|
Name |
Accession |
Description |
Interval |
E-value |
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-375 |
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: 563.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVP 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEIDSKnLKNSMLIDGLTDVYGEYHMGIT 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAK-LVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 161 AENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGS---FFEGDETIRANSTLEKLATLKSVFQEDGT 237
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKgevVVDRDEGPRPDTTLEKLAKLKPAFKKDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 238 VTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEAFA 317
Cdd:COG0183 240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 500021509 318 SQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:COG0183 320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMC 377
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-375 |
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: 558.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 5 VIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVPGVTI 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 85 NEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEIDSkNLKNSMLIDGLTDVYGEYHMGITAENV 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGL-NTLDGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 165 AKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGS---FFEGDETIRANSTLEKLATLKSVFQEDGTVTAG 241
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKgpvVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 242 NSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEAFASQSV 321
Cdd:cd00751 240 NASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQAL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 500021509 322 AVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:cd00751 320 ACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMC 373
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-375 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 550.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVP 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEIDSKNLKNSMLIDGLTDVYGEYHMGIT 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 161 AENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLP--NGSF--FEGDETIRANSTLEKLATLKSVFQEDG 236
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKqrKGDPvvVDTDEHPRPDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 237 TVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEAF 316
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 500021509 317 ASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLC 379
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-375 |
8.84e-173 |
|
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: 487.12 E-value: 8.84e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 6 IIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVPGVTIN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 86 EVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEfYGEEIDSKNLKNS-MLIDGLTDVYGEYHMGITAENV 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRS-LRWGVKPGNAELEdARLKDLTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 165 AKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLP---NGSFFEGDETIRANSTLEKLATLKSVFQEDGTVTAG 241
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKgrkGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 242 NSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEAFASQSV 321
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 500021509 322 AVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMC 373
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-375 |
2.28e-146 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 420.27 E-value: 2.28e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVP 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEIDSKNLKNSMLIDGLTDVYGEYHMGIT 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 161 AENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGS----FFEGDETIRANSTLEKLATLKSVFQEDG 236
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKgdpiVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 237 TVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEAF 316
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 500021509 317 ASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAIC 379
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-375 |
5.05e-138 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 399.26 E-value: 5.05e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVP 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEIDSKNLKNSMLIDGLTDVYGEYHMGIT 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 161 AENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGS----FFEGDETIRANSTLEKLATLKSVFQEDG 236
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKgeplAFATDEQPRAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 237 TVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEAF 316
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 500021509 317 ASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLC 379
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-375 |
2.13e-131 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 382.13 E-value: 2.13e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 2 KEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVPG 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 82 VTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEIDSKNLKNSMLIDGLTDVYGEYHMGITA 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 162 ENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNG-----SFFEGDETIrANSTLEKLATLKSVFQED- 235
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGrgrpsVIVDKDEGL-GKFDPAKLRKLRPSFKEDg 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 236 GTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEA 315
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 316 FASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGIC 379
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-375 |
1.66e-127 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 372.37 E-value: 1.66e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAG-LGQNVARQVAIKAGIPYKV 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEpRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 80 PGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEI-DSKNLknSMLIDGLTDVYGEYHMG 158
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMgDAKLV--DMMVGALHDPFGTIHMG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 159 ITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLP--NGSF-FEGDETIRANSTLEKLATLKSVFQED 235
Cdd:PRK09051 160 VTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKtrKGEVvFDTDEHVRADTTLEDLAKLKPVFKKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 236 -GTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNE 314
Cdd:PRK09051 240 nGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500021509 315 AFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMC 380
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-375 |
3.08e-126 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 369.28 E-value: 3.08e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLER-ANIAPERIDQVIFGNVLQAGL-GQNVARQVAIKAGIPYK 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 79 VPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNpefygeEIDSKNLKNSMLIDG----------L 148
