|
Name |
Accession |
Description |
Interval |
E-value |
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
49-432 |
0e+00 |
|
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: 541.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 49 VIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPCTTV 128
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 129 NKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPY-GGVKLEDLIVKDGLTDVYNKIHMGNCAENTA 207
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 208 KKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKGKPdVLVTEDEEYKR-VDFSKVPKLKTVFqKENGTVTA 286
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 287 ANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEAFSLVV 366
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953386780 367 LANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLIQK 432
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
47-433 |
0e+00 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 522.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 47 EVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPCT 126
Cdd:PLN02644 2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 127 TVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 204
Cdd:PLN02644 82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 205 NTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTT-KGKPDVLVTEDEEYKRVDFSKVPKLKTVFQKENGT 283
Cdd:PLN02644 162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 284 VTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEAFS 363
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953386780 364 LVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLIQKL 433
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
46-433 |
0e+00 |
|
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: 513.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 46 NEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPC 125
Cdd:COG0183 2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 126 TTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGG-VKLEDLIVKDGLTDVYNKIHMGNCAE 204
Cdd:COG0183 82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 205 NTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKgKPDVLVTEDEEYKR-VDFSKVPKLKTVFqKENGT 283
Cdd:COG0183 162 NVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDR-KGEVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 284 VTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEAFS 363
Cdd:COG0183 240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953386780 364 LVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLIQKL 433
Cdd:COG0183 320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
46-430 |
1.89e-169 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 480.80 E-value: 1.89e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 46 NEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPC 125
Cdd:PRK05790 2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 126 TTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCA 203
Cdd:PRK05790 82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLpgSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 204 ENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKGKPDVLVTEDeEYKRVDFS--KVPKLKTVFqKEN 281
Cdd:PRK05790 162 ENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTD-EHPRPDTTaeSLAKLRPAF-DKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 282 GTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEA 361
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953386780 362 FSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALK--QGEYGLASICNGGGGASALLI 430
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKrrGAKKGLATLCIGGGQGVALIV 390
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
50-431 |
2.34e-163 |
|
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: 464.78 E-value: 2.34e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 50 IVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPCTTVN 129
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 130 KVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATP---YGGVKLEDLIVKDgLTDVYNKIHMGNCAENT 206
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 207 AKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKGKPDVLVTEDEEYKRVDFSKVPKLKTVFqKENGTVTA 286
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 287 ANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEAFSLVV 366
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953386780 367 LANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLIQ 431
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
47-431 |
6.15e-153 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 438.76 E-value: 6.15e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 47 EVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPCT 126
Cdd:PRK08235 3 KTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 127 TVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPY--GGVKLEDLIVKDGLTDVYNKIHMGNCAE 204
Cdd:PRK08235 83 TVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYrmGDNEVIDLMVADGLTCAFSGVHMGVYGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 205 NTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTT-KGKPdvLVTEDEEYKRVDFS--KVPKLKTVFQKEn 281
Cdd:PRK08235 163 EVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQrKGDP--IVVAKDEAPRKDTTieKLAKLKPVFDKT- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 282 GTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEA 361
Cdd:PRK08235 240 GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953386780 362 FSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLIQ 431
Cdd:PRK08235 320 FAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrgGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
46-431 |
3.41e-125 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 368.45 E-value: 3.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 46 NEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPC 125
Cdd:PRK06954 7 DPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 126 TTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVKDGLTDVYNKIH-MGNC 202
Cdd:PRK06954 87 TTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpkARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 203 AENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKgKPDVLVTEDEEYKRVDFSKVPKLKTVFQKeNG 282
Cdd:PRK06954 167 AEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGK-KGDTVIDRDEQPFKANPEKIPTLKPAFSK-TG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 283 TVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEAF 362
Cdd:PRK06954 245 TVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAF 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953386780 363 SLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLIQ 431
Cdd:PRK06954 325 AVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRArgGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
46-433 |
1.74e-119 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 353.50 E-value: 1.74e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 46 NEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLqggegqaPT--------RQAALGA 117
Cdd:PRK09051 3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVI-------PTeprdmylsRVAAINA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 118 GLPISTPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVkDGLTDVYN 195
Cdd:PRK09051 76 GVPQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpaARWGARMGDAKLVDMMV-GALHDPFG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 196 KIHMGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKgKPDVLVTEDEEYKR-VDFSKVPKLK 274
Cdd:PRK09051 155 TIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTR-KGEVVFDTDEHVRAdTTLEDLAKLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 275 TVFQKENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDIT 354
Cdd:PRK09051 234 PVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 355 MWEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALK--QGEYGLASICNGGGGASALLIQK 432
Cdd:PRK09051 314 VIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQriGGRYALVTMCIGGGQGIAAIFER 393
|
.
