|
Name |
Accession |
Description |
Interval |
E-value |
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
10-327 |
4.23e-162 |
|
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: 457.33 E-value: 4.23e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY-GGVKLEDLIVKDGLTDV 88
Cdd:cd00751 67 LLAGLPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 89 YNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPdVVVKEDEEYKR-VDFSKVPK 167
Cdd:cd00751 147 FTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 168 LKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKED 247
Cdd:cd00751 226 LKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 248 IAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLI 325
Cdd:cd00751 305 IDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVI 384
|
..
gi 1897358218 326 QK 327
Cdd:cd00751 385 ER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
10-328 |
3.27e-152 |
|
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: 432.57 E-value: 3.27e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGG-VKLEDLIVKDGLTDV 88
Cdd:COG0183 71 LLAGLPESVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 89 YNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQpDVVVKEDEEYKR-VDFSKVPK 167
Cdd:COG0183 151 YTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKG-EVVVDRDEGPRPdTTLEKLAK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 168 LKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKED 247
Cdd:COG0183 230 LKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 248 IAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLI 325
Cdd:COG0183 309 IDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALII 388
|
...
gi 1897358218 326 QKL 328
Cdd:COG0183 389 ERV 391
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
13-328 |
5.28e-145 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 414.49 E-value: 5.28e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKDGLTDVYN 90
Cdd:PLN02644 73 GLPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 91 KIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV-KGQPDVVVKEDEEYKRVDFSKVPKLK 169
Cdd:PLN02644 153 DFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 170 TVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIA 249
Cdd:PLN02644 233 PSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 250 MWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 327
Cdd:PLN02644 313 YYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVEL 392
|
.
gi 1897358218 328 L 328
Cdd:PLN02644 393 M 393
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
10-326 |
2.09e-135 |
|
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: 389.66 E-value: 2.09e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTP---YGGVKLEDLIVKDgLT 86
Cdd:TIGR01930 66 LLAGLPESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 87 DVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVP 166
Cdd:TIGR01930 145 DANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 167 KLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKE 246
Cdd:TIGR01930 225 KLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSIS 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 247 DIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAML 324
Cdd:TIGR01930 304 DIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVI 383
|
..
gi 1897358218 325 IQ 326
Cdd:TIGR01930 384 LE 385
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
13-325 |
8.95e-131 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 377.96 E-value: 8.95e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN--RGSTPYGGVKLEDLIVKDGLTDVYN 90
Cdd:PRK05790 74 GLPVEVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPgsRWGQKMGDVELVDTMIHDGLTDAFN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 91 KIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDeEYKRVDFS--KVPKL 168
Cdd:PRK05790 154 GYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTD-EHPRPDTTaeSLAKL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 169 KTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDI 248
Cdd:PRK05790 233 RPAF-DKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADL 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897358218 249 AMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLI 325
Cdd:PRK05790 312 DLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKrrGAKKGLATLCIGGGQGVALIV 390
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
13-326 |
1.55e-122 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 357.10 E-value: 1.55e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY--GGVKLEDLIVKDGLTDVYN 90
Cdd:PRK08235 74 GIPWEVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYrmGDNEVIDLMVADGLTCAFS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 91 KIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVT-VKGQPDVVVKEDEEYKRVDFSKVPKLK 169
Cdd:PRK08235 154 GVHMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPqRKGDPIVVAKDEAPRKDTTIEKLAKLK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 170 TVFQKEnGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIA 249
Cdd:PRK08235 234 PVFDKT-GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDID 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897358218 250 MWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 326
Cdd:PRK08235 313 LFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrgGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
13-328 |
1.22e-99 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 298.80 E-value: 1.22e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKdGLTDVYN 90
Cdd:PRK09051 76 GVPQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpaARWGARMGDAKLVDMMVG-ALHDPFG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 91 KIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV-TVKGqpDVVVKEDEEYKR-VDFSKVPKL 168
Cdd:PRK09051 155 TIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIkTRKG--EVVFDTDEHVRAdTTLEDLAKL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 169 KTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDI 248
Cdd:PRK09051 233 KPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 249 AMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLIQ 326
Cdd:PRK09051 313 DVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQriGGRYALVTMCIGGGQGIAAIFE 392
|
..