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMG------KADSAFSRQAEIFDTtigwrfvnplM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 149 TDVYGEYHMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNG----SFFEGDETIRANSTLEK 224
Cdd:PRK09050 155 KAQYGVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKkgdpVVVDRDEHPRPETTLEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 225 LATLKSVFQEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSI 304
Cdd:PRK09050 235 LAKLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTI 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500021509 305 DDIDLFHLNEAFASQSVAVARDLKIPE--EKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK09050 315 DQFDVIELNEAFAAQGLAVLRQLGLADddARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMC 387
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-375 |
4.42e-118 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 348.11 E-value: 4.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKF-GGSLKDVSAVDLGAIALKGVLER-ANIAPERIDQVIFGNVLQAG-LGQNVARQVAIKAGIPY 77
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 78 KVPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLlnpefYGEEIDSKNLKNSMLIDGLtdvygeyhM 157
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMN-----HGVDFHPGLSKNVAKAAGM--------M 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 158 GITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVR--LPNGSF--FEGDETIRANSTLEKLATLKSVFQ 233
Cdd:PRK08947 148 GLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEghDADGVLklFDYDEVIRPETTVEALAALRPAFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 234 -EDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHL 312
Cdd:PRK08947 228 pVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500021509 313 NEAFASQSVAVARDLKI---PEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK08947 308 NEAFAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMC 373
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-375 |
4.68e-118 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 348.17 E-value: 4.68e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVP 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSqapLLLNPEFY--GEEIDSKNLKNSMLIDGLTDVYGEYHMG 158
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMS---LGMHGSYIraGAKFGDIKMVDLMQYDGLTDVFSGVFMG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 159 ITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRL---PNGSFFEGDETIRANSTLEKLATLKSVFQED 235
Cdd:PRK06633 159 ITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVtikKTTSLFDHDETVRPDTSLEILSKLRPAFDKN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 236 GTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEA 315
Cdd:PRK06633 239 GVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 316 FASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK06633 319 FAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLC 378
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-375 |
2.46e-117 |
|
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: 346.77 E-value: 2.46e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 2 KEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLER-ANIAPERIDQVIFGNVLQAGL-GQNVARQVAIKAGIPYKV 79
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 80 PGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLL----NPEFYGEEIDSKNLKNSMLIDGLTDVYGEY 155
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMgkadSAFSRSAKIEDTTIGWRFINPLMKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 156 HMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNG----SFFEGDETIRANSTLEKLATLKSV 231
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKkgepTVVDQDEHPRPETTLEGLAKLKPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 232 FQEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFH 311
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500021509 312 LNEAFASQSVAVARDLKIPE--EKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:TIGR02430 321 LNEAFAAQALAVLRELGLADddARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMC 386
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-259 |
7.26e-115 |
|
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: 335.04 E-value: 7.26e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 4 VVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVPGVT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 84 INEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFY-GEEIDSKNLKNSMLIDGLTDVYGEYHMGITAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARsGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 163 NVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNG---SFFEGDETIRANSTLEKLATLKSVFQEDGTVT 239
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRkgkPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
|
250 260
....*....|....*....|
gi 500021509 240 AGNSSGINDGASAVILMSKE 259
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-375 |
3.88e-113 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 336.20 E-value: 3.88e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGK-FGGSLKDVSAVDLGAIALKGVLERA-NIAPERIDQVIFGNVLQAG-LGQNVARQVAIKAGIPY 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGRaFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 78 kVPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQ--------APLLLNPEFYGEEIDSKNLKNSMLI---- 145
Cdd:PRK07851 81 -LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRfakgnsdsLPDTKNPLFAEAQARTAARAEGGAEawhd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 146 ---DG-LTDVYgeYHMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGSFFEGDETIRANST 221
Cdd:PRK07851 160 preDGlLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDGTVVSTDDGPRAGTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 222 LEKLATLKSVFQEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGE 301
Cdd:PRK07851 238 YEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500021509 302 YSIDDIDLFHLNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK07851 318 MSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMC 391
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-375 |
1.22e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 331.71 E-value: 1.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFG-GSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVL-QAGLGQNVARQVAIKAGIPYK 78
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 79 VPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLllnpefyGEEIDSKNLKnsmlidgLTDVYGEYHMG 158
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPM-------MGHVVRPNPR-------LVEAAPEYYMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 159 I--TAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRL------PNGSF------FEGDETIRANSTLEK 224
Cdd:PRK07661 147 MghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVtlrtvgENNKLqeetitFSQDEGVRADTTLEI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 225 LATLKSVFQEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSI 304
Cdd:PRK07661 227 LGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLEL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500021509 305 DDIDLFHLNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK07661 307 SDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMC 377
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-375 |
2.77e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 331.57 E-value: 2.77e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVP 80
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAplllnpEFYGEEIDSKNLKNSM-LIDGL----TDVYGEY 155