gi 1953386780 433 L 433
Cdd:PRK09051 394 L 394
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
48-305 |
1.19e-116 |
|
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: 341.59 E-value: 1.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 48 VVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPCTT 127
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 128 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMS---RGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 204
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 205 NTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKGKPDVLVTEDEEYKRVDFSKVPKLKTVFQKEnGTV 284
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTV 239
|
250 260
....*....|....*....|.
gi 1953386780 285 TAANASTLNDGAAAVVLMTAD 305
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
45-432 |
1.19e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 336.09 E-value: 1.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 45 LNEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTP 124
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 125 CTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNC 202
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLpgARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 203 AENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTV-TTKGKPDVLVTEDEEYKRVDFSKVPKLKTVFQKEn 281
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIpQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 282 GTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEA 361
Cdd:PRK05656 240 GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953386780 362 FSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHAL--KQGEYGLASICNGGGGASALLIQK 432
Cdd:PRK05656 320 FAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMirRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
45-431 |
1.33e-101 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 307.71 E-value: 1.33e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 45 LNEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTP 124
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 125 CTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGAT--P----YGGVKLEDLIVKDGLTDVYNKIH 198
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRwgPkhllHKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 199 MGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVttkgkpdvlVTEDEEYKRVDFSKVPKLKTVFQ 278
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND---------LDRDEGIRKTTMEDLAKLPPAFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 279 KeNGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEV 358
Cdd:PRK06366 232 K-NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEH 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953386780 359 NEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQG--EYGLASICNGGGGASALLIQ 431
Cdd:PRK06366 311 NEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRhmKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
47-423 |
1.41e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 298.05 E-value: 1.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 47 EVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPCT 126
Cdd:PRK06205 3 DAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 127 TVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMS--RGATPYGGVKLEDLIVKDGLT---DVYNKIH-MG 200
Cdd:PRK06205 83 QLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQLHDRLARGRETaggRRFPVPGgMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 201 NCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKGKPDVLVTEDEEYkRVDFS--KVPKLKTVFQ 278
Cdd:PRK06205 163 ETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHP-RADTTleSLAKLRPIMG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 279 K--ENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMW 356
Cdd:PRK06205 242 KqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLI 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953386780 357 EVNEAFS---LVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALK--QGEYGLASICNGGG 423
Cdd:PRK06205 322 ELNEAFAaqvLAVLKEWGFGADDEERLNVNGSGISLGHPVGATGGRILATLLRELQrrQARYGLETMCIGGG 393
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
45-433 |
5.20e-97 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 296.48 E-value: 5.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 45 LNEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEK-AGIPKEEVKEAYMGNVLQGGE-GQAPTRQAALGAGLPIS 122
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 123 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYG-GVKLEDL-----IVKDGLTDVYNK 196
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSrQAEIFDTtigwrFVNPLMKAQYGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 197 IHMGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKgKPDVLVTEDEEYKRVDFS--KVPKLK 274
Cdd:PRK09050 161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQK-KGDPVVVDRDEHPRPETTleALAKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 275 TVFqKENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDIT 354
Cdd:PRK09050 240 PVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 355 MWEVNEAFSLVVLANIKMLDL--DPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLI 430
Cdd:PRK09050 319 VIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTMCIGVGQGIALAI 398
|
...
gi 1953386780 431 QKL 433
Cdd:PRK09050 399 ERV 401
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
45-431 |
2.07e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 294.63 E-value: 2.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 45 LNEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTP 124
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 125 CTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS---NVPYVmsRGATPYGGVKLEDLIVKDGLTDVYNKIHMGN 201
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI--RAGAKFGDIKMVDLMQYDGLTDVFSGVFMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 202 CAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKgKPDVLVTEDEEYK-RVDFSKVPKLKTVFQKe 280
Cdd:PRK06633 160 TAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIK-KTTSLFDHDETVRpDTSLEILSKLRPAFDK- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 281 NGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNE 360
Cdd:PRK06633 238 NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953386780 361 AFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALK--QGEYGLASICNGGGGASALLIQ 431
Cdd:PRK06633 318 AFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRraKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
45-428 |
5.47e-86 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 267.79 E-value: 5.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 45 LNEVVIVSAARTPIG-SFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVL-QGGEGQAPTRQAALGAGLPIS 122
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANpEGATGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 123 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGatpyggvKLEDLIVKDGLTDVYnkIHMGNC 202
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRH-------MLREGWLVEHKPEIY--WSMLQT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 203 AENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTK---------GKPDVLVTEDEEYkRVDFSK--VP 271
Cdd:PRK07108 152 AENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGvadkatgrlFTKEVTVSADEGI-RPDTTLegVS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 272 KLKTVFqkENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKE 351
Cdd:PRK07108 231 KIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 352 DITMWEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVH-LVHALKQG-EYGLASICNGGG-GASAL 428
Cdd:PRK07108 309 DIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHaLIEGKRRGaKYVVVTMCIGGGqGAAGL 388
