|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-389 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 635.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVP 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 81 SFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGFKMGNQTLEDSMIADGLTDKFNDYHMGIT 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 161 AENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDPLIISQDEGIRPQTTIDKLAQLRPAFKKDG 240
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 241 SVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAF 320
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080967136 321 AAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQL--SDAKpTGVASLCIGGGQGIATVV 389
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMkrRGAK-KGLATLCIGGGQGVALIV 390
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-389 |
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: 606.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVP 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 81 SFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGFKMgNQTLEDSMIADGLTDKFNDYHMGIT 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 161 AENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDpLIISQDEGIRPQTTIDKLAQLRPAFKKDG 240
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKPAFKKDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 241 SVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAF 320
Cdd:COG0183 239 TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080967136 321 AAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQL--SDAKpTGVASLCIGGGQGIATVV 389
Cdd:COG0183 319 AAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELerRGGR-YGLATMCIGGGQGIALII 388
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-389 |
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: 595.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 5 VLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVPSFTV 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 85 NKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGFKMGNQTLeDSMIADGLTDKFNDYHMGITAENL 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 165 VEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGdPLIISQDEGIRPQTTIDKLAQLRPAFKKDGSVTA 244
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKG-PVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 245 GNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAFAAQS 324
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080967136 325 IAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQL--SDAKpTGVASLCIGGGQGIATVV 389
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELkrRGGR-YGLATMCIGGGQGAAMVI 384
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
7-389 |
0e+00 |
|
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: 511.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 7 AEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVPSFTVNK 86
Cdd:TIGR01930 2 VAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 87 VCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNS-RFGFKMGNQTLEDSMIADgLTDKFNDYHMGITAENLV 165
Cdd:TIGR01930 82 QCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 166 EQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGdPLIISQDEGIRPQTTIDKLAQLRPAFKKDGSVTAG 245
Cdd:TIGR01930 161 KKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKG-PVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 246 NASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAFAAQSI 325
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080967136 326 AVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLSDAKPT-GVASLCIGGGQGIATVV 389
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRyGLATMCIGGGQGAAVIL 384
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.07e-172 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 487.47 E-value: 1.07e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVP 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 81 SFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGFKMGNQTLEDSMIADGLTDKFNDYHMGIT 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 161 AENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDPLIISQDEGIRPQTTIDKLAQLRPAFKKDG 240
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 241 SVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAF 320
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080967136 321 AAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQL--SDAKpTGVASLCIGGGQGIATVVSK 391
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMirRDAK-KGLATLCIGGGQGVALAIER 392
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-389 |
1.58e-166 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 471.50 E-value: 1.58e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVP 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 81 SFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGFKMGNQTLEDSMIADGLTDKFNDYHMGIT 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 161 AENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDPLIISQDEGIRPQTTIDKLAQLRPAFKKDG 240
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 241 SVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAF 320
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 321 AAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLSD-AKPTGVASLCIGGGQGIATVV 389
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrGGGIGIAAICSGGGQGDAVLI 390
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-388 |
2.14e-158 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 450.95 E-value: 2.14e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAG-QGQNPARIAAIHGGVPEAV 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEpRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 80 PSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGFKMGNQTLEDSMIAdGLTDKFNDYHMGI 159
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMVG-ALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 160 TAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDpLIISQDEGIRPQTTIDKLAQLRPAFKKD 239
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGE-VVFDTDEHVRADTTLEDLAKLKPVFKKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 240 -GSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNE 318
Cdd:PRK09051 240 nGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080967136 319 AFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLsdaKPTG----VASLCIGGGQGIATV 388
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYEL---QRIGgryaLVTMCIGGGQGIAAI 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-389 |
6.98e-151 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 432.49 E-value: 6.98e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGnvlQA-GQGQNPA--RIAAIHGGVPE 77
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFG---QGyPNGEAPAigRVAALDAGLPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 78 AVPSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGFKMGNQTLEDSmIADGLTDKFNDYH- 156
Cdd:PRK06205 78 TVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDR-LARGRETAGGRRFp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 157 ----MGITAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDPLIISQDEGIRPQTTIDKLAQL 232
Cdd:PRK06205 157 vpggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLAKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 233 RP---AFKKDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVIN 309
Cdd:PRK06205 237 RPimgKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 310 DVDIFELNEAFAAQSIAVNRELQLPQD---KVNVNGGAIALGHPIGASGARTLVSLLHQLS--DAKpTGVASLCIGGGQG 384
Cdd:PRK06205 317 DIDLIELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQrrQAR-YGLETMCIGGGQG 395
|
....*
gi 1080967136 385 IATVV 389
Cdd:PRK06205 396 LAAVF 400
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
4-389 |
7.30e-147 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 421.75 E-value: 7.30e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 4 IVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVPSFT 83
Cdd:PRK06633 5 VYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 84 VNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSpMLLKNSRFGFKMGNQTLEDSMIADGLTDKFNDYHMGITAEN 163
Cdd:PRK06633 85 INKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLG-MHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 164 LVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDPLIiSQDEGIRPQTTIDKLAQLRPAFKKDGSVT 243
Cdd:PRK06633 164 ISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLF-DHDETVRPDTSLEILSKLRPAFDKNGVVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 244 AGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAFAAQ 323
Cdd:PRK06633 243 AGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQ 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080967136 324 SIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLSDAKP-TGVASLCIGGGQGIATVV 389
Cdd:PRK06633 323 SIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAkKGLVTLCIGGGMGMAMCV 389
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
4-389 |
4.55e-145 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 417.19 E-value: 4.55e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 4 IVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVPSFT 83
Cdd:PLN02644 3 VCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 84 VNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGFKMGNQTLEDSMIADGLTDKFNDYHMGITAEN 163
Cdd:PLN02644 83 VNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 164 LVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDP-LIISQDEGIRpQTTIDKLAQLRPAFKKD-GS 241
Cdd:PLN02644 163 CADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPsVIVDKDEGLG-KFDPAKLRKLRPSFKEDgGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 242 VTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAFA 321
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 322 AQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQL--SDAKpTGVASLCIGGGQGIATVV 389
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLrsKNGK-YGVAGICNGGGGASAIVV 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-391 |
2.04e-144 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 415.89 E-value: 2.04e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILE-HSQIDPNEINEVILGNVLQAGQ-GQNPARIAAIHGGVPEA 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMArNPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 79 VPSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGFKMgNQTLEDSMIA-----DGLTDKFN 153
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSR-QAEIFDTTIGwrfvnPLMKAQYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 154 DYHMGITAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDPLIISQDEGIRPQTTIDKLAQLR 233
Cdd:PRK09050 160 VDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALAKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 234 PAFKKDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDI 313
Cdd:PRK09050 240 PVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 314 FELNEAFAAQSIAVNRELQLPQD--KVNVNGGAIALGHPIGASGARTLVSLLHQLS-DAKPTGVASLCIGGGQGIATVVS 390
Cdd:PRK09050 320 IELNEAFAAQGLAVLRQLGLADDdaRVNPNGGAIALGHPLGMSGARLVLTALHQLErTGGRYALCTMCIGVGQGIALAIE 399
|
.