Cdd:PRK06205 81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNV------EFYTTDMRWGVRGGGVqLHDRLargrETAGGRR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 156 H-----MGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLP----NGSFFEGDETIRANSTLEKLA 226
Cdd:PRK06205 155 FpvpggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPqrkgDPTVVDRDEHPRADTTLESLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 227 TLKSVFQ---EDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYS 303
Cdd:PRK06205 235 KLRPIMGkqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLT 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500021509 304 IDDIDLFHLNEAFASQSVAVARDLKIPE---EKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK06205 315 LDDIDLIELNEAFAAQVLAVLKEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMC 389
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-375 |
6.58e-106 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 319.40 E-value: 6.58e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 3 EVVIIDAARTPIGKFG-GSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQ-NVARQVAIKAGIPYKVP 80
Cdd:PLN02287 47 DVVIVAAYRTPICKAKrGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEIDSKNLKNSMLidgltdvygeyHMGIT 160
Cdd:PLN02287 127 VRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLL-----------PMGIT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 161 AENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGSFFEGDET---------IRANSTLEKLATLKSV 231
Cdd:PLN02287 196 SENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDPKTGEEKpivisvddgIRPNTTLADLAKLKPV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 232 FQEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFH 311
Cdd:PLN02287 276 FKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFE 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500021509 312 LNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENK--QVGLASLC 375
Cdd:PLN02287 356 INEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKdcRFGVVSMC 421
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-375 |
2.98e-103 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 310.40 E-value: 2.98e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVP 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEF-YG-EEIDSKNLK--NSMLIDGLTDVYGEYH 156
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLrWGpKHLLHKNYKidDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 157 MGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVrlpngSFFEGDETIRaNSTLEKLATLKSVFQEDG 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPF-----NDLDRDEGIR-KTTMEDLAKLPPAFDKNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 237 TVTAGNSSGINDGASAvILMSKEKAIAE-NIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEA 315
Cdd:PRK06366 235 ILTAGNSAQLSDGGSA-LVMASEKAINEyGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNEA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 316 FASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK06366 314 FSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLC 373
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-375 |
5.17e-101 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 304.89 E-value: 5.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVP 80
Cdd:PRK06954 6 QDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEIDSKNLKNSMLIDGLTDVYGEYH-MGI 159
Cdd:PRK06954 86 CTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 160 TAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGSffeGDETI-------RANstLEKLATLKSVF 232
Cdd:PRK06954 166 FAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKK---GDTVIdrdeqpfKAN--PEKIPTLKPAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 233 QEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHL 312
Cdd:PRK06954 241 SKTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEI 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500021509 313 NEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK06954 321 NEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLC 383
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-375 |
1.42e-99 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 302.32 E-value: 1.42e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVP 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPE---FYGEEIDSKNLKNSM-------------- 143
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKmvrWLAGWYAAKSIGQKLaalgklrpsylapv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 144 --LIDGLTDVYGEYHMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEeIVPVRLPNGSFFEGDETIRANST 221
Cdd:PRK08170 162 igLLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKE-VVPLFDRDGKFYDHDDGVRPDSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 222 LEKLATLKSVFQED-GTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKG 300
Cdd:PRK08170 241 MEKLAKLKPFFDRPyGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 301 EYSIDDIDLFHLNEAFASQSVAVARDLK-----------------IPEEKLNIYGGAIALGHPIGASGARIVVSLLNELK 363
Cdd:PRK08170 321 GLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLHLLHALK 400
|
410
....*....|..
gi 500021509 364 HENKQVGLASLC 375
Cdd:PRK08170 401 RRGTKRGIAAIC 412
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-375 |
2.59e-99 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 300.77 E-value: 2.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKF-GGSLKDVSAVDLGAIALKGVLERA-NIAPERIDQVIFGNVL-QAGLGQNVARQVAIKAGIPY 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGKApRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 78 KVPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLL-----LNPE-FYGEEidsknlknsmlidgltDV 151
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMgnkpsMSPAiFARDE----------------NV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 152 YGEYHMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPV----RLPNGS---------FFEGDETIRA 218
Cdd:PRK09052 149 GIAYGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYeiteRFPDLAtgevdvktrTVDLDEGPRA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 219 NSTLEKLATLKSVFQEDGTVTAGNSSGINDGASAVILMSkEKAIAE-NIPYLATIKVTSEVGVDPAIMGYAPYYAVNEAL 297
Cdd:PRK09052 229 DTSLEGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVS-EKALKQfNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAAL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500021509 298 AKGEYSIDDIDLFHLNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK09052 308 KQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMC 385
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-375 |
2.41e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 298.34 E-value: 2.41e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKF--GGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAG-LGQNVARQVAIKAGIPY 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGkkDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 78 KVPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLL-------LNPEFygeeidskNLKNSMLidgltd 150
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGsdggawaMDPST--------NFPTYFV------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 151 vygeyHMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNG-SFFEGDETIRANSTLEKLATLK 229
Cdd:PRK08242 147 -----PQGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGlTILDHDEHMRPGTTMESLAKLK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 230 SVFQEDGTV---------------------TAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYA 288
Cdd:PRK08242 222 PSFAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 289 PYYAVNEALAKGEYSIDDIDLFHLNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQ 368
Cdd:PRK08242 302 PVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKR 381
|
....*..