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
47-433 |
5.10e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 262.34 E-value: 5.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 47 EVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGeGQAP--TRQAALGAGLPISTP 124
Cdd:PRK07801 3 EAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQAGniARTSWLAAGLPEEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 125 CTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGA-------TPYGGVKledlivkdGLTDVYNK- 196
Cdd:PRK07801 82 GVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAgeqlgftSPFAESK--------GWLHRYGDq 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 197 -IHMGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVttkgkpdvlVTEDEEYKRVDFSKVPKLKT 275
Cdd:PRK07801 154 eVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPRETSLEKMAGLKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 276 VFqkENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITM 355
Cdd:PRK07801 225 LV--EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 356 WEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLIQKL 433
Cdd:PRK07801 303 VEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERtgGRYGLQTMCEGGGTANVTIIERL 382
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
50-432 |
7.01e-84 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 262.79 E-value: 7.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 50 IVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAALGAGLPISTPCTTV 128
Cdd:PRK08131 6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 129 NKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGgvklEDLIVKDG----------LTDVYNKIH 198
Cdd:PRK08131 86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFS----RDAKVFDTtigarfpnpkIVAQYGNDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 199 MGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKGK-PDVLVTEDEEYK-RVDFSKVPKLKTV 276
Cdd:PRK08131 162 MPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKlPPKLVAEDEHPRpSSTVEALTKLKPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 277 FqkENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMW 356
Cdd:PRK08131 242 F--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDII 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 357 EVNEAFSLVVLANIKMLDL--DPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALK--QGEYGLASICNGGGGASALLIQK 432
Cdd:PRK08131 320 EINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQrrGKRYAVVSLCIGVGQGLAMVIER 399
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
46-429 |
1.03e-82 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 261.24 E-value: 1.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 46 NEVVIVSAARTPI-GSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQA-PTRQAALGAGLPIST 123
Cdd:PLN02287 46 DDVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnECRMAAFYAGFPETV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 124 PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPyggvKLEDL-IVKDGLtdvynkIHMGNC 202
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNP----RVESFsQAQDCL------LPMGIT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 203 AENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTV------TTKGKPDVLVTEDEEYKRVDFSKVPKLKTV 276
Cdd:PLN02287 196 SENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTkivdpkTGEEKPIVISVDDGIRPNTTLADLAKLKPV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 277 FqKENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMW 356
Cdd:PLN02287 276 F-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLF 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953386780 357 EVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ----GEYGLASICNGGG-GASALL 429
Cdd:PLN02287 355 EINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgkdCRFGVVSMCIGTGmGAAAVF 432
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
45-427 |
3.00e-81 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 255.45 E-value: 3.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 45 LNEVVIVSAARTPIG-SFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAALGAGLPIS 122
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEqGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 123 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVmsrgatpyGGVKLEDLIVKDGLTDVYnkIHMGNC 202
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--------GHVVRPNPRLVEAAPEYY--MGMGHT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 203 AENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTK-----GKP---DVLVTEDEEYkRVDFSK--VPK 272
Cdd:PRK07661 151 AEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRtvgenNKLqeeTITFSQDEGV-RADTTLeiLGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 273 LKTVFQKeNGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKED 352
Cdd:PRK07661 230 LRPAFNV-KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953386780 353 ITMWEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALK-QGE-YGLASICNGGGGASA 427
Cdd:PRK07661 309 IGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKrRNEqFGIVTMCIGGGMGAA 385
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
47-433 |
4.75e-81 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 255.03 E-value: 4.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 47 EVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAALGAGLPISTPC 125
Cdd:PRK07850 3 NPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 126 TTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMSRGATPYGGvkledlivkDGLTDVYNkIHMGN---C 202
Cdd:PRK07850 83 TTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP--LGANAGPGRG---------LPRPDSWD-IDMPNqfeA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 203 AENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTT---KGKP---DVLVTEDEEYKRVDFSKVPKLKTV 276
Cdd:PRK07850 151 AERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVldeEGQPtgeTRLVTRDQGLRDTTMEGLAGLKPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 277 FqkENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEP---IDFPVApayAVPKVLRDAGLKKEDI 353
Cdd:PRK07850 231 L--EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPyyhLDGPVQ---ATAKVLEKAGMKIGDI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 354 TMWEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLIQ 431
Cdd:PRK07850 306 DLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERtdKSTALITMCAGGALSTGTIIE 385
|
..
gi 1953386780 432 KL 433
Cdd:PRK07850 386 RI 387
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
45-433 |
5.20e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 252.34 E-value: 5.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 45 LNEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEgQAPT--RQAALGAGLPIS 122
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGE-QATNvaRNAVLASKLPES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 123 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMSRGATpyggvkledLIVKDGLTDV--------Y 194
Cdd:PRK06504 80 VPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP--MGSPST---------LPAKNGLGHYkspgmeerY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 195 NKIH----MGncAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKGKPDVLVTEDEEYkRVDFS-- 268
Cdd:PRK06504 149 PGIQfsqfTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGI-RFDATle 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 269 KVPKLKTVfqKENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGL 348
Cdd:PRK06504 226 GIAGVKLI--AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGM 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 349 KKEDITMWEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGAS 426
Cdd:PRK06504 304 KIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQrgKRYGLQTMCEGGGMAN 383
|
....*..