gi 1897358218 327 KL 328
Cdd:PRK09051 393 RL 394
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
13-326 |
3.83e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 290.26 E-value: 3.83e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKDGLTDVYN 90
Cdd:PRK06954 79 GLPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpkARGGMRMGHGQVLDHMFLDGLEDAYD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 91 KIH-MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQpDVVVKEDEEYKRVDFSKVPKLK 169
Cdd:PRK06954 159 KGRlMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKG-DTVIDRDEQPFKANPEKIPTLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 170 TVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIA 249
Cdd:PRK06954 238 PAFSK-TGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVD 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897358218 250 MWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 326
Cdd:PRK06954 317 LFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRArgGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
10-328 |
2.90e-92 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 280.30 E-value: 2.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYG-GVKLEDL-----IVKD 83
Cdd:PRK09050 73 LLAGLPVSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSrQAEIFDTtigwrFVNP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 84 GLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEeYKRVDFS 163
Cdd:PRK09050 153 LMKAQYGVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDE-HPRPETT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 164 --KVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDV 241
Cdd:PRK09050 232 leALAKLKPVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 242 GLKKEDIAMWEVNEAFSLVVLANIKMLEI--DPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGG 317
Cdd:PRK09050 311 GLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTMCIGV 390
|
330
....*....|.
gi 1897358218 318 GGASAMLIQKL 328
Cdd:PRK09050 391 GQGIALAIERV 401
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
13-327 |
7.77e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 266.37 E-value: 7.77e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKDGLTDVYN 90
Cdd:PRK05656 74 GLPHSVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLpgARTGLRMGHAQLVDSMITDGLWDAFN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 91 KIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV-TVKGQPDVVVKEDEEYKRVDFSKVPKLK 169
Cdd:PRK05656 154 DYHMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIpQRKGEPLAFATDEQPRAGTTAESLAKLK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 170 TVFQKEnGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIA 249
Cdd:PRK05656 234 PAFKKD-GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 250 MWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQK 327
Cdd:PRK05656 313 LIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMirRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
13-326 |
1.10e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 260.73 E-value: 1.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS---NVPYVmnRGSTPYGGVKLEDLIVKDGLTDVY 89
Cdd:PRK06633 75 GIPKEVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI--RAGAKFGDIKMVDLMQYDGLTDVF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 90 NKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLK 169
Cdd:PRK06633 153 SGVFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 170 TVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIA 249
Cdd:PRK06633 233 PAFDK-NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLE 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897358218 250 MWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLIQ 326
Cdd:PRK06633 312 VIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRraKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
10-318 |
1.73e-82 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 255.30 E-value: 1.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN--RGSTPYGGVKLEDLIVKDGLT- 86
Cdd:PRK06205 71 LDAGLPVTVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQLHDRLARGRETa 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 87 --DVYNKIH-MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYkRVDFS 163
Cdd:PRK06205 151 ggRRFPVPGgMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHP-RADTT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 164 --KVPKLKTVFQK--ENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLK 239
Cdd:PRK06205 230 leSLAKLRPIMGKqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 240 DVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQ---KVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASIC 314
Cdd:PRK06205 310 RAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQrrQARYGLETMC 389
|
....
gi 1897358218 315 NGGG 318
Cdd:PRK06205 390 IGGG 393
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
10-327 |
2.40e-81 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 251.95 E-value: 2.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVY 89
Cdd:PRK06445 78 FLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNPKLLTDPKYIEYDLTTGY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 90 NkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLK 169
Cdd:PRK06445 158 V---MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 170 TVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIA 249
Cdd:PRK06445 235 PAF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDID 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 250 MWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQK 327
Cdd:PRK06445 314 LWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLqiKGKDYGVATLCVGGGQGGAVVLER 393
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
10-328 |
6.47e-80 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 248.76 E-value: 6.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGS-TPYGGVKLEDLIVKDGltdv 88
Cdd:PRK09052 78 LLAGLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSmSPAIFARDENVGIAYG---- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 89 ynkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKgQPD-----VVVKEDE----EYKR 159
Cdd:PRK09052 154 -----MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITER-FPDlatgeVDVKTRTvdldEGPR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 160 VDFS--KVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMV 237
Cdd:PRK09052 228 ADTSleGLAKLKPVFANK-GSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 238 LKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICN 315
Cdd:PRK09052 307 LKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMVTMCV 386
|
330
....*....|...