gi 500021509 369 VGLASLC 375
Cdd:PRK08242 382 TALITLC 388
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-375 |
2.15e-97 |
|
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: 295.31 E-value: 2.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 3 EVVIIDAARTPIGKF-GGSLKDVSAVDLGAIALKGVLER-ANIAPERIDQVIFGNVLQA-GLGQNVARQVAIKAGIPYKV 79
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSkGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVQQTlEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 80 PGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLlnpefYGEEIDSKNLKNSMLIDGLtdvygeyhMGI 159
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMM-----HGVDFHPGMSLHVAKAAGM--------MGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 160 TAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVR--LPNGSF--FEGDETIRANSTLEKLATLKSVFQ-E 234
Cdd:TIGR02445 148 TAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQghDADGFLkqFDYDEVIRPETTVESLAALRPAFDpK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 235 DGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNE 314
Cdd:TIGR02445 228 NGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500021509 315 AFASQSVAVARDLKIPE---EKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:TIGR02445 308 AFAAQALPCLKDLGLLDkmdEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMC 371
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-375 |
7.23e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 291.23 E-value: 7.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGlGQ--NVARQVAIKAGIPYK 78
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQagNIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 79 VPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPL----LLNPE--FYGEEIDSKnlknsmlidGLTDVY 152
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPIssamTAGEQlgFTSPFAESK---------GWLHRY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 153 G--EYHMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVrlpNGsfFEGDETIRaNSTLEKLATLKS 230
Cdd:PRK07801 151 GdqEVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV---GG--VTVDEGPR-ETSLEKMAGLKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 231 VFqEDGTVTAGNSSGINDGASAVILMSkEKAIAE-NIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDL 309
Cdd:PRK07801 225 LV-EGGRLTAAVASQISDGASAVLLAS-ERAVKRhGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDV 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500021509 310 FHLNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK07801 303 VEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMC 368
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-375 |
1.15e-94 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 288.98 E-value: 1.15e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGL-GQNVARQVAIKAGIPYKV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 80 PGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPefyGEEIDSKNLK-----------NSMLIDGl 148
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGK---AESAFSRDAKvfdttigarfpNPKIVAQ- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 149 tdvYGEYHMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGS-----FFEGDETIRANSTLE 223
Cdd:PRK08131 157 ---YGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRklppkLVAEDEHPRPSSTVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 224 KLATLKSVFqEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYS 303
Cdd:PRK08131 234 ALTKLKPLF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLT 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500021509 304 IDDIDLFHLNEAFASQSVAVARDLKIP--EEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK08131 313 LDDMDIIEINEAFASQVLGCLKGLGVDfdDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLC 386
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-375 |
2.29e-90 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 277.37 E-value: 2.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGS------LKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGlgQNVA---RQVAI 71
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVG--ENWLyggRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 72 KAGIPYKVPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFygeEIDSKNLKNSMLIDglTDV 151
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHI---EPNPKLLTDPKYIE--YDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 152 YGEYHMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLP-NGS--FFEGDETIRANSTLEKLATL 228
Cdd:PRK06445 154 TTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEvEGKkkVVDVDQSVRPDTSLEKLAKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 229 KSVFQEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDID 308
Cdd:PRK06445 234 PPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDID 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500021509 309 LFHLNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK06445 314 LWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLC 380
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-375 |
6.84e-89 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 273.53 E-value: 6.84e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAG-LGQNVARQVAIKAGIPYKV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 80 PGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYgeeidSKNLKNSMLIDGLTDVYG--EYHM 157
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLP-----AKNGLGHYKSPGMEERYPgiQFSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 158 GITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVP--VRLPNGS--FFEGDETIRANSTLEKLATLKsVFQ 233
Cdd:PRK06504 156 FTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPleITRADGSgeMHTVDEGIRFDATLEGIAGVK-LIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 234 EDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLN 313
Cdd:PRK06504 235 EGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVN 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500021509 314 EAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK06504 315 EAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMC 376
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-374 |
2.32e-88 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 271.25 E-value: 2.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 3 EVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVleRANIAPErIDQVIFGNVLqaGLGQNVARQVAIKAGIPYKVPGV 82
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGMERE-IDDVILGNVV--GPGGNVARLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 83 TINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEIdsknlknsmlidgltdvyGEYHMGITAE 162
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSPETI------------------GDPDMGVAAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 163 NVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPvrlpngsfFEG--DETIRANSTLEKL-ATLKSVFQEDGTVT 239
Cdd:PRK06690 139 YVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILS--------FNGllDESIKKEMNYERIiKRTKPAFLHNGTVT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 240 AGNSSGINDGASAVILMSKEKAIAENI-PYLATIKvTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEAFAS 318
Cdd:PRK06690 211 AGNSCGVNDGACAVLVMEEGQARKLGYkPVLRFVR-SAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFAS 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 500021509 319 QSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASL 374
Cdd:PRK06690 290 KVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATL 345
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-375 |
1.00e-86 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 268.18 E-value: 1.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGK-FGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAG-LGQNVARQVAIKAGIPYK 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAKsWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 79 VPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPlllnpefygEEIDSKNLKNSMLIDGLTDVYgeYHMG 158
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQ---------NEMNRHMLREGWLVEHKPEIY--WSML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 159 ITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGS-------------FFEGDETIRANSTLEKL 225
Cdd:PRK07108 150 QTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVadkatgrlftkevTVSADEGIRPDTTLEGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 226 ATLKSVFqEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSID 305
Cdd:PRK07108 230 SKIRSAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 306 DIDLFHLNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK07108 309 DIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMC 378
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-375 |
1.46e-81 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 256.06 E-value: 1.46e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 4 VVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVPGVT 83
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 84 INEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLnpefygeeidSKNLKnSMLID----------------- 146
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGV----------SKKLA-RALVDlnkartlgqrlklfsrl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 147 GLTDV------YGEY----HMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRL-PNGSFFEGDET 215
Cdd:PRK08963 156 RLRDLlpvppaVAEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVpPYKQPLEEDNN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 216 IRANSTLEKLATLKSVF-QEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDP---AIMGyaPYY 291
Cdd:PRK08963 236 IRGDSTLEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwqdMLLG--PAY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 292 AVNEALAKGEYSIDDIDLFHLNEAFASQSVA--------------VARDLKIPE---EKLNIYGGAIALGHPIGASGARI 354
Cdd:PRK08963 314 ATPLALERAGLTLADLTLIDMHEAFAAQTLAnlqmfaserfarekLGRSQAIGEvdmSKFNVLGGSIAYGHPFAATGARM 393
|
410 420
....*....|....*....|.