gi 1953386780 427 ALLIQKL 433
Cdd:PRK06504 384 VTIVERL 390
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
45-432 |
2.97e-79 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 250.41 E-value: 2.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 45 LNEVVIVSAARTPIGSFLGS------LSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQA-PTRQAALGA 117
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPIFLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 118 GLPISTPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGGVKLEDLIVKDGLTDVYNki 197
Cdd:PRK06445 81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNPKLLTDPKYIEYDLTTGYV-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 198 hMGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKGKPDVLVTEDEEYKRVDFSKVPKLKTVF 277
Cdd:PRK06445 159 -MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLPPAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 278 qKENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWE 357
Cdd:PRK06445 238 -KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953386780 358 VNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHAL--KQGEYGLASICNGGGGASALLIQK 432
Cdd:PRK06445 317 INEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLqiKGKDYGVATLCVGGGQGGAVVLER 393
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
45-433 |
6.40e-77 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 244.53 E-value: 6.40e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 45 LNEVVIVSAARTPIG-SFLGSLSSLPATKLGSIAIQGVIEKA-GIPKEEVKEAYMGNVLQGGE-GQAPTRQAALGAGLPI 121
Cdd:PRK09052 5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEqGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 122 STPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGA-TPYGGVKLEDLIVKDGltdvynkihMG 200
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSmSPAIFARDENVGIAYG---------MG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 201 NCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKgKPDV----------LVTEDEEyKRVDFS-- 268
Cdd:PRK09052 156 LTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITER-FPDLatgevdvktrTVDLDEG-PRADTSle 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 269 KVPKLKTVFQKEnGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGL 348
Cdd:PRK09052 234 GLAKLKPVFANK-GSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 349 KKEDITMWEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHAL--KQGEYGLASICNGGGGAS 426
Cdd:PRK09052 313 KQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMVTMCVGTGMGA 392
|
....*..
gi 1953386780 427 ALLIQKL 433
Cdd:PRK09052 393 AGIFERL 399
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
47-433 |
1.09e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 244.14 E-value: 1.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 47 EVVIVSAARTPIG-SFLGSLSSLPATKLGSIAIQGVIEKA-GIPKEEVKEAYMGNVLQGGE-GQAPTRQAALGAGLPiST 123
Cdd:PRK07851 3 EAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYD-FL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 124 PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRG------------------ATPYGGVKLEDLI 185
Cdd:PRK07851 82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSlpdtknplfaeaqartaaRAEGGAEAWHDPR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 186 VKDGLTDVYnkIHMGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVttkgkPD--VLVTEDEEYK 263
Cdd:PRK07851 162 EDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL-----PDgtVVSTDDGPRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 264 RVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVL 343
Cdd:PRK07851 235 GTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 344 RDAGLKKEDITMWEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALK--QGEYGLASICNG 421
Cdd:PRK07851 314 ARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQthDKTFGLETMCVG 393
|
410
....*....|..
gi 1953386780 422 GGGASALLIQKL 433
Cdd:PRK07851 394 GGQGMAMVLERL 405
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
46-433 |
1.52e-74 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 237.94 E-value: 1.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 46 NEVVIVSAARTPIG-SFLGSLSSLPATKLGSIAIQGVIEK-AGIPKEEVKEAYMGNVLQGGE-GQAPTRQAALGAGLPIS 122
Cdd:PRK08947 2 EDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLEqGFNIARNAALLAGIPHS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 123 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMSRGATPYggvkledlivkDGLTDVYNKIH--MG 200
Cdd:PRK08947 82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--MNHGVDFH-----------PGLSKNVAKAAgmMG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 201 NCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPvtvtTKGKpdvlvTEDEEYKRVDFSKV---------- 270
Cdd:PRK08947 149 LTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIP----TEGH-----DADGVLKLFDYDEVirpettveal 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 271 PKLKTVFQKENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKK 350
Cdd:PRK08947 220 AALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 351 EDITMWEVNEAF---SLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGA 425
Cdd:PRK08947 300 SDIDVFELNEAFaaqSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERkdAQFGLATMCIGLGQG 379
|
....*...
gi 1953386780 426 SALLIQKL 433
Cdd:PRK08947 380 IATVFERV 387
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
48-429 |
1.25e-73 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 236.80 E-value: 1.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 48 VVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPCTT 127
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 128 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRG-----------------ATPYGGVKLEDLI-VKDG 189
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKlaralvdlnkartlgqrLKLFSRLRLRDLLpVPPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 190 LTDVYNKIHMGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVTTKGKP---DVLVTEDEeykrvD 266
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPleeDNNIRGDS-----T 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 267 FSKVPKLKTVFQKENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPI-DFPVAPAYAVPKVLRD 345
Cdd:PRK08963 242 LEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWqDMLLGPAYATPLALER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 346 AGLKKEDITMWEVNEAFSLVVLANIKML-----------------DLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHAL 408
Cdd:PRK08963 322 AGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHEL 401
|
410 420
....*....|....*....|....