gi 1897358218 316 GGGGASAMLIQKL 328
Cdd:PRK09052 387 GTGMGAAGIFERL 399
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
10-200 |
9.08e-80 |
|
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: 243.36 E-value: 9.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN---RGSTPYGGVKLEDLIVKDGLT 86
Cdd:pfam00108 68 LKAGIPDSAPAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 87 DVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVP 166
Cdd:pfam00108 148 DAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLA 227
|
170 180 190
....*....|....*....|....*....|....
gi 1897358218 167 KLKTVFQKEnGTVTAANASTLNDGAAALVLMTAD 200
Cdd:pfam00108 228 KLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
10-328 |
6.19e-76 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 238.13 E-value: 6.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGstpyggvKLEDLIVKDGLTDVY 89
Cdd:PRK07108 73 LRAGLPVTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRH-------MLREGWLVEHKPEIY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 90 nkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQ---------PDVVVKEDEEYkRV 160
Cdd:PRK07108 146 --WSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVAdkatgrlftKEVTVSADEGI-RP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 161 DFSK--VPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVL 238
Cdd:PRK07108 223 DTTLegVSKIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 239 KDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGhltHALKQGE-----YGLASI 313
Cdd:PRK07108 301 KQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTG---HALIEGKrrgakYVVVTM 377
|
330
....*....|....*
gi 1897358218 314 CNGGGGASAMLIQKL 328
Cdd:PRK07108 378 CIGGGQGAAGLFEVL 392
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
18-328 |
6.77e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 239.15 E-value: 6.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 18 TPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY---------GGVKLEDL--------- 79
Cdd:PRK08170 80 VPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWlagwyaaksIGQKLAALgklrpsyla 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 80 ----IVKdGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGnEVIPVtVTVKGQpdvvVKEDE 155
Cdd:PRK08170 160 pvigLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL-FDRDGK----FYDHD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 156 EYKRVDFS--KVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYA 233
Cdd:PRK08170 233 DGVRPDSSmeKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 234 ASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EIDPQKVNINGGAVSLGHPIGMSGARIV 296
Cdd:PRK08170 313 ATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWadeeycreqlgldgalgELDRERLNVDGGAIALGHPVGASGARIV 392
|
330 340 350
....*....|....*....|....*....|....
gi 1897358218 297 GHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 328
Cdd:PRK08170 393 LHLLHALKRrgTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
11-322 |
1.31e-74 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 234.64 E-value: 1.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 11 LQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVmnrgstpyGGVKLEDLIVKDGLTDVYn 90
Cdd:PRK07661 74 LAGLPYTVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--------GHVVRPNPRLVEAAPEYY- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 91 kIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV-------KGQPDVVVKEDEEYKRVDFS 163
Cdd:PRK07661 145 -MGMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLrtvgennKLQEETITFSQDEGVRADTT 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 164 K--VPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDV 241
Cdd:PRK07661 224 LeiLGKLRPAFNV-KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 242 GLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK-QGE-YGLASICNGGGG 319
Cdd:PRK07661 303 GLELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKrRNEqFGIVTMCIGGGM 382
|
...
gi 1897358218 320 ASA 322
Cdd:PRK07661 383 GAA 385
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
19-328 |
1.39e-74 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 235.28 E-value: 1.39e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 19 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNvpYVM-NRGSTP-------------------YGGVKLED 78
Cdd:PRK07851 82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSR--FAKgNSDSLPdtknplfaeaqartaaraeGGAEAWHD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 79 LIVKDGLTDVYnkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvkgqPD--VVVKEDEE 156
Cdd:PRK07851 160 PREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL-----PDgtVVSTDDGP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 157 YKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASM 236
Cdd:PRK07851 233 RAGTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 237 VLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASIC 314
Cdd:PRK07851 312 ALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQthDKTFGLETMC 391
|
330
....*....|....
gi 1897358218 315 NGGGGASAMLIQKL 328
Cdd:PRK07851 392 VGGGQGMAMVLERL 405
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
13-326 |
3.76e-74 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 233.36 E-value: 3.76e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNR------GSTPYGGVKLEDLIVKDGLT 86
Cdd:PRK06366 74 GLPFGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSdlrwgpKHLLHKNYKIDDAMLVDGLI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 87 DVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvkgqpdvvVKEDEEYKRVDFSKVP 166
Cdd:PRK06366 154 DAFYFEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND---------LDRDEGIRKTTMEDLA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 167 KLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKE 246
Cdd:PRK06366 225 KLPPAFDK-NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSID 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 247 DIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQG--EYGLASICNGGGGASAML 324
Cdd:PRK06366 304 YYDLVEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRhmKTGLATLCHGGGGAHTLT 383
|
..
