|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-393 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 610.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVC 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 81 GFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLdAKARSGYRLGDGQVYDVILRDGLMCATHGYHMGI 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVL-PGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 161 TAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTF-VFSQDEFPKANSTAEALGALRPAFDKA 239
Cdd:PRK05790 160 TAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPvVVDTDEHPRPDTTAESLAKLRPAFDKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 240 GTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEA 319
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446709201 320 FAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIERL 393
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-393 |
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: 591.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVC 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 81 GFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDaKARSGYRLgDGQVYDVILRDGLMCATHGYHMGI 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLP-KARWGYRM-NAKLVDPMINPGLTDPYTGLSMGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 161 TAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEFPKANSTAEALGALRPAFDKAG 240
Cdd:COG0183 159 TAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 241 TVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEAF 320
Cdd:COG0183 239 TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446709201 321 AAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIERL 393
Cdd:COG0183 319 AAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-392 |
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: 578.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 5 VIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFTV 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 85 NKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDaKARSGYRLGDGQVyDVILRDGLMCATHGYHMGITAEN 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLP-KARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAEN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 165 VAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEFPKANSTAEALGALRPAFDKAGTVTA 244
Cdd:cd00751 159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 245 GNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEAFAAQF 324
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446709201 325 LAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIER 392
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-391 |
2.29e-180 |
|
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: 506.38 E-value: 2.29e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 6 IVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFTVN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 86 KVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGYRLGDGQVYDVILRDgLMCATHGYHMGITAENV 165
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 166 AKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEFPKANSTAEALGALRPAFDKAGTVTAG 245
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 246 NASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEAFAAQFL 325
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446709201 326 AVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIE 391
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.24e-163 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 464.36 E-value: 1.24e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVC 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 81 GFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLdAKARSGYRLGDGQVYDVILRDGLMCATHGYHMGI 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVL-PGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 161 TAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRK-KTFVFSQDEFPKANSTAEALGALRPAFDKA 239
Cdd:PRK05656 160 TAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKgEPLAFATDEQPRAGTTAESLAKLKPAFKKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 240 GTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEA 319
Cdd:PRK05656 240 GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446709201 320 FAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIER 392
Cdd:PRK05656 320 FAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-393 |
5.06e-163 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 462.89 E-value: 5.06e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGlgqnP-----ARQALLKSGL 75
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTE----PrdmylSRVAAINAGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 76 AETVCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAkARSGYRLGDGQVYDVILrDGLMCATHG 155
Cdd:PRK09051 78 PQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPA-ARWGARMGDAKLVDMMV-GALHDPFGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 156 YHMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEFPKANSTAEALGALRPA 235
Cdd:PRK09051 156 IHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 236 FDK-AGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLI 314
Cdd:PRK09051 236 FKKeNGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVI 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446709201 315 EANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIERL 393
Cdd:PRK09051 316 EANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFERL 394
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-391 |
8.62e-152 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 434.14 E-value: 8.62e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVC 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 81 GFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLdAKARSGYRLGDGQVYDVILRDGLMCATHGYHMGI 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYIL-PGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 161 TAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRK-KTFVFSQDEFPKANSTAEALGALRPAFDKA 239
Cdd:PRK08235 160 YGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKgDPIVVAKDEAPRKDTTIEKLAKLKPVFDKT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 240 GTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEA 319
Cdd:PRK08235 240 GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446709201 320 FAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIE 391
Cdd:PRK08235 320 FAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-393 |
9.21e-142 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 408.71 E-value: 9.21e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 2 KNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCG 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 82 FTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLdAKARSGYRLGDGQVYDVILRDGLMCATHGYHMGIT 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYL-PEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 162 AENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVT---RKKTFVFSQDEFPKANstAEALGALRPAFDK 238
Cdd:PLN02644 160 AELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgrgRPSVIVDKDEGLGKFD--PAKLRKLRPSFKE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 239 -AGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEAN 317
Cdd:PLN02644 238 dGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEIN 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446709201 318 EAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIERL 393
Cdd:PLN02644 318 EAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELM 393
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.57e-140 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 405.18 E-value: 2.57e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVC 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 81 GFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYllDAKARSGYRLGDGQVYDVILRDGLMCATHGYHMGI 160
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMH--GSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 161 TAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEFPKANSTAEALGALRPAFDKAG 240
Cdd:PRK06633 160 TAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDKNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 241 TVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEAF 320
Cdd:PRK06633 240 VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446709201 321 AAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIE 391
Cdd:PRK06633 320 AAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-394 |
3.07e-140 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 405.14 E-value: 3.07e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNvlQAGLGQNPA--RQALLKSGLAET 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 79 VCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAP-YLLDAkaRSGYRLGDGQVYDVILRDGLMC--ATHG 155
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEfYTTDM--RWGVRGGGVQLHDRLARGRETAggRRFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 156 YHMGI--TAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRK-KTFVFSQDEFPKANSTAEALGAL 232
Cdd:PRK06205 157 VPGGMieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKgDPTVVDRDEHPRADTTLESLAKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 233 RP---AFDKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLA 309
Cdd:PRK06205 237 RPimgKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 310 DIDLIEANEAFAAQFLAVGKNLGF---DSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGI 386
Cdd:PRK06205 317 DIDLIELNEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGL 396
|
....*...