gi 1953386780 409 KQ--GEYGLASICNGGG-GASALL 429
Cdd:PRK08963 402 RRrgGGLGLTTACAAGGlGAAMVL 425
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
48-433 |
5.33e-73 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 235.30 E-value: 5.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 48 VVIVSAARTPigsFL---GSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTP 124
Cdd:PRK08170 5 VYIVDGARTP---FLkarGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 125 CTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPY---------GGVKLEDL----------- 184
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWlagwyaaksIGQKLAALgklrpsylapv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 185 --IVKdGLTDVYNKIHMGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGsEVIPVtVTTKGKpdvlVTEDEEY 262
Cdd:PRK08170 162 igLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL-FDRDGK----FYDHDDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 263 KRVDFS--KVPKLKTVFQKENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVP 340
Cdd:PRK08170 235 VRPDSSmeKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 341 KVLRDAGLKKEDITMWEVNEAFSLVVLANIKMLD-----------------LDPQKVNMNGGAVSLGHPIGMSGARIVVH 403
Cdd:PRK08170 315 PLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLH 394
|
410 420 430
....*....|....*....|....*....|..
gi 1953386780 404 LVHALKQ--GEYGLASICNGGGGASALLIQKL 433
Cdd:PRK08170 395 LLHALKRrgTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
46-433 |
3.26e-69 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 223.49 E-value: 3.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 46 NEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVieKAGIPkEEVKEAYMGNVLQGGEGQAptRQAALGAGLPISTPC 125
Cdd:PRK06690 1 NRAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGME-REIDDVILGNVVGPGGNVA--RLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 126 TTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPyggvkledlivkdgltDVYNKIHMGNCAEN 205
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSP----------------ETIGDPDMGVAAEY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 206 TAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTvttkGKPDVLVTEDEEYKRVdfskVPKLKTVFQKeNGTVT 285
Cdd:PRK06690 140 VAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN----GLLDESIKKEMNYERI----IKRTKPAFLH-NGTVT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 286 AANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEAFSLV 365
Cdd:PRK06690 211 AGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASK 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 366 VLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLIQKL 433
Cdd:PRK06690 291 VVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKRedMKYGIATLGIGGGIGLALLFEKV 360
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
47-433 |
1.03e-67 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 220.91 E-value: 1.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 47 EVVIVSAARTPIGSFL--GSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAALGAGLPIST 123
Cdd:PRK08242 3 EAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDqGADIARTAVLAAGLPETV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 124 PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPyggvkledliVKDGLTDVYNKIHMGNCA 203
Cdd:PRK08242 83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWA----------MDPSTNFPTYFVPQGISA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 204 ENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVtvttKGKPDVLVTEDEEYKR--VDFSKVPKLKTVFQ--- 278
Cdd:PRK08242 153 DLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV----KDQNGLTILDHDEHMRpgTTMESLAKLKPSFAmmg 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 279 -----------------KENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFPVAPAYAVPK 341
Cdd:PRK08242 229 emggfdavalqkypeveRINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 342 VLRDAGLKKEDITMWEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHAL--KQGEYGLASIC 419
Cdd:PRK08242 309 ALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELerRGKRTALITLC 388
|
410
....*....|....
gi 1953386780 420 NGGGGASALLIQKL 433
Cdd:PRK08242 389 VGGGMGIATIIERV 402
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
47-433 |
2.70e-56 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 191.53 E-value: 2.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 47 EVVIVSAARTP--IGSF-LGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQ-GGEGQAPTRQAALGAGLPIS 122
Cdd:PRK06025 3 EAYIIDAVRTPrgIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQrGKQGGDLGRMAALDAGYDIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 123 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS----NVPYVMSRGATPYGgvkledliVKDG---LTDVYN 195
Cdd:PRK06025 83 ASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaaMAAEDMAAGKPPLG--------MGSGnlrLRALHP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 196 KIHMGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTvttkgKPDVLVTED-EEYKRVDFSK--VPK 272
Cdd:PRK06025 155 QSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY-----RDDGSVALDhEEFPRPQTTAegLAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 273 LKTVFQK-------ENGTVT------------------AANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVE 327
Cdd:PRK06025 230 LKPAFTAiadypldDKGTTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 328 PIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGHPIGMSGARIVVHLVHA 407
Cdd:PRK06025 310 PTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDE 389
|
410 420
....*....|....*....|....*...