gi 1897358218 325 IQ 326
Cdd:PRK06366 384 LE 385
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
10-327 |
1.65e-73 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 232.36 E-value: 1.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGgvklEDLIVKDG----- 84
Cdd:PRK08131 72 LLAGLPVTVPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFS----RDAKVFDTtigar 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 85 -----LTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV-TVKGQPDVVVKEDEEYK 158
Cdd:PRK08131 148 fpnpkIVAQYGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVpQGRKLPPKLVAEDEHPR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 159 -RVDFSKVPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMV 237
Cdd:PRK08131 228 pSSTVEALTKLKPLF--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 238 LKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEI--DPQKVNINGGAVSLGHPIGMSGARIVghLTHA----LKQGEYGLA 311
Cdd:PRK08131 306 LARAGLTLDDMDIIEINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLA--LTAArelqRRGKRYAVV 383
|
330
....*....|....*.
gi 1897358218 312 SICNGGGGASAMLIQK 327
Cdd:PRK08131 384 SLCIGVGQGLAMVIER 399
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
10-328 |
1.70e-72 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 229.08 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMNRGSTPYggvkledlivkDGLTDVY 89
Cdd:PRK08947 74 LLAGIPHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--MNHGVDFH-----------PGLSKNV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 90 NKIH--MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkGQpdvvvKEDEEYKRVDFSKV-- 165
Cdd:PRK08947 141 AKAAgmMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTE----GH-----DADGVLKLFDYDEVir 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 166 --------PKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMV 237
Cdd:PRK08947 212 pettvealAALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 238 LKDVGLKKEDIAMWEVNEAF---SLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLAS 312
Cdd:PRK08947 292 LKRAGLSISDIDVFELNEAFaaqSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERkdAQFGLAT 371
|
330
....*....|....*.
gi 1897358218 313 ICNGGGGASAMLIQKL 328
Cdd:PRK08947 372 MCIGLGQGIATVFERV 387
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
10-328 |
3.42e-72 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 228.05 E-value: 3.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP--YVMNRG-----STPYGGVKledlivk 82
Cdd:PRK07801 72 LAAGLPEEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPisSAMTAGeqlgfTSPFAESK------- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 83 dGLTDVYNK--IHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkgqpDVVVkeDEEYKRV 160
Cdd:PRK07801 145 -GWLHRYGDqeVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG-------GVTV--DEGPRET 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 161 DFSKVPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKD 240
Cdd:PRK07801 215 SLEKMAGLKPLV--EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 241 VGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGG 318
Cdd:PRK07801 293 TGLSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERtgGRYGLQTMCEGGG 372
|
330
....*....|
gi 1897358218 319 GASAMLIQKL 328
Cdd:PRK07801 373 TANVTIIERL 382
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
10-328 |
6.61e-71 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 224.99 E-value: 6.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMNRGSTpyggvkledLIVKDGLTDV- 88
Cdd:PRK06504 72 LASKLPESVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP--MGSPST---------LPAKNGLGHYk 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 89 -------YNKIH----MGscAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEY 157
Cdd:PRK06504 141 spgmeerYPGIQfsqfTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 158 kRVDFS--KVPKLKTVfqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAAS 235
Cdd:PRK06504 219 -RFDATleGIAGVKLI--AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 236 MVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASI 313
Cdd:PRK06504 296 RALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQrgKRYGLQTM 375
|
330
....*....|....*
gi 1897358218 314 CNGGGGASAMLIQKL 328
Cdd:PRK06504 376 CEGGGMANVTIVERL 390
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
13-326 |
1.97e-67 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 217.16 E-value: 1.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP-----------YVMNRGST------PYGGVK 75
Cdd:PRK08963 77 GMNVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaralVDLNKARTlgqrlkLFSRLR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 76 LEDLI-VKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQP---DVVV 151
Cdd:PRK08963 157 LRDLLpVPPAVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPleeDNNI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 152 KEDEeykrvDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPI-DFPIAP 230
Cdd:PRK08963 237 RGDS-----TLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWqDMLLGP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 231 VYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EIDPQKVNINGGAVSLGHPIGMSGA 293
Cdd:PRK08963 312 AYATPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGA 391
|
330 340 350
....*....|....*....|....*....|....*
gi 1897358218 294 RIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 326
Cdd:PRK08963 392 RMITQTLHELRRrgGGLGLTTACAAGGLGAAMVLE 426
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
10-324 |
6.15e-67 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 216.55 E-value: 6.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyggvKLEDL-IVKDGLtdv 88
Cdd:PLN02287 117 FYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNP----RVESFsQAQDCL--- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 89 ynkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV------TVKGQPDVVVKEDEEYKRVDF 162
Cdd:PLN02287 190 ---LPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTkivdpkTGEEKPIVISVDDGIRPNTTL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 163 SKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVG 242
Cdd:PLN02287 267 ADLAKLKPVF-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 243 LKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ----GEYGLASICNGGG 318
Cdd:PLN02287 346 LELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgkdCRFGVVSMCIGTG 425
|
....*..