gi 446709201 387 AMVIERLN 394
Cdd:PRK06205 397 AAVFERVN 404
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-393 |
1.30e-137 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 398.56 E-value: 1.30e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIER-AKIDSQHVDEVIMGNVLQAGL-GQNPARQALLKSGLAET 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 79 VCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLdAKARSGYRLgDGQVYDVILR----DGLMCATH 154
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVM-GKADSAFSR-QAEIFDTTIGwrfvNPLMKAQY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 155 GYH-MGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTF-VFSQDEFPKANSTAEALGAL 232
Cdd:PRK09050 159 GVDsMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPvVVDRDEHPRPETTLEALAKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 233 RPAFDKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADID 312
Cdd:PRK09050 239 KPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 313 LIEANEAFAAQFLAVGKNLGF--DSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVI 390
Cdd:PRK09050 319 VIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAI 398
|
...
gi 446709201 391 ERL 393
Cdd:PRK09050 399 ERV 401
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-393 |
1.71e-122 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 359.66 E-value: 1.71e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIG-SFNGSLASTSAIDLGATVIKAAIER-AKIDSQHVDEVIMGNVLQAG-LGQNPARQALLKSGLAE 77
Cdd:PRK08947 1 MEDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 78 TVCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGYrlgdgqvydvilrdGLMCATHGYH 157
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGVDFHPGL--------------SKNVAKAAGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 158 MGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPV---NVVTRKKTFVFsqDEFPKANSTAEALGALRP 234
Cdd:PRK08947 147 MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTeghDADGVLKLFDY--DEVIRPETTVEALAALRP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 235 AFD-KAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDL 313
Cdd:PRK08947 225 AFDpVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 314 IEANEAFAAQFLAVGKNLG-FDS--EKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVI 390
Cdd:PRK08947 305 FELNEAFAAQSLPCLKDLGlLDKmdEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVF 384
|
...
gi 446709201 391 ERL 393
Cdd:PRK08947 385 ERV 387
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-393 |
2.77e-122 |
|
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.
Pssm-ID: 131483 Cd Length: 400 Bit Score: 359.48 E-value: 2.77e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 2 KNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIER-AKIDSQHVDEVIMGNVLQAGL-GQNPARQALLKSGLAETV 79
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 80 CGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLdAKARSGYRLGdGQVYDVILR----DGLMCATHG 155
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVM-GKADSAFSRS-AKIEDTTIGwrfiNPLMKALYG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 156 YH-MGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTF-VFSQDEFPKANSTAEALGALR 233
Cdd:TIGR02430 159 VDsMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPtVVDQDEHPRPETTLEGLAKLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 234 PAFDKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDL 313
Cdd:TIGR02430 239 PVVRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 314 IEANEAFAAQFLAVGKNLGF--DSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIE 391
Cdd:TIGR02430 319 IELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIE 398
|
..
gi 446709201 392 RL 393
Cdd:TIGR02430 399 RV 400
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-393 |
2.56e-120 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 354.06 E-value: 2.56e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFN-GSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVL-QAGLGQNPARQALLKSGLAET 78
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 79 VCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLldakarsgyrlgdGQVydVILRDGLMCATHGYHM 158
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM-------------GHV--VRPNPRLVEAAPEYYM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 159 GI--TAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRK---------KTFVFSQDEFPKANSTAE 227
Cdd:PRK07661 146 GMghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgennklqeETITFSQDEGVRADTTLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 228 ALGALRPAFDKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQ 307
Cdd:PRK07661 226 ILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 308 LADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIA 387
Cdd:PRK07661 306 LSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAA 385
|
....*.
gi 446709201 388 MVIERL 393
Cdd:PRK07661 386 GVFELL 391
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-263 |
8.60e-119 |
|
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: 345.44 E-value: 8.60e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 4 CVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 84 VNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGYRLGDGQVYDVILRDGLMCATHGYHMGITAE 163
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 164 NVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEFPKANSTAEALGALRPAFDKAGTVT 243
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
|
250 260
....*....|....*....|
gi 446709201 244 AGNASGINDGAAALVIMEES 263
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
5-391 |
2.85e-117 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 346.49 E-value: 2.85e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 5 VIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFTV 84
Cdd:PRK06954 10 VIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 85 NKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLdAKARSGYRLGDGQVYDVILRDGLMCA-THGYHMGITAE 163
Cdd:PRK06954 90 NKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLL-PKARGGMRMGHGQVLDHMFLDGLEDAyDKGRLMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 164 NVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEFP-KANstAEALGALRPAFDKAGTV 242
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPfKAN--PEKIPTLKPAFSKTGTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 243 TAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEAFAA 322
Cdd:PRK06954 247 TAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446709201 323 QFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIE 391
Cdd:PRK06954 327 VTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-394 |
2.20e-116 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 344.68 E-value: 2.20e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIG-SFNGSLASTSAIDLGATVIKAAIERA-KIDSQHVDEVIMGNVLQAG-LGQNPARQALLKSGLaE 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGY-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 78 TVCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLA-------------PYLLDAKARSGYRL--------- 135
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFakgnsdslpdtknPLFAEAQARTAARAeggaeawhd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 136 --GDGQVYDVILRdglmcathgyhMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVnvvTRKKTFV 213
Cdd:PRK07851 160 prEDGLLPDVYIA-----------MGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPV---TLPDGTV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 214 FSQDEFPKANSTAEALGALRPAFDKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGP 293
Cdd:PRK07851 226 VSTDDGPRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 294 VPATQKALQLAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTL 373
Cdd:PRK07851 306 VEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTF 385
|
410 420
....*....|....*....|.
