384 AA 385
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-337 |
4.18e-73 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 231.82 E-value: 4.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGE-GQAPTRQAVLGAGLPiSTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNvpYVM-NRGST 78
Cdd:PRK07851 55 LGCGLPGGEqGFNMARVVAVLLGYD-FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSR--FAKgNSDSL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 79 P-------------------YGGVKLEDLIVKDGLTDVYnkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAG 139
Cdd:PRK07851 132 PdtknplfaeaqartaaraeGGAEAWHDPREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 140 KFGNEVIPVTVtvkgqPD--VVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVT 217
Cdd:PRK07851 210 FFEREITPVTL-----PDgtVVSTDDGPRAGTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 218 PLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPI 297
Cdd:PRK07851 284 PLARIVSTGVSGLSPEIMGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPF 363
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1897357996 298 GMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK07851 364 GMTGARITTTLLNNLQthDKTFGLETMCVGGGQGMAMVLERL 405
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-337 |
1.32e-72 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 229.59 E-value: 1.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGeGQAP--TRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP--YVMNRG 76
Cdd:PRK07801 53 FGCVDTIG-PQAGniARTSWLAAGLPEEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPisSAMTAG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 77 -----STPYGGVKledlivkdGLTDVYNK--IHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVT 149
Cdd:PRK07801 132 eqlgfTSPFAESK--------GWLHRYGDqeVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 150 vtvkgqpDVVVkeDEEYKRVDFSKVPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAA 229
Cdd:PRK07801 204 -------GVTV--DEGPRETSLEKMAGLKPLV--EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 230 VEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLT 309
Cdd:PRK07801 273 DDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLL 352
|
330 340 350
....*....|....*....|....*....|
gi 1897357996 310 HALKQ--GEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK07801 353 HELERtgGRYGLQTMCEGGGTANVTIIERL 382
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
15-337 |
1.80e-72 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 229.47 E-value: 1.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 15 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMNRGSTPYggvkledlivkDGL 94
Cdd:PRK08947 70 RNAALLAGIPHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--MNHGVDFH-----------PGL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 95 TDVYNKIH--MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkGQpdvvvKEDEEYKRVDFS 172
Cdd:PRK08947 137 SKNVAKAAgmMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTE----GH-----DADGVLKLFDYD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 173 KV----------PKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYA 242
Cdd:PRK08947 208 EVirpettvealAALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 243 ASMVLKDVGLKKEDIAMWEVNEAF---SLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEY 317
Cdd:PRK08947 288 TQKALKRAGLSISDIDVFELNEAFaaqSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERkdAQF 367
|
330 340
....*....|....*....|
gi 1897357996 318 GLASICNGGGGASAMLIQKL 337
Cdd:PRK08947 368 GLATMCIGLGQGIATVFERV 387
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
2-335 |
2.74e-70 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 224.86 E-value: 2.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 2 GNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP----------- 70
Cdd:PRK08963 57 GQVVQMPEAPNIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaral 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 71 YVMNRGST------PYGGVKLEDLI-VKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGN 143
Cdd:PRK08963 137 VDLNKARTlgqrlkLFSRLRLRDLLpVPPAVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 144 EVIPVTVTVKGQP---DVVVKEDEeykrvDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLA 220
Cdd:PRK08963 217 EVMTAHVPPYKQPleeDNNIRGDS-----TLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 221 RIVAFADAAVEPI-DFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EIDPQ 282
Cdd:PRK08963 292 YLRSYAFAAIDVWqDMLLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMS 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1897357996 283 KVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 335