gi 1897358218 319 -GASAML 324
Cdd:PLN02287 426 mGAAAVF 432
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
10-328 |
2.22e-66 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 213.98 E-value: 2.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyggvkledliVKDGLTDVY 89
Cdd:PRK08242 74 LAAGLPETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWA----------MDPSTNFPT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 90 NKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVtvtvKGQPDVVVKEDEEYKR--VDFSKVPK 167
Cdd:PRK08242 144 YFVPQGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV----KDQNGLTILDHDEHMRpgTTMESLAK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 168 LKTVFQ--------------------KENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFP 227
Cdd:PRK08242 220 LKPSFAmmgemggfdavalqkypeveRINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIML 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 228 IAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQ 305
Cdd:PRK08242 300 TGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELerRG 379
|
330 340
....*....|....*....|...
gi 1897358218 306 GEYGLASICNGGGGASAMLIQKL 328
Cdd:PRK08242 380 KRTALITLCVGGGMGIATIIERV 402
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
10-328 |
3.20e-64 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 207.65 E-value: 3.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyGGVKLEDLIVkdgltDVY 89
Cdd:PRK07850 72 LHAGLPYHVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGR-GLPRPDSWDI-----DMP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 90 NKIhmgSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV---KGQP---DVVVKEDEEYKRVDFS 163
Cdd:PRK07850 146 NQF---EAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVldeEGQPtgeTRLVTRDQGLRDTTME 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 164 KVPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGL 243
Cdd:PRK07850 223 GLAGLKPVL--EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGM 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 244 KKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGAS 321
Cdd:PRK07850 301 KIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERtdKSTALITMCAGGALST 380
|
....*..
gi 1897358218 322 AMLIQKL 328
Cdd:PRK07850 381 GTIIERI 387
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
10-328 |
1.48e-61 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 199.99 E-value: 1.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 10 LLQGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyggvkledlivkdgltDVY 89
Cdd:PRK06690 65 LEAGLGLHIPGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSP----------------ETI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 90 NKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkGQPDVVVKEDEEYKRVdfskVPKLK 169
Cdd:PRK06690 129 GDPDMGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN----GLLDESIKKEMNYERI----IKRTK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 170 TVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIA 249
Cdd:PRK06690 201 PAFLH-NGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDID 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 250 MWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 327
Cdd:PRK06690 280 YFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKRedMKYGIATLGIGGGIGLALLFEK 359
|
.
gi 1897358218 328 L 328
Cdd:PRK06690 360 V 360
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
207-327 |
1.90e-60 |
|
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: 189.39 E-value: 1.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 207 VTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGH 286
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1897358218 287 PIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 327
Cdd:pfam02803 81 PLGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
13-328 |
6.17e-54 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 181.90 E-value: 6.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS----NVPYVMNRGSTPYGgvkledliVKDG---L 85
Cdd:PRK06025 78 GYDIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaaMAAEDMAAGKPPLG--------MGSGnlrL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 86 TDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkgQPDVVVKED-EEYKRVDFSK 164
Cdd:PRK06025 150 RALHPQSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY-----RDDGSVALDhEEFPRPQTTA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 165 --VPKLKTVFQK-------ENGTV------------------TAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFA 217
Cdd:PRK06025 225 egLAALKPAFTAiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 218 DAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVG 297
Cdd:PRK06025 305 NMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIG 384
|
330 340 350
....*....|....*....|....*....|...