gi 500021509 355 VVSLLNELKHENKQVGLASLC 375
Cdd:PRK08963 394 ITQTLHELRRRGGGLGLTTAC 414
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-375 |
7.67e-81 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 252.72 E-value: 7.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAG-LGQNVARQVAIKAGIPYKV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 80 PGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLN--PEFYGEEIDSKNlknsmlIDgLTDVYGeyhm 157
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANagPGRGLPRPDSWD------ID-MPNQFE---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 158 giTAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGSFfEG-----------DETIRaNSTLEKLA 226
Cdd:PRK07850 150 --AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDE-EGqptgetrlvtrDQGLR-DTTMEGLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 227 TLKSVFqEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDD 306
Cdd:PRK07850 226 GLKPVL-EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGD 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500021509 307 IDLFHLNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK07850 305 IDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMC 373
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-375 |
1.27e-75 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 240.45 E-value: 1.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTP--IGKFG-GSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGL-GQNVARQVAIKAGIP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPrgIGKVGkGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 77 YKVPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEE----IDSKNLKnsmlidgLTDVY 152
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGKpplgMGSGNLR-------LRALH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 153 GEYHMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGSF-FEGDETIRANSTLEKLATLKSV 231
Cdd:PRK06025 154 PQSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGSVaLDHEEFPRPQTTAEGLAALKPA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 232 FQ-------EDGTVT-------------------AGNSSGINDGASAVILMSKEKAIAENIPYLATIKVTSEVGVDPAIM 285
Cdd:PRK06025 234 FTaiadyplDDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 286 GYAPYYAVNEALAKGEYSIDDIDLFHLNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHPIGASGARIVVSLLNELKHE 365
Cdd:PRK06025 314 LNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERR 393
|
410
....*....|
gi 500021509 366 NKQVGLASLC 375
Cdd:PRK06025 394 GLKRGLVTMC 403
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-375 |
1.22e-60 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 201.67 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVP 80
Cdd:PRK09268 6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 81 GVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEF------------YGEEIDS-KNLKNSMLI-- 145
Cdd:PRK09268 86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLrkillelnraktTGDRLKAlGKLRPKHLApe 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 146 --------DGLTdvygeyhMGITAENVAKKFAVSREEQDKFAHNSQMKAANAQEKNLFEEEIVPvrlpngsfFEG---DE 214
Cdd:PRK09268 166 iprngeprTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITP--------FLGltrDN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 215 TIRANSTLEKLATLKSVF--QEDGTVTAGNSSGINDGASAVILMSKEKAIAENIPYLATIkVTSEV-------GVDPAIM 285
Cdd:PRK09268 231 NLRPDSSLEKLAKLKPVFgkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYL-VDAETaavdfvhGKEGLLM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 286 gyAPYYAVNEALAKGEYSIDDIDLFHLNEAFASQSVAVARDLKIPE-----------------EKLNIYGGAIALGHPIG 348
Cdd:PRK09268 310 --APAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEycrerlgldaplgsidrSKLNVNGSSLAAGHPFA 387
|
410 420
....*....|....*....|....*..
gi 500021509 349 ASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:PRK09268 388 ATGGRIVATLAKLLAEKGSGRGLISIC 414
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
9-375 |
2.86e-60 |
|
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: 200.03 E-value: 2.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 9 AARTPIGKFGGSLK---DVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVPGVTIN 85
Cdd:cd00826 3 AAMTAFGKFGGENGadaNDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 86 EVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAplllnpefygeeidSKNLKNSMLIDGLTDVYGeyhmgitaenva 165
Cdd:cd00826 83 NLCGSGLRALALAMQLIAGGDANCILAGGFEKMETS--------------AENNAKEKHIDVLINKYG------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 166 kkfavSREEQDKFAHNSQMKAANAQEKNLFEEEIVPVRLPNGsffEGDETIRAN--------STLEKLATLKSVFQEDGT 237
Cdd:cd00826 137 -----MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGR---KGDIHSDADeyiqfgdeASLDEIAKLRPAFDKEDF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 238 VTAGNSSGINDGASAVILMSKEKA-------IAENIPYLATIKVTSEVGVDPA----IMGYAPYYAVNEALAKGEYSIDD 306
Cdd:cd00826 209 LTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 307 IDLFHLNEAFASQSVAVARDLKI-PEEK-----------------LNIYGGAIALGHPIGASGARIVVSLLNELKHENKQ 368
Cdd:cd00826 289 LDLIEAHDAFAANACATNEALGLcPEGQggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGK 368
|
410
....*....|..