gi 1953386780 408 LKQ--GEYGLASICNGGGGASALLIQKL 433
Cdd:PRK06025 390 LERrgLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
312-432 |
1.42e-52 |
|
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: 172.06 E-value: 1.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 312 VKPLARVAAFADAAVEPIDFPVAPAYAVPKVLRDAGLKKEDITMWEVNEAFSLVVLANIKMLDLDPQKVNMNGGAVSLGH 391
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1953386780 392 PIGMSGARIVVHLVHALKQ--GEYGLASICNGGGGASALLIQK 432
Cdd:pfam02803 81 PLGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
51-431 |
1.67e-52 |
|
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: 180.77 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 51 VSAARTPIGSFLGSLSSL---PATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPISTPCTT 127
Cdd:cd00826 1 AGAAMTAFGKFGGENGADandLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 128 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvmsrgatpyggvklEDLIVKDGLTDVYNKIHMgncaenta 207
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSA---------------ENNAKEKHIDVLINKYGM-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 208 kkmnitREEQDTYALSSYTRSKAAWEAGRFGSEVIPVTVttKGKPDVLVTEDEEYKR----VDFSKVPKLKTVFQKEnGT 283
Cdd:cd00826 138 ------RACPDAFALAGQAGAEAAEKDGRFKDEFAKFGV--KGRKGDIHSDADEYIQfgdeASLDEIAKLRPAFDKE-DF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 284 VTAANASTLNDGAAAVVLMTADAA-------RRLKVKPLARVAAFADAAVEPIDFPVA----PAYAVPKVLRDAGLKKED 352
Cdd:cd00826 209 LTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVggdgPIEAARKALEKAGLGIGD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 353 ITMWEVNEAFSLVVLANIKMLDLDPQK------------------VNMNGGAVSLGHPIGMSGARIVVHLVHALKQGEY- 413
Cdd:cd00826 289 LDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGk 368
|
410 420
....*....|....*....|....
gi 1953386780 414 ------GLASICNGGGGASALLIQ 431
Cdd:cd00826 369 rqgagaGLALLCIGGGGGAAMCIE 392
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
43-429 |
1.38e-48 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 171.24 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 43 PTLNEVVIVSAARTPIGSFLGSLSSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPIS 122
Cdd:PRK09268 4 PTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 123 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMS-----------RGATPYGGVKL------EDLI 185
Cdd:PRK09268 84 TPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNeglrkillelnRAKTTGDRLKAlgklrpKHLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 186 V--------KDGLTdvynkihMGNCAENTAKKMNITREEQDTYALSSYTRSKAAWEAGRFGSEVIPVtvttKGkpdvlVT 257
Cdd:PRK09268 164 PeiprngepRTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF----LG-----LT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 258 EDEEYkRVDFS--KVPKLKTVFQK-ENGTVTAANASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAVEPIDFP-- 332
Cdd:PRK09268 228 RDNNL-RPDSSleKLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDFVHGKeg 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 333 --VAPAYAVPKVLRDAGLKKEDITMWEVNEAFSLVVLANIKM------------LD-----LDPQKVNMNGGAVSLGHPI 393
Cdd:PRK09268 307 llMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAwedeeycrerlgLDaplgsIDRSKLNVNGSSLAAGHPF 386
|
410 420 430
....*....|....*....|....*....|....*....
gi 1953386780 394 GMSGARIVVHLVHAL--KQGEYGLASICNGGG-GASALL 429
Cdd:PRK09268 387 AATGGRIVATLAKLLaeKGSGRGLISICAAGGqGVTAIL 425
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
77-427 |
5.75e-18 |
|
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: 85.01 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 77 AIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPIsTPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVA 156
Cdd:cd00829 23 AARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIASGLADVVLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 157 GGMESMSNVPYVMSRGATPyGGVKLEDLIVKDGLT--DVYnkihmGNCAENTAKKMNITREEqdtYALSSYTRSKA---- 230
Cdd:cd00829 102 VGAEKMSDVPTGDEAGGRA-SDLEWEGPEPPGGLTppALY-----ALAARRYMHRYGTTRED---LAKVAVKNHRNaarn 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 231 --AWEAGrfgseviPVTVTtkgkpDVLvtedeeykrvdfsKVPKLktvfqkeNGTVTAANASTLNDGAAAVVLMTADAAR 308
Cdd:cd00829 173 pyAQFRK-------PITVE-----DVL-------------NSRMI-------ADPLRLLDCCPVSDGAAAVVLASEERAR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 309 RLKVKPL----ARVAAFADAAVEPIDFPVAPA--YAVPKVLRDAGLKKEDITMWEVNEAFSLVVLANIKMLDLDPQ---- 378