gi 1897358218 298 HLTHALKQ--GEYGLASICNGGGGASAMLIQKL 328
Cdd:PRK06025 385 TVLDELERrgLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
13-327 |
3.99e-44 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 156.21 E-value: 3.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYV-----------MNRGSTPYGGVKL----- 76
Cdd:PRK09268 79 ALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAvneglrkilleLNRAKTTGDRLKAlgklr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 77 -EDLIV--------KDGLTdvynkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVtvtvKGqp 147
Cdd:PRK09268 159 pKHLAPeiprngepRTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF----LG-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 148 dvvVKEDEEYkRVDFS--KVPKLKTVFQK-ENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPI 224
Cdd:PRK09268 226 ---LTRDNNL-RPDSSleKLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDFV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 225 DFP----IAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLE-----------------IDPQKVNINGGAVS 283
Cdd:PRK09268 302 HGKegllMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEdeeycrerlgldaplgsIDRSKLNVNGSSLA 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1897358218 284 LGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQK 327
Cdd:PRK09268 382 AGHPFAATGGRIVATLAKLLaeKGSGRGLISICAAGGQGVTAILER 427
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
13-326 |
2.83e-38 |
|
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: 139.94 E-value: 2.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 13 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvmnrgstpyggvklEDLIVKDGLTDVYNKI 92
Cdd:cd00826 71 GGLQEAPAIGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSA---------------ENNAKEKHIDVLINKY 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 93 HMgscaentakklniaRNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvKGQPDVVVKEDEEYKR----VDFSKVPKL 168
Cdd:cd00826 136 GM--------------RACPDAFALAGQAGAEAAEKDGRFKDEFAKFGV--KGRKGDIHSDADEYIQfgdeASLDEIAKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 169 KTVFQKEnGTVTAANASTLNDGAAALVLMTADAA-------KRLNVTPLARIVAFADAAVEPIDFPIA----PVYAASMV 237
Cdd:cd00826 200 RPAFDKE-DFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVggdgPIEAARKA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 238 LKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQK------------------VNINGGAVSLGHPIGMSGARIVGHL 299
Cdd:cd00826 279 LEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAEL 358
|
330 340 350
....*....|....*....|....*....|....
gi 1897358218 300 THALKQGEY-------GLASICNGGGGASAMLIQ 326
Cdd:cd00826 359 CFELKGEAGkrqgagaGLALLCIGGGGGAAMCIE 392
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
181-325 |
4.84e-14 |
|
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: 70.94 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 181 AANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI----APVYAASMVLKDVGLKKEDIAMWEVNEA 256
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 257 FSLVVLANIKMLEIDPQKV---NINGGAVSLGHPIGMSGARIVGHLTHALKQGEY---------GLASICNGGGGASAML 324
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIpptpreprtVLLLGFGLGGTNAAVV 253
|
.
gi 1897358218 325 I 325
Cdd:cd00327 254 L 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
19-322 |
2.68e-12 |
|
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: 66.90 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 19 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyGGVKLEDLIVKDGLT--DVYNKI---H 93
Cdd:cd00829 69 PATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRA-SDLEWEGPEPPGGLTppALYALAarrY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 94 M---GSCAENTAKklnIARNEQDAYAINSYtrskaAWEAGkfgneviPVTV-TVKGQPDVVvkedEEYKRVDFSKVpklk 169
Cdd:cd00829 148 MhryGTTREDLAK---VAVKNHRNAARNPY-----AQFRK-------PITVeDVLNSRMIA----DPLRLLDCCPV---- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 170 tvfqkengtvtaanastlNDGAAALVLMTADAAKRLNVTPlARIVAFADA-------AVEPIDFPIAPVYAASMVLKDVG 242
Cdd:cd00829 205 ------------------SDGAAAVVLASEERARELTDRP-VWILGVGAAsdtpslsERDDFLSLDAARLAARRAYKMAG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 243 LKKEDIAMWEVNEAFSLVVLANIKML---------------EIDPQ---KVNINGGAVSLGHPIGMSGARIVGHLTHALK 304
Cdd:cd00829 266 ITPDDIDVAELYDCFTIAELLALEDLgfcekgeggklvregDTAIGgdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLR 345
|
330 340
....*....|....*....|....*.