gi 446709201 374 GLATLCIGGGQGIAMVIERLN 394
Cdd:PRK07851 386 GLETMCVGGGQGMAMVLERLS 406
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-393 |
2.05e-113 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 336.98 E-value: 2.05e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIG-SFNGSLASTSAIDLGATVIKAAIERAK-IDSQHVDEVIMGNVL-QAGLGQNPARQALLKSGLAE 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVPgLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 78 TVCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGyrlgdgqvyDVILRDGLMCATHGyh 157
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSMSP---------AIFARDENVGIAYG-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 158 MGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRK----------KTFVFSQDEFPKANSTAE 227
Cdd:PRK09052 154 MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatgevdvKTRTVDLDEGPRADTSLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 228 ALGALRPAFDKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQ 307
Cdd:PRK09052 234 GLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 308 LADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIA 387
Cdd:PRK09052 314 QDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAA 393
|
....*.
gi 446709201 388 MVIERL 393
Cdd:PRK09052 394 GIFERL 399
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-391 |
6.87e-113 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 335.06 E-value: 6.87e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVC 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 81 GFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGYR---LGDGQVYDVILRDGLMCATHGYH 157
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRWGPKhllHKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 158 MGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVtrkktfvfSQDEFPKaNSTAEALGALRPAFD 237
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFNDL--------DRDEGIR-KTTMEDLAKLPPAFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 238 KAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEAN 317
Cdd:PRK06366 232 KNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446709201 318 EAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIE 391
Cdd:PRK06366 312 EAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-392 |
2.50e-109 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 326.35 E-value: 2.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGL-GQNPARQALLKSGLAETV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 80 CGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLdAKARSGYRLgDGQVYDVIL----RDGLMCATHG 155
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVM-GKAESAFSR-DAKVFDTTIgarfPNPKIVAQYG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 156 YH-MGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKT--FVFSQDEFPKANSTAEALGAL 232
Cdd:PRK08131 159 NDsMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLppKLVAEDEHPRPSSTVEALTKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 233 RPAFDkAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADID 312
Cdd:PRK08131 239 KPLFE-GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 313 LIEANEAFAAQFLAVGKNLG--FDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVI 390
Cdd:PRK08131 318 IIEINEAFASQVLGCLKGLGvdFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVI 397
|
..
gi 446709201 391 ER 392
Cdd:PRK08131 398 ER 399
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
5-392 |
9.80e-109 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 326.72 E-value: 9.80e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 5 VIVSAVRTAI-GSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQ-NPARQALLKSGLAETVCGF 82
Cdd:PLN02287 49 VIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETVPVR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 83 TVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGYRLGDGQvydvilRDGLMcathgyHMGITA 162
Cdd:PLN02287 129 TVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQA------QDCLL------PMGITS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 163 ENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPV--NVVTRK----KTFVFSQDEFPKANSTAEALGALRPAF 236
Cdd:PLN02287 197 ENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtKIVDPKtgeeKPIVISVDDGIRPNTTLADLAKLKPVF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 237 DKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEA 316
Cdd:PLN02287 277 KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEI 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446709201 317 NEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKT--LGLATLCIGGGQGIAMVIER 392
Cdd:PLN02287 357 NEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKDcrFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-393 |
1.11e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 317.21 E-value: 1.11e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRT--AIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAG-LGQNPARQALLKSGLAE 77
Cdd:PRK08242 1 MTEAYIYDAVRTprGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 78 TVCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGyrlgDGQVydvilrdglmcATHGYH 157
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAM----DPST-----------NFPTYF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 158 M--GITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPV---NVVTrkktfVFSQDEFPKANSTAEALGAL 232
Cdd:PRK08242 146 VpqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVkdqNGLT-----ILDHDEHMRPGTTMESLAKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 233 RPAFDKAGTV---------------------TAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGM 291
Cdd:PRK08242 221 KPSFAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 292 GPVPATQKALQLAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDK 371
Cdd:PRK08242 301 GPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGK 380
|
410 420
....*....|....*....|..
gi 446709201 372 TLGLATLCIGGGQGIAMVIERL 393
Cdd:PRK08242 381 RTALITLCVGGGMGIATIIERV 402
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-392 |
3.89e-103 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 310.50 E-value: 3.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGS------LASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGlgQN---PARQALL 71
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVG--ENwlyGGRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 72 KSGLAETVCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAP------------YLLDAKARSgyrlgdgq 139
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPmgdnphiepnpkLLTDPKYIE-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 140 vYDVilrdglmcaTHGYHMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEF 219
Cdd:PRK06445 151 -YDL---------TTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 220 PKANSTAEALGALRPAFDKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQK 299
Cdd:PRK06445 221 VRPDTSLEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 300 ALQLAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLC 379
Cdd:PRK06445 301 ALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLC 380
|
410
....*....|...