gi 500021509 369 V-----GLASLC 375
Cdd:cd00826 369 RqgagaGLALLC 380
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
267-375 |
3.23e-47 |
|
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: 157.03 E-value: 3.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 267 PYLATIKVTSEVGVDPAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEAFASQSVAVARDLKIPEEKLNIYGGAIALGHP 346
Cdd:pfam02803 2 KPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHP 81
|
90 100
....*....|....*....|....*....
gi 500021509 347 IGASGARIVVSLLNELKHENKQVGLASLC 375
Cdd:pfam02803 82 LGASGARILVTLLHELKRRGGKYGLASLC 110
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
7-365 |
9.44e-23 |
|
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: 98.49 E-value: 9.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 7 IDAARTPIGKFGgslkDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKvPGVTINE 86
Cdd:cd00829 1 VGVGMTPFGRRS----DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGK-PATRVEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 87 VCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPLLLNPEFYGEEIDsKNLKNSMLIDGLTDVYGEY---HMgitaen 163
Cdd:cd00829 76 AGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLE-WEGPEPPGGLTPPALYALAarrYM------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 164 vaKKFAVSREEQDKFAhnsqMKA-ANAQeKNlfeeeivpvrlPNGSFfegdetiRANSTLEKLatLKS--VFqedGTVTA 240
Cdd:cd00829 149 --HRYGTTREDLAKVA----VKNhRNAA-RN-----------PYAQF-------RKPITVEDV--LNSrmIA---DPLRL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 241 GNSSGINDGASAVILMSKEKA--IAENIPYLATIkvtsEVGVDPAIMGYAPYY--------AVNEALAKGEYSIDDIDLF 310
Cdd:cd00829 199 LDCCPVSDGAAAVVLASEERAreLTDRPVWILGV----GAASDTPSLSERDDFlsldaarlAARRAYKMAGITPDDIDVA 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500021509 311 HLNEAFAS---------------------QSVAVARDLKIPeekLNIYGGAIALGHPIGASGARIVVSLLNELKHE 365
Cdd:cd00829 275 ELYDCFTIaellaledlgfcekgeggklvREGDTAIGGDLP---VNTSGGLLSKGHPLGATGLAQAVEAVRQLRGE 347
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-365 |
1.53e-18 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 86.49 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKfggsLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLqAGL--GQ-NVARQVAIKAGIPy 77
Cdd:PRK06064 1 MRDVAIIGVGQTKFGE----LWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMS-AGLfvSQeHIAALIADYAGLA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 78 KVPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAPlllnpefyGEEIDSknlknsmLIDGLTDVYGEYHM 157
Cdd:PRK06064 75 PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVP--------TPDATE-------AIARAGDYEWEEFF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 158 GIT--------AENVAKKFAVSREEQDKFAHNSQMKAAN---AQeknlFEEEIvpvrlpngsffegdetiransTLEKLa 226
Cdd:PRK06064 140 GATfpglyaliARRYMHKYGTTEEDLALVAVKNHYNGSKnpyAQ----FQKEI---------------------TVEQV- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 227 tLKSVFQEDgTVTAGNSSGINDGASAVILMSKEKA--IAENIPYLATIKV---TSEVGVDPAIMGY-APYYAVNEALAKG 300
Cdd:PRK06064 194 -LNSPPVAD-PLKLLDCSPITDGAAAVILASEEKAkeYTDTPVWIKASGQasdTIALHDRKDFTTLdAAVVAAEKAYKMA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 301 EYSIDDIDLFHLNEAFASQSVAVARDL---------------------KIPeekLNIYGGAIALGHPIGASGARIVVSLL 359
Cdd:PRK06064 272 GIEPKDIDVAEVHDCFTIAEILAYEDLgfakkgeggklaregqtyiggDIP---VNPSGGLKAKGHPVGATGVSQAVEIV 348
|
....*.
gi 500021509 360 NELKHE 365
Cdd:PRK06064 349 WQLRGE 354
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
29-367 |
6.98e-18 |
|
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: 82.49 E-value: 6.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 29 LGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPyKVPGVTINEVCGSGLKAIMLGRQAIQLGEAD 108
Cdd:cd00327 10 LGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNGKAD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 109 IVAVGGTEnmsqaplllnpefygeeidsknlknsmlidgltdvygeyhmgitaenvakkfavsreeqdkfahnsqmkaan 188
Cdd:cd00327 89 IVLAGGSE------------------------------------------------------------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 189 aqeknlfeeeivpvrlpngsffegdetiranstleklatlksvfqedgtvtagnSSGINDGASAVILMSKEKAIAENIPY 268
Cdd:cd00327 97 ------------------------------------------------------EFVFGDGAAAAVVESEEHALRRGAHP 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 269 LATIKVTSEVGVD----PAIMGYAPYYAVNEALAKGEYSIDDIDLFHLNEAFASQSVAVARDLKIPEEK---LNIYGGAI 341
Cdd:cd00327 123 QAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGvrsPAVSATLI 202
|
330 340
....*....|....*....|....*.