Cdd:PRK08963 372 KFNVLGGSIAYGHPFAATGARMITQTLHELRRrgGGLGLTTACAAGGLGAAMVLE 426
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-337 |
1.58e-69 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 222.07 E-value: 1.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGE-GQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTP 79
Cdd:PRK08242 55 LGCVTPVGDqGADIARTAVLAAGLPETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 80 yggvkledliVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVtvtvKGQPDVV 159
Cdd:PRK08242 135 ----------MDPSTNFPTYFVPQGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV----KDQNGLT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 160 VKEDEEYKR--VDFSKVPKLKTVFQ--------------------KENGTVTAANASTLNDGAAALVLMTADAAKRLNVT 217
Cdd:PRK08242 201 ILDHDEHMRpgTTMESLAKLKPSFAmmgemggfdavalqkypeveRINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 218 PLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPI 297
Cdd:PRK08242 281 PRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPL 360
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1897357996 298 GMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK08242 361 GATGAMILGTVLDELerRGKRTALITLCVGGGMGIATIIERV 402
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
2-333 |
9.64e-69 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 221.56 E-value: 9.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 2 GNVLQGGEGQA-PTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPy 80
Cdd:PLN02287 99 GTVLAPGSQRAnECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNP- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 81 ggvKLEDL-IVKDGLtdvynkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV------TVK 153
Cdd:PLN02287 178 ---RVESFsQAQDCL------LPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTkivdpkTGE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 154 GQPDVVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPI 233
Cdd:PLN02287 249 EKPIVISVDDGIRPNTTLADLAKLKPVF-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 234 DFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK 313
Cdd:PLN02287 328 VMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMK 407
|
330 340
....*....|....*....|....*
gi 1897357996 314 Q----GEYGLASICNGGG-GASAML 333
Cdd:PLN02287 408 RrgkdCRFGVVSMCIGTGmGAAAVF 432
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
2-337 |
9.20e-68 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 217.28 E-value: 9.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 2 GNVLQGGE-GQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPy 80
Cdd:PRK07850 54 GCVTQAGEqSNNITRTAWLHAGLPYHVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGR- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 81 GGVKLEDLIVkdgltDVYNKIhmgSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV---KGQP- 156
Cdd:PRK07850 133 GLPRPDSWDI-----DMPNQF---EAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVldeEGQPt 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 157 --DVVVKEDEEYKRVDFSKVPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPID 234
Cdd:PRK07850 205 geTRLVTRDQGLRDTTMEGLAGLKPVL--EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYY 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 235 FPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ 314
Cdd:PRK07850 283 HLDGPVQATAKVLEKAGMKIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELER 362
|
330 340
....*....|....*....|....*
gi 1897357996 315 --GEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK07850 363 tdKSTALITMCAGGALSTGTIIERI 387
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
1-337 |
1.56e-63 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 205.77 E-value: 1.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAptRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPy 80
Cdd:PRK06690 49 LGNVVGPGGNVA--RLSALEAGLGLHIPGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSP- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 81 ggvkledlivkdgltDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkGQPDVVV 160
Cdd:PRK06690 126 ---------------ETIGDPDMGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN----GLLDESI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 161 KEDEEYKRVdfskVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPV 240
Cdd:PRK06690 187 KKEMNYERI----IKRTKPAFLH-NGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 241 YAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYG 318
Cdd:PRK06690 262 FAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKRedMKYG 341
|
330
....*....|....*....