gi 446709201 380 IGGGQGIAMVIER 392
Cdd:PRK06445 381 VGGGQGGAVVLER 393
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-392 |
3.13e-99 |
|
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (TIGR02437). The FadBA complex is the major complex active for beta-oxidation of fatty acids in E. coli. [Fatty acid and phospholipid metabolism, Degradation]
Pssm-ID: 131498 Cd Length: 385 Bit Score: 300.32 E-value: 3.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 3 NCVIVSAVRTAIG-SFNGSLASTSAIDLGATVIKAAIER-AKIDSQHVDEVIMGNVLQA-GLGQNPARQALLKSGLAETV 79
Cdd:TIGR02445 1 DVVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVQQTlEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 80 CGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLldakarSGYRLGDGQVYDVILRDGLMcathgyhmG 159
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMM------HGVDFHPGMSLHVAKAAGMM--------G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 160 ITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKT-FVFSQDEFPKANSTAEALGALRPAFD- 237
Cdd:TIGR02445 147 LTAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFlKQFDYDEVIRPETTVESLAALRPAFDp 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 238 KAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEAN 317
Cdd:TIGR02445 227 KNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELN 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446709201 318 EAFAAQFLAVGKNLGF---DSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIER 392
Cdd:TIGR02445 307 EAFAAQALPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-393 |
6.16e-99 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 299.31 E-value: 6.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAG-LGQNPARQALLKSGLAETV 79
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpQAGNIARTSWLAAGLPEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 80 CGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPylLDAKARSGYRLG------DGQVYDVILRDGLMCAT 153
Cdd:PRK07801 81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTAGEQLGftspfaESKGWLHRYGDQEVSQF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 154 HGyhmgitAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTrkktfvfsQDEFPKaNSTAEALGALR 233
Cdd:PRK07801 159 RG------AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGGVT--------VDEGPR-ETSLEKMAGLK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 234 PAFDkAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDL 313
Cdd:PRK07801 224 PLVE-GGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 314 IEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIERL 393
Cdd:PRK07801 303 VEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIERL 382
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-393 |
1.60e-91 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 280.46 E-value: 1.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAG-LGQNPARQALLKSGLAETV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 80 CGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYL----LDAKARSGYRLGDG--QVYDVILRDGLMcat 153
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGspstLPAKNGLGHYKSPGmeERYPGIQFSQFT--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 154 hgyhmgiTAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQ-DEFPKANSTAEALGAL 232
Cdd:PRK06504 158 -------GAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTvDEGIRFDATLEGIAGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 233 RPaFDKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADID 312
Cdd:PRK06504 231 KL-IAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDID 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 313 LIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIER 392
Cdd:PRK06504 310 LYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
.
gi 446709201 393 L 393
Cdd:PRK06504 390 L 390
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
25-393 |
2.38e-91 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 281.14 E-value: 2.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 25 SAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFTVNKVCGSGLKSVALAAQAIQA 104
Cdd:PRK08170 26 SASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 105 GQAQSIVAGGMENMSLAPYLL-----------------DAKARSGYRLGDGQVYDVI-LRDGLMCATHGYHMGITAENVA 166
Cdd:PRK08170 106 GRADLVLAGGVEAMSHAPLLFsekmvrwlagwyaaksiGQKLAALGKLRPSYLAPVIgLLRGLTDPVVGLNMGQTAEVLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 167 KEYGITREMQDELALHSQRKAAAAIESGAFtAEIVPVnvVTRKKTFvFSQDEFPKANSTAEALGALRPAFDKA-GTVTAG 245
Cdd:PRK08170 186 HRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPL--FDRDGKF-YDHDDGVRPDSSMEKLAKLKPFFDRPyGRVTAG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 246 NASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEAFAAQFL 325
Cdd:PRK08170 262 NSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 326 A----------------VGKNLG-FDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAM 388
Cdd:PRK08170 342 AclaawadeeycreqlgLDGALGeLDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGTKRGIAAICIGGGQGGAM 421
|
....*
gi 446709201 389 VIERL 393
Cdd:PRK08170 422 LLERV 426
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-393 |
2.02e-90 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 277.81 E-value: 2.02e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIG-SFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAG-LGQNPARQALLKSGLAET 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 79 VCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLApylldAKARSGYRLGDG-------QVYdvilrdglmc 151
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCV-----QNEMNRHMLREGwlvehkpEIY---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 152 athgYHMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVT----------RKKTFVFSQDEFPK 221
Cdd:PRK07108 146 ----WSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAgvadkatgrlFTKEVTVSADEGIR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 222 ANSTAEALGALRPAFdKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKAL 301
Cdd:PRK07108 222 PDTTLEGVSKIRSAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 302 QLAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIG 381
Cdd:PRK07108 301 KQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIG 380
|
410
....*....|..
gi 446709201 382 GGQGIAMVIERL 393
Cdd:PRK07108 381 GGQGAAGLFEVL 392
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-393 |
2.62e-88 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 272.37 E-value: 2.62e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAG-LGQNPARQALLKSGLAETV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 80 CGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPylLDAKARSGYRLGDGQVYDVILRDGLMcathgyhmg 159
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP--LGANAGPGRGLPRPDSWDIDMPNQFE--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 160 iTAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKK-------TFVFSQDEFPKaNSTAEALGAL 232
Cdd:PRK07850 150 -AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEegqptgeTRLVTRDQGLR-DTTMEGLAGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 233 RPAFDkAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADID 312
Cdd:PRK07850 228 KPVLE-GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDID 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 313 LIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIER 392
Cdd:PRK07850 307 LVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
.