gi 500021509 342 ALGHPIGASGARIVVSLLNELKHENK 367
Cdd:cd00327 203 MTGHPLGAAGLAILDELLLMLEHEFI 228
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
16-365 |
8.25e-13 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 69.10 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 16 KFGGSlKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKVPgVTINEVCGSGLKAI 95
Cdd:PRK12578 12 KFGRR-DDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVP-LRVEAMCATGLAAS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 96 MLGRQAIQLGEADIVAVGGTENMSqaplllnpefygeEIDSknlKNSMLIDGLTDVY-GEYHM-GIT-----AENVAKKF 168
Cdd:PRK12578 90 LTAYTAVASGLVDMAIAVGVDKMT-------------EVDT---STSLAIGGRGGNYqWEYHFyGTTfptyyALYATRHM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 169 AV--SREEQDKFAHNSQMKAANAQEKNLFEEEIvpvrlpngsffegdetiransTLEKLatLKSVFQEdGTVTAGNSSGI 246
Cdd:PRK12578 154 AVygTTEEQMALVSVKAHKYGAMNPKAHFQKPV---------------------TVEEV--LKSRAIS-WPIKLLDSCPI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 247 NDGASAVILMSKEKaiaenipylatikvTSEVGVDPAI----MGYAPYY-----------------AVNEALAKGEYSID 305
Cdd:PRK12578 210 SDGSATAIFASEEK--------------VKELKIDSPVwitgIGYANDYayvarrgewvgfkatqlAARQAYNMAKVTPN 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500021509 306 DIDLFHLNEAFASQSVAVARDL---------KIPEE---------KLNIYGGAIALGHPIGASGARIVVSLLNELKHE 365
Cdd:PRK12578 276 DIEVATVHDAFTIAEIMGYEDLgftekgkggKFIEEgqsekggkvGVNLFGGLKAKGHPLGATGLSMIYEITKQLRDE 353
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
28-356 |
1.34e-08 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 56.23 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 28 DLGAIALKGVLERANIAPERIDQVIFGNV---LQAGLGQNVARQVAIKAGIpYKVPGVTINEVCGSGLKAIMLGRQAIQL 104
Cdd:PRK06289 28 DLTREVVDGTLAAAGVDADDIEVVHVGNFfgeLFAGQGHLGAMPATVHPAL-WGVPASRHEAACASGSVATLAAMADLRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 105 GEADIVAVGGTENMSQAP------LLLNPEFYGEEI-DSKNLKNSMLIDgLTDVYG------EYHMGITAENvakKFAVS 171
Cdd:PRK06289 107 GRYDVALVVGVELMKTVPgdvaaeHLGAAAWTGHEGqDARFPWPSMFAR-VADEYDrrygldEEHLRAIAEI---NFANA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 172 ReeqdkfahnsqmKAANAQEKNLFeeeivpvrLPNGSFFEGDETiraNSTLEklatlksvfqedGTVTAGNSSGINDGAS 251
Cdd:PRK06289 183 R------------RNPNAQTRGWA--------FPDEATNDDDAT---NPVVE------------GRLRRQDCSQVTDGGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 252 AVILMSKekAIAENIPYLATIKVTSEVGVDPAIMGYA---------PYY------AVNEALAKGEYSIDDIDLFHLNEAF 316
Cdd:PRK06289 228 GVVLASD--AYLRDYADARPIPRIKGWGHRTAPLGLEqkldrsagdPYVlphvrqAVLDAYRRAGVGLDDLDGFEVHDCF 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500021509 317 -ASQSVA--------------------VARDLKIPeekLNIYGGAIALGHPIGASGARIVV 356
Cdd:PRK06289 306 tPSEYLAidhigltgpgeswkaiengeIAIGGRLP---INPSGGLIGGGHPVGASGVRMLL 363
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
22-120 |
1.63e-07 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 52.42 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 22 KDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPyKVPGVTINEVCGSGLKAIMLGRQA 101
Cdd:COG0332 47 PDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLFPSTACLVQHKLGAK-NAAAFDINAACSGFVYALSVAAAL 125
|
90
....*....|....*....
gi 500021509 102 IQLGEADIVAVGGTENMSQ 120
Cdd:COG0332 126 IRSGQAKNVLVVGAETLSR 144
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-351 |
2.46e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 52.26 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 1 MKEVVIIDAARTPIGKfggsLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGnVLQAGL-GQNVARQVAIKA--GIPY 77
Cdd:PRK07516 1 MMTASIVGWAHTPFGK----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLG-HFNAGFsPQDFPASLVLQAdpALRF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 78 KvPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENMSQAP------LLLNPEFYGEEIDSKNlknsmlidGLTDV 151
Cdd:PRK07516 76 K-PATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPtaevgdILLGASYLKEEGDTPG--------GFAGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 152 YGEyhmgiTAENVAKKFavsREEQDKFAhnsqMKAAnaqeKNlfeeeivpvrlpngsffegdetiRANSTLEKLATLKSV 231
Cdd:PRK07516 147 FGR-----IAQAYFQRY---GDQSDALA----MIAA----KN-----------------------HANGVANPYAQMRKD 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 232 FQED--GTVTAGNS-----------SGINDGASAVILMSKEkaIAENIPYLATIKVTSEVG-------VDPAIMGyAPYY 291
Cdd:PRK07516 188 LGFEfcRTVSEKNPlvagplrrtdcSLVSDGAAALVLADAE--TARALQRAVRFRARAHVNdflplsrRDPLAFE-GPRR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 292 AVNEALAKGEYSIDDIDLFHLNEAF---------------------ASQSVAVARDLKIPeekLNIYGGAIALGHPIGAS 350
Cdd:PRK07516 265 AWQRALAQAGVTLDDLSFVETHDCFtiaelieyeamglappgqgarAIREGWTAKDGKLP---VNPSGGLKAKGHPIGAT 341
|
.