Cdd:cd00829 221 ELTDRPVwilgVGAASDTPSLSERDDFLSLDAarLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKgegg 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953386780 379 --------------KVNMNGGAVSLGHPIGMSGARIVVHLVHALKqGEYG--------LASICNGGGGASA 427
Cdd:cd00829 301 klvregdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLR-GEAGarqvpgarVGLAHNIGGTGSA 370
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
70-430 |
5.40e-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: 68.62 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 70 ATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAALGAGLPiSTPCTTVNKVCASGMKAIMMASQSLMCG 149
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 150 HQDVMVAGGMESmsnvpyvmsrgatpyggvkledlivkdgltdvynkihmgncaentakkmnitreeqdtyalssytrsk 229
Cdd:cd00327 86 KADIVLAGGSEE-------------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 230 aaweagrfgsevipvtvttkgkpdvlvtedeeykrvdfskvpklktvfqkengtvtaanaSTLNDGAAAVVLMTADAARR 309
Cdd:cd00327 98 ------------------------------------------------------------FVFGDGAAAAVVESEEHALR 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 310 LKVKPLARVAAFADAAVEPIDFPV----APAYAVPKVLRDAGLKKEDITMWEVNEAFSLVVLANIKMLDLDPQKV---NM 382
Cdd:cd00327 118 RGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspAV 197
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953386780 383 NGGAVSLGHPIGMSGARIVVHLVHALKQGEY---------GLASICNGGGGASALLI 430
Cdd:cd00327 198 SATLIMTGHPLGAAGLAILDELLLMLEHEFIpptpreprtVLLLGFGLGGTNAAVVL 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
77-427 |
1.91e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 62.22 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 77 AIQGVIEKAGIPKEEVKEAYMGNVLQGG--EGQAPTRQAALGAGL-PIstPCTTVNKVCASGMKAIMMASQSLMCGHQDV 153
Cdd:PRK06064 29 AGLEALEDAGIDGKDIDAMYVGNMSAGLfvSQEHIAALIADYAGLaPI--PATRVEAACASGGAALRQAYLAVASGEADV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 154 MVAGGMESMSNVPY-----VMSR----------GATPYG-------------GVKLEDL---IVKDGLTDVYNKIHMgnc 202
Cdd:PRK06064 107 VLAAGVEKMTDVPTpdateAIARagdyeweeffGATFPGlyaliarrymhkyGTTEEDLalvAVKNHYNGSKNPYAQ--- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 203 aentaKKMNITREEqdtyALSSytrSKAAWeagrfgseviPVTVTtkgkpdvlvtedeeykrvdfskvpklktvfqkeng 282
Cdd:PRK06064 184 -----FQKEITVEQ----VLNS---PPVAD----------PLKLL----------------------------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 283 tvtaaNASTLNDGAAAVVLMTADAARRLKVKPLARVAAFADAAV------EPIDFPVAPAYAVPKVLRDAGLKKEDITMW 356
Cdd:PRK06064 207 -----DCSPITDGAAAVILASEEKAKEYTDTPVWIKASGQASDTialhdrKDFTTLDAAVVAAEKAYKMAGIEPKDIDVA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 357 EVNEAFSlvVLANIKMLDLDPQK--------------------VNMNGGAVSLGHPIGMSGARIVVHLVHALKQG----- 411
Cdd:PRK06064 282 EVHDCFT--IAEILAYEDLGFAKkgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEaekgr 359
|
410 420
....*....|....*....|...
gi 1953386780 412 ------EYGLASicN-GGGGASA 427
Cdd:PRK06064 360 qqvigaGYGLTH--NvGGTGHTA 380
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
77-413 |
1.84e-07 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 52.77 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 77 AIQGVIEKAGIPKEEVKEAYMGNVLqggeGQAPTRQAALGaGLPIS-------TPCTTVNKVCASGMKAIMMASQSLMCG 149
Cdd:PRK06289 33 VVDGTLAAAGVDADDIEVVHVGNFF----GELFAGQGHLG-AMPATvhpalwgVPASRHEAACASGSVATLAAMADLRAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 150 HQDVMVAGGMESMSNVPYVMSR---GATPYGGVKLEDL-----IVKDGLTDVYNK------IHMGNCAENtakkmNITRE 215
Cdd:PRK06289 108 RYDVALVVGVELMKTVPGDVAAehlGAAAWTGHEGQDArfpwpSMFARVADEYDRrygldeEHLRAIAEI-----NFANA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 216 EQDTYAlssYTRSkaaWeagRFgsevipvtvttkgkPDVLVTEDEEYKRVDFSKVPKLktvfqkengtvtaaNASTLNDG 295
Cdd:PRK06289 183 RRNPNA---QTRG---W---AF--------------PDEATNDDDATNPVVEGRLRRQ--------------DCSQVTDG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 296 AAAVVLMTADAARRL--------------KVKPLARVAAFADAAVEPIDFPVAPAyAVPKVLRDAGLKKEDITMWEVNEA 361
Cdd:PRK06289 226 GAGVVLASDAYLRDYadarpiprikgwghRTAPLGLEQKLDRSAGDPYVLPHVRQ-AVLDAYRRAGVGLDDLDGFEVHDC 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953386780 362 FSLVVLANIKMLDLDP------------------QKVNMNGGAVSLGHPIGMSGARIvvhLVHALKQ-----GEY 413
Cdd:PRK06289 305 FTPSEYLAIDHIGLTGpgeswkaiengeiaiggrLPINPSGGLIGGGHPVGASGVRM---LLDAAKQvtgtaGDY 376
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
113-164 |
2.62e-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: 49.46 E-value: 2.62e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1953386780 113 AALGAGLPISTPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSN 164