gi 446709201 393 L 393
Cdd:PRK07850 387 I 387
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
5-392 |
1.34e-85 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 266.46 E-value: 1.34e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 5 VIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFTV 84
Cdd:PRK08963 8 AIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYSV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 85 NKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPY---------LLDA-KARS-GYRLGdgQVYDVILRDGLMCA- 152
Cdd:PRK08963 88 SRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIgvskklaraLVDLnKARTlGQRLK--LFSRLRLRDLLPVPp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 153 -----THGYHMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFvfSQDEFPKANSTAE 227
Cdd:PRK08963 166 avaeySTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPL--EEDNNIRGDSTLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 228 ALGALRPAFD-KAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPAL-MGMGPVPATQKALQLAG 305
Cdd:PRK08963 244 DYAKLRPAFDrKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQdMLLGPAYATPLALERAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 306 LQLADIDLIEANEAFAAQFLA----------VGKNLG-------FDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQA 368
Cdd:PRK08963 324 LTLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLGrsqaigeVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRR 403
|
410 420
....*....|....*....|....
gi 446709201 369 RDKTLGLATLCIGGGQGIAMVIER 392
Cdd:PRK08963 404 RGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-393 |
3.19e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 262.79 E-value: 3.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 1 MKNCVIVSAVRT--AIGSF-NGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGL-GQNPARQALLKSGLA 76
Cdd:PRK06025 1 MAEAYIIDAVRTprGIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 77 ETVCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSG---YRLGDGQVYdviLRdglmcAT 153
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGkppLGMGSGNLR---LR-----AL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 154 H-GYHMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVnvVTRKKTFVFSQDEFPKANSTAEALGAL 232
Cdd:PRK06025 153 HpQSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV--YRDDGSVALDHEEFPRPQTTAEGLAAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 233 RPAF--------DKAGTV------------------TAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPP 286
Cdd:PRK06025 231 KPAFtaiadyplDDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 287 ALMGMGPVPATQKALQLAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAM 366
Cdd:PRK06025 311 TLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDEL 390
|
410 420
....*....|....*....|....*..
gi 446709201 367 QARDKTLGLATLCIGGGQGIAMVIERL 393
Cdd:PRK06025 391 ERRGLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-393 |
1.39e-79 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 248.91 E-value: 1.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 3 NCVIVSAVRTAIGSFNGSLASTSAIDLGATVIK---AAIERAkidsqhVDEVIMGNVLqaGLGQNPARQALLKSGLAETV 79
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTflsKGMERE------IDDVILGNVV--GPGGNVARLSALEAGLGLHI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 80 CGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYllDAKAR-SGYRLGDGQvydvilrdglmcathgyhM 158
Cdd:PRK06690 74 PGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF--QNRARfSPETIGDPD------------------M 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 159 GITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVvtrkktfvFSQDEFPKANSTAEALGALRPAFDK 238
Cdd:PRK06690 134 GVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNG--------LLDESIKKEMNYERIIKRTKPAFLH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 239 AGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANE 318
Cdd:PRK06690 206 NGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINE 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446709201 319 AFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIERL 393
Cdd:PRK06690 286 AFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-391 |
1.44e-74 |
|
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: 237.01 E-value: 1.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 7 VSAVRTAIGSFNG---SLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFT 83
Cdd:cd00826 1 AGAAMTAFGKFGGengADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 84 VNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSlapylldakarsgyrlgdgqvydvilrdglmcathgyhmgITAE 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME----------------------------------------TSAE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 164 NVAKEYGI--------TREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEFPK--ANSTAEALGALR 233
Cdd:cd00826 121 NNAKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQfgDEASLDEIAKLR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 234 PAFDKAGTVTAGNASGINDGAAALVIMEESAA-------LAAGLTPLARIKSYASGGVPPA----LMGMGPVPATQKALQ 302
Cdd:cd00826 201 PAFDKEDFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 303 LAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEK------------------VNVNGGAIALGHPIGASGARILVTLLH 364
Cdd:cd00826 281 KAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCF 360
|
410 420 430
....*....|....*....|....*....|..
gi 446709201 365 AMQARDKTL-----GLATLCIGGGQGIAMVIE 391
Cdd:cd00826 361 ELKGEAGKRqgagaGLALLCIGGGGGAAMCIE 392
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
270-392 |
6.75e-67 |
|
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: 207.88 E-value: 6.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 270 LTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGH 349
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446709201 350 PIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIER 392
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
5-392 |
1.14e-58 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 196.66 E-value: 1.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 5 VIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFTV 84
Cdd:PRK09268 10 AILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 85 NKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAP---------YLLDA--------KARSGYRLGDGQVYDVILRD 147
Cdd:PRK09268 90 QQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPiavneglrkILLELnrakttgdRLKALGKLRPKHLAPEIPRN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 148 GLmcATHGYHMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRkktfvfsqDEFPKANSTAE 227
Cdd:PRK09268 170 GE--PRTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR--------DNNLRPDSSLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 228 ALGALRPAFDKA--GTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGV-----PPALMgMGPVPATQKA 300
Cdd:PRK09268 240 KLAKLKPVFGKGgrATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVdfvhgKEGLL-MAPAYAVPRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 301 LQLAGLQLADIDLIEANEAFAAQFLA----------------VGKNLG-FDSEKVNVNGGAIALGHPIGASGARILVTLL 363
Cdd:PRK09268 319 LARNGLTLQDFDFYEIHEAFASQVLAtlkawedeeycrerlgLDAPLGsIDRSKLNVNGSSLAAGHPFAATGGRIVATLA 398
|
410 420
....*....|....*....|....*....