gi 500021509 351 G 351
Cdd:PRK07516 342 G 342
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
65-116 |
1.56e-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: 49.84 E-value: 1.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 500021509 65 VARQVAIKAGIpyKVPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTE 116
Cdd:cd00834 140 AAGQVAIRLGL--RGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
17-128 |
5.54e-06 |
|
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: 47.24 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 17 FGGSLKDVSAVD----LGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPYKV------------- 79
Cdd:pfam00109 74 FGISPREAERMDpqqrLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPRRGspfavgtmpsvia 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 80 -----------PGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTEnmsqapLLLNPE 128
Cdd:pfam00109 154 grisyflglrgPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVN------LLLTPL 207
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
65-116 |
6.80e-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: 47.78 E-value: 6.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 500021509 65 VARQVAIKAGIpyKVPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTE 116
Cdd:COG0304 140 AAGHVSIRFGL--KGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
28-118 |
2.14e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 42.96 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 28 DLGAIALKGVLERANIAPERIDQVIFGNVLqaglGQNVARQVAIkagipYKV-----PGVTINEVCGSGLKAIMLGRQAI 102
Cdd:PRK08256 24 DMAAEAGRAALADAGIDYDAVQQAYVGYVY----GDSTSGQRAL-----YEVgmtgiPIVNVNNNCSTGSTALFLARQAV 94
|
90
....*....|....*.
gi 500021509 103 QLGEADIVAVGGTENM 118
Cdd:PRK08256 95 RSGAADCALALGFEQM 110
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
23-119 |
5.54e-04 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 41.37 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 23 DVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPyKVPGVTINEVCGSGLKAIMLGRQAI 102
Cdd:cd00830 47 GETTSDLAVEAAKKALEDAGIDADDIDLIIVATSTPDYLFPATACLVQARLGAK-NAAAFDINAACSGFLYGLSTAAGLI 125
|
90
....*....|....*..
gi 500021509 103 QLGEADIVAVGGTENMS 119
Cdd:cd00830 126 RSGGAKNVLVVGAETLS 142
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
288-368 |
1.50e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 40.28 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 288 APYYAVNEALAKGeySIDDIDLFHLNEAFASQSVAVARDLKI--------------PEEK----LNIYGGAIALGHPIGA 349
Cdd:PRK06365 298 AAKEAYEMAGITD--PLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgkPELPgklpVNPSGGLLAAGHAVGA 375
|
90
....*....|....*....
gi 500021509 350 SGARIVVSLLNELKHENKQ 368
Cdd:PRK06365 376 TGIMQAVFMFWQLQGRIKK 394
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
65-118 |
1.70e-03 |
|
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: 39.93 E-value: 1.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 500021509 65 VARQVAIKAGIpyKVPGVTINEVCGSGLKAIMLGRQAIQLGEADIVAVGGTENM 118
Cdd:cd00825 75 ASGQIATPLGI--HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEEL 126
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
246-354 |
2.90e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 39.29 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 246 INDGASAVILMSKEKA--IAENIPYLATIkvtsEVGVDPAIMGY-----APYYAVNEALAKGEySIDDIDLFHLNEAFAS 318
Cdd:PRK07937 204 ITDGAAAVVLAAGDRAreLRERPAWITGI----EHRIESPSLGArdltrSPSTALAAEAATGG-DAGGVDVAELHAPFTH 278
|
90 100 110
....*....|....*....|....*....|....*...
gi 500021509 319 QSVAVARDLKIPEE-KLNIYGGAIAlGHPIGASG-ARI 354
Cdd:PRK07937 279 QELILREALGLGDKtKVNPSGGALA-ANPMFAAGlERI 315
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-124 |
8.91e-03 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 37.80 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021509 5 VIIDAARTPIGKFGGSLKDVSAVDLGAIALKGVLERANIAPERIDQVIFGNVLQAGLGQNVARQVAIKAGIPyKVPGVTI 84
Cdd:cd00827 27 VDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYLAELLGLT-NAEAFDL 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 500021509 85 NEVCGSGLKAIMLGRQAIQLGE--------ADIVAVGGTENMSQAPLL 124
Cdd:cd00827 106 KQACYGGTAALQLAANLVESGPwryalvvaSDIASYLLDEGSALEPTL 153
|
|
| |