Cdd:cd00834 142 GQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
290-401 |
6.31e-06 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 48.10 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 290 STLNDGAAAVVLMTADAARRLK------VKPLARVAAFADAAVEP-IDFPVAPA--YAVPKVLRDAGLK--KEDITMWEV 358
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGkkdpvyVKALQLAVSNGWELQYNgWDGSYFPTtrIAARKAYREAGITdpREELSMAEV 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953386780 359 NEAFS---LVVLANIK--------------MLDLDPQ-KVNMNGGAVSLGHPIGMSGARIV 401
Cdd:PRK06157 294 HDCFSiteLVTMEDLGlsergqawrdvldgFFDADGGlPCQIDGGLKCFGHPIGASGLRML 354
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
124-169 |
3.23e-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: 45.86 E-value: 3.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1953386780 124 PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNvPYVM 169
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT-PLGL 197
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
77-418 |
4.43e-05 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 45.65 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 77 AIQGVIEKAGIPKEE--VKEAYMGNVL------QGGEGQAPTR---QAALGAGLpISTPCTTVNKVCASGMKAIMMASQS 145
Cdd:PTZ00455 55 AIQGTLENTGLDGKAalVDKVVVGNFLgelfssQGHLGPAAVGslgQSGASNAL-LYKPAMRVEGACASGGLAVQSAWEA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 146 LMCGHQDVMVAGGMESMSNVPyvmSRGATPYGGvKLEDLIVKDGLTDVYNKIHMGNCAENTAKKMNITREEQDTYALSSY 225
Cdd:PTZ00455 134 LLAGTSDIALVVGVEVQTTVS---ARVGGDYLA-RAADYRRQRKLDDFTFPCLFAKRMKYIQEHGHFTMEDTARVAAKAY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 226 TRSKAAWEAGRFGSEVIPVTVTTKGKPDVLVTEDEEYKrvdfskvPKLKTvfqkengtvtaANASTLNDGAAAVVLMTAD 305
Cdd:PTZ00455 210 ANGNKNPLAHMHTRKLSLEFCTGASDKNPKFLGNETYK-------PFLRM-----------TDCSQVSDGGAGLVLASEE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 306 AARRLKVKP--------LARVAAFADAAVEPIDFP--VAPAYAVPKVLRDAGLKKEDITMWEVNEAFSLVVLANIKMLDL 375
Cdd:PTZ00455 272 GLQKMGLSPndsrlveiKSLACASGNLYEDPPDATrmFTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGI 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953386780 376 -DPQK-----------------VNMNGGAVSLGHPIGMSGARIVVHLVHALKQ--GEYGLASI 418
Cdd:PTZ00455 352 aEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGqcGEYQMKNI 414
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
124-161 |
5.52e-05 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 45.16 E-value: 5.52e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1953386780 124 PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMES 161
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
124-162 |
1.93e-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: 42.62 E-value: 1.93e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1953386780 124 PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESM 162
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
66-162 |
2.92e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 42.96 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 66 SSLPATKLGSIAIQGVIEKAGIPKEEVKEAYMGNVLqggeGQAPTRQAAL---G-AGLPIstpcTTVNKVCASGMKAIMM 141
Cdd:PRK08256 18 ASWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVY----GDSTSGQRALyevGmTGIPI----VNVNNNCSTGSTALFL 89
|
90 100
....*....|....*....|.
gi 1953386780 142 ASQSLMCGHQDVMVAGGMESM 162
Cdd:PRK08256 90 ARQAVRSGAADCALALGFEQM 110
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
290-427 |
3.11e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 39.55 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 290 STLNDGAAAVVLMTADAARRLK-------------VKPLARVaafadaavEPIDFPvAPAYAVPKVLRDAGLKKEDITMW 356
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALQravrfrarahvndFLPLSRR--------DPLAFE-GPRRAWQRALAQAGVTLDDLSFV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953386780 357 EVNEAFSLVVLANIKMLDLDPQ------------------KVNMNGGAVSLGHPIGMSGarIVVHLVHALK-QGEYG--- 414
Cdd:PRK07516 284 ETHDCFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATG--VSMHVLAAMQlTGEAGgmq 361
|
170
....*....|....*...
gi 1953386780 415 -----LASICNGGGGASA 427
Cdd:PRK07516 362 ipgakLAGVFNMGGAAVA 379
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
93-163 |
6.22e-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: 38.57 E-value: 6.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953386780 93 KEAYMGNVLQGGEGQAPTRQAALGAGLPIST-PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS 163
Cdd:cd00828 122 ARAVNPYVSPKWMLSPNTVAGWVNILLLSSHgPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
|
|
| |