gi 446709201 364 HAMQARDKTLGLATLCIGGGQGIAMVIER 392
Cdd:PRK09268 399 KLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
224-390 |
1.01e-23 |
|
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: 99.06 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 224 STAEALGALRPAFDKAGTVTAG--NASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVP----PALMGMGPVPAT 297
Cdd:cd00327 72 LTALALAVQQVQNGKADIVLAGgsEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 298 QKALQLAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKV---NVNGGAIALGHPIGASGARILVTLLHAMQARDK--- 371
Cdd:cd00327 152 RKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIppt 231
|
170 180
....*....|....*....|...
gi 446709201 372 ----TLGLATLCIGGGQGIAMVI 390
Cdd:cd00327 232 prepRTVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
19-390 |
3.75e-13 |
|
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: 69.98 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 19 GSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCgFTVNKVCGSGLKSVALA 98
Cdd:cd00829 9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPA-TRVEAAGASGSAAVRAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 99 AQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGYRLGDGQVYDVILrdglmcaTHGYHMGITAENVAKEYGITREMQDE 178
Cdd:cd00829 88 AAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPPGGL-------TPPALYALAARRYMHRYGTTREDLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 179 LALhSQRKAAA----AIESGAFTAEIVpvnvvtrkktfvfsqdefpkANST--AEALGALrpafdkagtvtagNASGIND 252
Cdd:cd00829 161 VAV-KNHRNAArnpyAQFRKPITVEDV--------------------LNSRmiADPLRLL-------------DCCPVSD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 253 GAAALVIMEESAALAAGLTPlARIKSYASGGVPPALMGMGP-------VPATQKALQLAGLQLADIDLIEANEAFAAQFL 325
Cdd:cd00829 207 GAAAVVLASEERARELTDRP-VWILGVGAASDTPSLSERDDflsldaaRLAARRAYKMAGITPDDIDVAELYDCFTIAEL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 326 AVGKNLGFDSE------------------KVNVNGGAIALGHPIGASGARILVTLLH-------AMQARDKTLGLATLCI 380
Cdd:cd00829 286 LALEDLGFCEKgeggklvregdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRqlrgeagARQVPGARVGLAHNIG 365
|
410
....*....|
gi 446709201 381 GGGQGIAMVI 390
Cdd:cd00829 366 GTGSAAVVTI 375
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
230-356 |
1.95e-07 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 52.81 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 230 GALRPaFDKAGTvtaGNASGinDGAAALVIMEESAALAAGLTPLARI--KSYASGG---VPPALMGMGPVPATQKALQLA 304
Cdd:PRK07910 226 GACRP-FDKDRD---GFVFG--EGGALMVIETEEHAKARGANILARImgASITSDGfhmVAPDPNGERAGHAMTRAIELA 299
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446709201 305 GLQLADIDLIEANeAFAAQF--LAVGK--NLGFDSEKVNVNGGAIALGHPIGASGA 356
Cdd:PRK07910 300 GLTPGDIDHVNAH-ATGTSVgdVAEGKaiNNALGGHRPAVYAPKSALGHSVGAVGA 354
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
252-356 |
2.39e-07 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 52.48 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 252 DGAAALVIMEESAALAAGLTPLARIKSYASGG-----VPPALMGMGPVPATQKALQLAGLQLADIDLIEA-------NEA 319
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDYINAhgtstpaGDK 311
|
90 100 110
....*....|....*....|....*....|....*..
gi 446709201 320 FAAQflAVGKNLGFDSEKVNVNGGAIALGHPIGASGA 356
Cdd:PRK07314 312 AETQ--AIKRVFGEHAYKVAVSSTKSMTGHLLGAAGA 346
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
231-356 |
7.27e-07 |
|
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: 51.00 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 231 ALRPaFDKagtvtagNASGIN--DGAAALVIMEESAALAAGLTPLARIKSYASGG-----VPPALMGMGPVPATQKALQL 303
Cdd:cd00834 216 ASRP-FDK-------DRDGFVlgEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALAD 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446709201 304 AGLQLADIDLI-------------EANeAFAAQFLAVGKNLgfdseKVNVNGGAIalGHPIGASGA 356
Cdd:cd00834 288 AGLSPEDIDYInahgtstplndaaESK-AIKRVFGEHAKKV-----PVSSTKSMT--GHLLGAAGA 345
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
248-375 |
1.35e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 49.95 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 248 SGINDGAAALVIMeeSAALAAGLTPLARIKSYA--------SGGVPPALMGmgPVPATQKALQLAGLQLADIDLIEANEA 319
Cdd:PRK07516 213 SLVSDGAAALVLA--DAETARALQRAVRFRARAhvndflplSRRDPLAFEG--PRRAWQRALAQAGVTLDDLSFVETHDC 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 320 FA-AQFL---AVG---KNLGFDSEK-----------VNVNGGAIALGHPIGASG-------ARILVTLLHAMQARDKTLG 374
Cdd:PRK07516 289 FTiAELIeyeAMGlapPGQGARAIRegwtakdgklpVNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPGAKLA 368
|
.