gi 1897357996 319 LASICNGGGGASAMLIQKL 337
Cdd:PRK06690 342 IATLGIGGGIGLALLFEKV 360
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
216-336 |
3.50e-59 |
|
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: 186.31 E-value: 3.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 216 VTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGH 295
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1897357996 296 PIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 336
Cdd:pfam02803 81 PLGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
7-337 |
2.77e-55 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 185.75 E-value: 2.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 7 GGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS----NVPYVMNRGSTPYGg 82
Cdd:PRK06025 63 GKQGGDLGRMAALDAGYDIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaaMAAEDMAAGKPPLG- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 83 vkledliVKDG---LTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkgQPDVV 159
Cdd:PRK06025 142 -------MGSGnlrLRALHPQSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY-----RDDGS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 160 VKED-EEYKRVDFSK--VPKLKTVFQK-------ENGTV------------------TAANASTLNDGAAALVLMTADAA 211
Cdd:PRK06025 210 VALDhEEFPRPQTTAegLAALKPAFTAiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 212 KRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAV 291
Cdd:PRK06025 290 EKHGLKPRARIVAMANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAI 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1897357996 292 SLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK06025 370 ALGHPIGATGSILIGTVLDELERrgLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
14-336 |
6.18e-48 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 166.61 E-value: 6.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 14 TRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYV-----------MNRGSTPYGG 82
Cdd:PRK09268 71 TRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAvneglrkilleLNRAKTTGDR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 83 VKL------EDLIV--------KDGLTdvynkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPV 148
Cdd:PRK09268 151 LKAlgklrpKHLAPeiprngepRTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 149 TVTVKGQ---PDVVVKedeeykrvdfsKVPKLKTVFQK-ENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVA 224
Cdd:PRK09268 224 LGLTRDNnlrPDSSLE-----------KLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 225 FADAAVEPIDFP----IAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLE-----------------IDPQK 283
Cdd:PRK09268 293 AETAAVDFVHGKegllMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEdeeycrerlgldaplgsIDRSK 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1897357996 284 VNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQK 336
Cdd:PRK09268 373 LNVNGSSLAAGHPFAATGGRIVATLAKLLaeKGSGRGLISICAAGGQGVTAILER 427
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
1-335 |
8.63e-44 |
|
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: 154.96 E-value: 8.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvmnrgstpy 80
Cdd:cd00826 50 LGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSA---------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 81 ggvklEDLIVKDGLTDVYNKIHMgscaentakklniaRNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvKGQPDVVV 160
Cdd:cd00826 120 -----ENNAKEKHIDVLINKYGM--------------RACPDAFALAGQAGAEAAEKDGRFKDEFAKFGV--KGRKGDIH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 161 KEDEEYKR----VDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAA-------KRLNVTPLARIVAFADAA 229
Cdd:cd00826 179 SDADEYIQfgdeASLDEIAKLRPAFDKE-DFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 230 VEPIDFPIA----PVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQK------------------VNIN 287
Cdd:cd00826 258 EDKKVIKMVggdgPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPN 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1897357996 288 GGAVSLGHPIGMSGARIVGHLTHALKQGEY-------GLASICNGGGGASAMLIQ 335
Cdd:cd00826 338 GGAIAIGHPIGASGAAICAELCFELKGEAGkrqgagaGLALLCIGGGGGAAMCIE 392
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
190-334 |
3.77e-13 |
|
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: 68.24 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 190 AANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI----APVYAASMVLKDVGLKKEDIAMWEVNEA 265
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 266 FSLVVLANIKMLEIDPQKV---NINGGAVSLGHPIGMSGARIVGHLTHALKQGEY---------GLASICNGGGGASAML 333
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIpptpreprtVLLLGFGLGGTNAAVV 253
|
.
gi 1897357996 334 I 334
Cdd:cd00327 254 L 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
2-331 |
1.02e-11 |
|
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: 65.36 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 2 GNVLQGGEGQAPTRQAVLGAGLPIsTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyG 81
Cdd:cd00829 44 GNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRA-S 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 82 GVKLEDLIVKDGLT--DVYNKI---HM---GSCAENTAKklnIARNEQDAYAINSYtrskaAWEAGkfgneviPVTV-TV 152
Cdd:cd00829 122 DLEWEGPEPPGGLTppALYALAarrYMhryGTTREDLAK---VAVKNHRNAARNPY-----AQFRK-------PITVeDV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 153 KGQPDVVvkedEEYKRVDFSKVpklktvfqkengtvtaanastlNDGAAALVLMTADAAKRLNVTPlARIVAFADA---- 228