gi 1897358218 305 qGEYG--------LASICNGGGGASA 322
Cdd:cd00829 346 -GEAGarqvpgarVGLAHNIGGTGSA 370
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
19-322 |
8.60e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 52.98 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 19 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP---------------YVMNRGSTPyggvkledlivkD 83
Cdd:PRK06064 77 PATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPtpdateaiaragdyeWEEFFGATF------------P 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 84 GLTDVYNKIHM---GSCAENTAKklnIARNEQDAYAINSYtrskaaweaGKFGNEvipVTVtvkgqpDVVVKEdeeykrv 160
Cdd:PRK06064 145 GLYALIARRYMhkyGTTEEDLAL---VAVKNHYNGSKNPY---------AQFQKE---ITV------EQVLNS------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 161 dfSKVPKLKTVFqkengtvtaaNASTLNDGAAALVLMTADAAKRLNVTPLaRIVAFADAavepIDFPI-----------A 229
Cdd:PRK06064 197 --PPVADPLKLL----------DCSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQA----SDTIAlhdrkdfttldA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 230 PVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EIDPQ-KVNINGGAVSLGHPIGMS 291
Cdd:PRK06064 260 AVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLgfakkgeggklaregqtYIGGDiPVNPSGGLKAKGHPVGAT 339
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1897358218 292 GARIVGHLTHALKQG-----------EYGLASicN-GGGGASA 322
Cdd:PRK06064 340 GVSQAVEIVWQLRGEaekgrqqvigaGYGLTH--NvGGTGHTA 380
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
185-296 |
1.51e-07 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 52.34 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 185 STLNDGAAALVLMTADAAKRLNVTPLARIVAFAdAAVEP--------IDFPIAP--VYAASMVLKDVGLK--KEDIAMWE 252
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGKKDPVYVKALQ-LAVSNgwelqyngWDGSYFPttRIAARKAYREAGITdpREELSMAE 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1897358218 253 VNEAFSLVVLANIKMLEIDPQ------------------KVNINGGAVSLGHPIGMSGARIV 296
Cdd:PRK06157 293 VHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
12-59 |
8.94e-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: 46.76 E-value: 8.94e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1897358218 12 QGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSN 59
Cdd:cd00834 146 IRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
19-64 |
1.57e-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: 46.24 E-value: 1.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1897358218 19 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNvPYVM 64
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT-PLGL 197
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
19-56 |
3.83e-05 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 45.16 E-value: 3.83e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1897358218 19 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMES 56
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
19-72 |
1.85e-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: 42.24 E-value: 1.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1897358218 19 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSN----VPYVMNRGSTPYG 72
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTplgfAGFSAAGMLSPDG 222
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
185-313 |
4.99e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 41.42 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358218 185 STLNDGAAALVLMTADAAKRLNVTP----LARIVAFADAAVEPIDFP------IAPVYAASMVLKDVGLKKEDIAMWEVN 254
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASGNLYEDPpdatrmFTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897358218 255 EAFSLVVLANIKMLEI-DPQK-----------------VNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASI 313
Cdd:PTZ00455 336 DCFTIAELLMYEALGIaEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGqcGEYQMKNI 414
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
187-248 |
1.54e-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: 39.83 E-value: 1.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1897358218 187 LNDGAAALVLMTADAAKRLNVTPLARIVAFA---DAA--VEPIDFPIAPVYAASMVLKDVGLKKEDI 248
Cdd:cd00834 229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGassDAYhiTAPDPDGEGAARAMRAALADAGLSPEDI 295
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
19-58 |
3.48e-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: 3.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1897358218 19 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS 58
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
190-248 |
4.59e-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: 38.54 E-value: 4.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1897358218 190 GAAALVLMTADAAKRLNVTPLARIVAFA---DAA--VEPIDFPIAPVYAASMVLKDVGLKKEDI 248
Cdd:COG0304 232 GAGVLVLEELEHAKARGAKIYAEVVGYGassDAYhiTAPAPDGEGAARAMRAALKDAGLSPEDI 295
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
11-58 |
6.51e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 38.05 E-value: 6.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1897358218 11 LQGLPISTPCTtinkvCASGMKAIMMASQSLMCGHQDVMVAGGMESMS 58
Cdd:PRK09116 153 LKGRVIPTSSA-----CTSGSQGIGYAYEAIKYGYQTVMLAGGAEELC 195
|
|
| |