gi 446709201 375 L 375
Cdd:PRK07516 369 G 369
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
247-360 |
2.43e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 49.12 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 247 ASGINDGAAALVIMEESAALAAGLTPLaRIKSYASGGVPPALMG-------MGPVPATQKALQLAGLQLADIDLIEANEA 319
Cdd:PRK06064 208 CSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQASDTIALHDrkdfttlDAAVVAAEKAYKMAGIEPKDIDVAEVHDC 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446709201 320 FA-AQFLAVgKNLGFdSEK-------------------VNVNGGAIALGHPIGASGARILV 360
Cdd:PRK06064 287 FTiAEILAY-EDLGF-AKKgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQAV 345
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
231-356 |
3.78e-06 |
|
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: 48.55 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 231 ALRPaFDKagtvtagNASGIN--DGAAALVIMEESAALAAGLTPLARIKSYASGG-----VPPALMGMGPVPATQKALQL 303
Cdd:COG0304 216 ASRP-FDK-------DRDGFVlgEGAGVLVLEELEHAKARGAKIYAEVVGYGASSdayhiTAPAPDGEGAARAMRAALKD 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446709201 304 AGLQLADIDLIEA----------NEAfaaqfLAVGKNLGFDSEKVNVNggAI--ALGHPIGASGA 356
Cdd:COG0304 288 AGLSPEDIDYINAhgtstplgdaAET-----KAIKRVFGDHAYKVPVS--STksMTGHLLGAAGA 345
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
248-389 |
3.94e-06 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 48.74 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 248 SGINDGAAALVIMEESAALAAGLTP----LARIKSY--ASGGV---PPALMGM-GPVPATQKALQLAGLQLADIDLIEAN 317
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLacASGNLyedPPDATRMfTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 318 EAFAAQFLAVGKNLGFDSE------------------KVNVNGGAIALGHPIGASGARILVTLLHAMQAR------DKTL 373
Cdd:PTZ00455 336 DCFTIAELLMYEALGIAEYghakdlirngatalegriPVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQcgeyqmKNIP 415
|
170
....*....|....*..
gi 446709201 374 GL-ATLCIGGGQGIAMV 389
Cdd:PTZ00455 416 ALgATLNMGGDDKTAVS 432
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
248-360 |
5.07e-06 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 48.15 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 248 SGINDGAAALVIMEESAALA-AGLTPLARIKSY--------------ASGGVP---PALMGmgpvpATQKALQLAGLQLA 309
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDyADARPIPRIKGWghrtaplgleqkldRSAGDPyvlPHVRQ-----AVLDAYRRAGVGLD 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446709201 310 DIDLIEANEAF-AAQFLAV--------GKN--------LGFDSEK-VNVNGGAIALGHPIGASGARILV 360
Cdd:PRK06289 295 DLDGFEVHDCFtPSEYLAIdhigltgpGESwkaiengeIAIGGRLpINPSGGLIGGGHPVGASGVRMLL 363
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
180-369 |
9.23e-06 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 47.55 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 180 ALHSqrkAAAAIESGAFTAEIVP-VNVVTRKKTFV-FSQdefpkanstaeaLGALRP-----AFDKA--GTVTAgnasgi 250
Cdd:cd00833 176 ALHL---ACQSLRSGECDLALVGgVNLILSPDMFVgFSK------------AGMLSPdgrcrPFDADadGYVRG------ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 251 nDGAAALVIMEESAALAAGLTPLARIKSYA--SGGvpPALMGMGPVPATQ-----KALQLAGLQLADIDLIEA------- 316
Cdd:cd00833 235 -EGVGVVVLKRLSDALRDGDRIYAVIRGSAvnQDG--RTKGITAPSGEAQaalirRAYARAGVDPSDIDYVEAhgtgtpl 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446709201 317 ---------NEAFAA-----QFLAVGknlgfdSEKVNVnggaialGHPIGASGARILVTLLHAMQAR 369
Cdd:cd00833 312 gdpievealAKVFGGsrsadQPLLIG------SVKSNI-------GHLEAAAGLAGLIKVVLALEHG 365
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
252-356 |
7.71e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 44.27 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 252 DGAAALVIMEESAALAAGLTPLARIKSY-----ASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEA-------NEA 319
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAhgtatrlNDQ 289
|
90 100 110
....*....|....*....|....*....|....*..
gi 446709201 320 FAAQFLavgKNLgFDSeKVNVNGGAIALGHPIGASGA 356
Cdd:PRK05952 290 REANLI---QAL-FPH-RVAVSSTKGATGHTLGASGA 321
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
250-368 |
1.14e-04 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 43.78 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 250 INDGAAALVIMEESAALAAGLTPLARIKSYA-----SGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEAFAAQF 324
Cdd:cd00825 159 FGDGAGALVVEELEHALARGAHIYAEIVGTAatidgAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIG 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446709201 325 LAVGKNLG---FDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQA 368
Cdd:cd00825 239 DVKELKLLrseFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEH 285
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
248-359 |
1.63e-04 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 43.48 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 248 SGINDGAAALVIMEESAALAAGLTPLARIKSY---ASGGVPPALMG------MGPVPATQKALQLAGLQ--LADIDLIEA 316
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGKKDPVYVKALqlaVSNGWELQYNGwdgsyfPTTRIAARKAYREAGITdpREELSMAEV 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446709201 317 NEAFAAQFLAVGKNLGFDSE------------------KVNVNGGAIALGHPIGASGARIL 359
Cdd:PRK06157 294 HDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
180-378 |
1.91e-04 |
|
"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: 43.20 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 180 ALHSQRKAAAAIESGafTAEIVPVNVVTRKKTFVFSQDEFPKANSTAEAL--GALRPAF-DKAGTVTAGnasgindGAAA 256
Cdd:cd00828 165 ALEALDLAVEAIRSG--KADIVVVGGVEDPLEEGLSGFANMGALSTAEEEpeEMSRPFDeTRDGFVEAE-------GAGV 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 257 LVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPAT----QKALQLAGLQLADIDLIEAN------------EAF 320
Cdd:cd00828 236 LVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGIaraiRTALAKAGLSLDDLDVISAHgtstpandvaesRAI 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446709201 321 AAQFLAVGKNLGFDSEKVNVnggaialGHPIGASGArILVTLLHAMQARDKTLGLATL 378
Cdd:cd00828 316 AEVAGALGAPLPVTAQKALF-------GHSKGAAGA-LQLIGALQSLEHGLIPPTANL 365
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
242-371 |
2.30e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 42.97 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 242 VTAGNASGINDGAAALVIMEESAALAAGLTPLaRIKSYASGG--VPPALMGMGPVP------------------------ 295
Cdd:PRK06365 217 LTRLDVCAMSDGAACAILASEDKAFEITDKPV-LIKAIGTGSdtLRLADRPFGEVPllpnespddykdlrypgvhsfrag 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 296 --ATQKALQLAGLQ--LADIDLIEANEAFAAQFLAVGKNLGF----------DSEK--------VNVNGGAIALGHPIGA 353
Cdd:PRK06365 296 rmAAKEAYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiESGKpelpgklpVNPSGGLLAAGHAVGA 375
|
170
....*....|....*...