Cdd:cd00829 187 LNSRMIA----DPLRLLDCCPV----------------------SDGAAAVVLASEERARELTDRP-VWILGVGAAsdtp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 229 ---AVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML---------------EIDPQ---KVNIN 287
Cdd:cd00829 240 slsERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLgfcekgeggklvregDTAIGgdlPVNTS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1897357996 288 GGAVSLGHPIGMSGARIVGHLTHALKqGEYG--------LASICNGGGGASA 331
Cdd:cd00829 320 GGLLSKGHPLGATGLAQAVEAVRQLR-GEAGarqvpgarVGLAHNIGGTGSA 370
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
21-331 |
1.86e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 52.21 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 21 AGLPiSTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP---------------YVMNRGSTPyggvkl 85
Cdd:PRK06064 71 AGLA-PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPtpdateaiaragdyeWEEFFGATF------ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 86 edlivkDGLTDVYNKIHM---GSCAENTAKklnIARNEQDAYAINSYtrskaaweaGKFGNEvipVTVtvkgqpDVVVKE 162
Cdd:PRK06064 144 ------PGLYALIARRYMhkyGTTEEDLAL---VAVKNHYNGSKNPY---------AQFQKE---ITV------EQVLNS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 163 deeykrvdfSKVPKLKTVFqkengtvtaaNASTLNDGAAALVLMTADAAKRLNVTPLaRIVAFADAavepIDFPI----- 237
Cdd:PRK06064 197 ---------PPVADPLKLL----------DCSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQA----SDTIAlhdrk 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 238 ------APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EIDPQ-KVNINGGAVSL 293
Cdd:PRK06064 253 dfttldAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLgfakkgeggklaregqtYIGGDiPVNPSGGLKAK 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1897357996 294 GHPIGMSGARIVGHLTHALKQG-----------EYGLASicN-GGGGASA 331
Cdd:PRK06064 333 GHPVGATGVSQAVEIVWQLRGEaekgrqqvigaGYGLTH--NvGGTGHTA 380
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
194-305 |
2.78e-07 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 51.57 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 194 STLNDGAAALVLMTADAAKRLNVTPLARIVAFAdAAVEP--------IDFPIAP--VYAASMVLKDVGLK--KEDIAMWE 261
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGKKDPVYVKALQ-LAVSNgwelqyngWDGSYFPttRIAARKAYREAGITdpREELSMAE 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1897357996 262 VNEAFSLVVLANIKMLEIDPQ------------------KVNINGGAVSLGHPIGMSGARIV 305
Cdd:PRK06157 293 VHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
17-68 |
3.51e-06 |
|
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: 48.30 E-value: 3.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1897357996 17 AVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSN 68
Cdd:cd00834 142 GQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
28-73 |
2.56e-05 |
|
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: 45.47 E-value: 2.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1897357996 28 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNvPYVM 73
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT-PLGL 197
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
28-65 |
5.46e-05 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 44.39 E-value: 5.46e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1897357996 28 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMES 65
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
28-66 |
3.16e-04 |
|
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: 41.47 E-value: 3.16e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1897357996 28 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESM 66
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
194-322 |
8.14e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 41.03 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357996 194 STLNDGAAALVLMTADAAKRLNVTP----LARIVAFADAAVEPIDFP------IAPVYAASMVLKDVGLKKEDIAMWEVN 263
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASGNLYEDPpdatrmFTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897357996 264 EAFSLVVLANIKMLEI-DPQK-----------------VNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASI 322
Cdd:PTZ00455 336 DCFTIAELLMYEALGIaEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGqcGEYQMKNI 414
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
196-257 |
2.85e-03 |
|
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: 39.06 E-value: 2.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1897357996 196 LNDGAAALVLMTADAAKRLNVTPLARIVAFA---DAA--VEPIDFPIAPVYAASMVLKDVGLKKEDI 257
Cdd:cd00834 229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGassDAYhiTAPDPDGEGAARAMRAALADAGLSPEDI 295
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
1-67 |
3.64e-03 |
|
"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: 38.96 E-value: 3.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1897357996 1 MGNVLQGGEGQAPTRQAVLGAGLPIST-PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS 67
Cdd:cd00828 126 NPYVSPKWMLSPNTVAGWVNILLLSSHgPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
199-257 |
7.66e-03 |
|
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: 37.77 E-value: 7.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1897357996 199 GAAALVLMTADAAKRLNVTPLARIVAFA---DAA--VEPIDFPIAPVYAASMVLKDVGLKKEDI 257
Cdd:COG0304 232 GAGVLVLEELEHAKARGAKIYAEVVGYGassDAYhiTAPAPDGEGAARAMRAALKDAGLSPEDI 295
|
|
| |