gi 446709201 354 SGARILVTLLHAMQARDK 371
Cdd:PRK06365 376 TGIMQAVFMFWQLQGRIK 393
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
186-377 |
3.62e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 42.37 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 186 KAAAAIESGAFTAEIVpVNVVTRKKTFVFSQDEFPKANSTAEALGalRPAFdkAGTVTAGNASGINDGAAALVIM----- 260
Cdd:PRK07937 145 QARAGLDAGKWTEEQM-AEVAARSRADARRNPSAEPSISVDELLA--RPYF--ADPLRRHDIAPITDGAAAVVLAagdra 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 261 EESAALAAGLTPLA-RIKSYASGGvppalMGMGPVPATQKALQLA-GLQLADIDLIEANEAFAAQFLAVGKNLGF-DSEK 337
Cdd:PRK07937 220 RELRERPAWITGIEhRIESPSLGA-----RDLTRSPSTALAAEAAtGGDAGGVDVAELHAPFTHQELILREALGLgDKTK 294
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446709201 338 VNVNGGAIAlGHPIGASG-ARILVTLLHAMQAR-DKTLGLAT 377
Cdd:PRK07937 295 VNPSGGALA-ANPMFAAGlERIGEAARHIWDGSaRRALAHAT 335
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
250-356 |
4.31e-04 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 42.09 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 250 INDGAAALVIMEESAALAAGLTPLARIKSYASGG-----VPPALMGMGPVPATQKALQLAGLQLADIDLIEAN------- 317
Cdd:PLN02836 253 IGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGdahhiTQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAHatstplg 332
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446709201 318 ---EAFAAQFL----AVGKNLGFDSEKvnvngGAIalGHPIGASGA 356
Cdd:PLN02836 333 davEARAIKTVfsehATSGGLAFSSTK-----GAT--GHLLGAAGA 371
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
223-373 |
2.85e-03 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 39.33 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 223 NSTAEAlgALRPaFDkagtvTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGG-----VPPALMGMGPVPAT 297
Cdd:PRK14691 141 NSTPEK--ASRP-FD-----TARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSAdayhmTSGAEDGDGAYRAM 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 298 QKALQLAGLQLADIDLIEANeafaAQFLAVG--------KNLGFDSEKVNVNGGAIALGHPIGASGAriLVTLLHAMQAR 369
Cdd:PRK14691 213 KIALRQAGITPEQVQHLNAH----ATSTPVGdlgeinaiKHLFGESNALAITSTKSATGHLLGAAGG--LETIFTVLALR 286
|
....
gi 446709201 370 DKTL 373
Cdd:PRK14691 287 DQIV 290
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
252-355 |
2.93e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 39.50 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 252 DGAAALVIMEESAALAAGLTPLARIKSYA---------SGGVPPALMGMG-PVPATQKALQLAGLQLADIDLIEANEAFA 321
Cdd:PRK08256 215 CGAAAAIVCSEEFARKHGLDRAVEIVAQAmttdtpstfDGRSMIDLVGYDmTRAAAQQVYEQAGIGPEDIDVVELHDCFS 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446709201 322 AQFLAVGKNLGF----DSEK--------------VNVNGGAIALGHPIGASG 355
Cdd:PRK08256 295 ANELLTYEALGLcpegEAEKfiddgdntyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
246-355 |
7.42e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 38.29 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709201 246 NASGINDGAAALVIMEESAALAAGLTPLARIKS--YASGGVPPALMG-----MGPVPATQKALQLAGLQLADIDLIEANE 318
Cdd:PRK12578 205 DSCPISDGSATAIFASEEKVKELKIDSPVWITGigYANDYAYVARRGewvgfKATQLAARQAYNMAKVTPNDIEVATVHD 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446709201 319 AFAAQFLAVGKNLGF-------------DSEK-----VNVNGGAIALGHPIGASG 355
Cdd:PRK12578 285 AFTIAEIMGYEDLGFtekgkggkfieegQSEKggkvgVNLFGGLKAKGHPLGATG 339
|
|
| |