gi 1080967136 391 K 391
Cdd:PRK09050 400 R 400
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-388 |
3.78e-130 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 378.92 E-value: 3.78e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIG-VFGGVFKDIPAYELGATVIRQILE-HSQIDPNEINEVILGNVLQAG-QGQNPARIAAIHGGVPE 77
Cdd:PRK08947 1 MEDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLArNPALDPAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 78 AVPSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLlKNSRFGFKMGNQTLEDSMIadgltdkfndyhM 157
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMN-HGVDFHPGLSKNVAKAAGM------------M 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 158 GITAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDPLIISQDEGIRPQTTIDKLAQLRPAFK 237
Cdd:PRK08947 148 GLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 238 -KDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFEL 316
Cdd:PRK08947 228 pVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080967136 317 NEAFAAQSIAVNRELQL---PQDKVNVNGGAIALGHPIGASGARTLVSLLHQLSDAKPT-GVASLCIGGGQGIATV 388
Cdd:PRK08947 308 NEAFAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQfGLATMCIGLGQGIATV 383
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
4-391 |
7.88e-128 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 375.64 E-value: 7.88e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 4 IVLAEAYRTPI--GVFGGvFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAG-QGQNPARIAAIHGGVPEAVP 80
Cdd:PLN02287 48 VVIVAAYRTPIckAKRGG-FKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGsQRANECRMAAFYAGFPETVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 81 SFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMllknsRFGFKMGNQTLEDSMIADGLTDkfndyhMGIT 160
Cdd:PLN02287 127 VRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPM-----AWEGGVNPRVESFSQAQDCLLP------MGIT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 161 AENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVE---VPQRKGD--PLIISQDEGIRPQTTIDKLAQLRPA 235
Cdd:PLN02287 196 SENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHtkiVDPKTGEekPIVISVDDGIRPNTTLADLAKLKPV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 236 FKKDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFE 315
Cdd:PLN02287 276 FKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 316 LNEAFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQL----SDAKpTGVASLCIGGGQGIATVVSK 391
Cdd:PLN02287 356 INEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMkrrgKDCR-FGVVSMCIGTGMGAAAVFER 434
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-388 |
1.45e-123 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 362.53 E-value: 1.45e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIG-VFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVL-QAGQGQNPARIAAIHGGVPEA 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 79 VPSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMllknsrfgfkMGNQTLEDSMIADgltdKFNDYHMG 158
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPM----------MGHVVRPNPRLVE----AAPEYYMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 159 I--TAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDP--------LIISQDEGIRPQTTIDK 228
Cdd:PRK07661 147 MghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGEnnklqeetITFSQDEGVRADTTLEI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 229 LAQLRPAFKKDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVI 308
Cdd:PRK07661 227 LGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLEL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 309 NDVDIFELNEAFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLS-DAKPTGVASLCIGGGQGIAT 387
Cdd:PRK07661 307 SDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKrRNEQFGIVTMCIGGGMGAAG 386
|
.
gi 1080967136 388 V 388
Cdd:PRK07661 387 V 387
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-386 |
6.05e-123 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 361.13 E-value: 6.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVP 80
Cdd:PRK06954 6 QDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 81 SFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGFKMGNQTLEDSMIADGLTDKFNDYH-MGI 159
Cdd:PRK06954 86 CTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 160 TAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDpLIISQDEGIRpQTTIDKLAQLRPAFKKD 239
Cdd:PRK06954 166 FAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGD-TVIDRDEQPF-KANPEKIPTLKPAFSKT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 240 GSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEA 319
Cdd:PRK06954 244 GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEA 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080967136 320 FAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQL-SDAKPTGVASLCIGGGQGIA 386
Cdd:PRK06954 324 FAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALrARGGKRGVASLCIGGGEATA 391
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-263 |
6.35e-123 |
|
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: 355.84 E-value: 6.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 4 IVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVPSFT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 84 VNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLL-KNSRFGFKMGNQTLEDSMIADGLTDKFNDYHMGITAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 163 NLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDPlIISQDEGIRPQTTIDKLAQLRPAFKKDGSV 242
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
|
250 260
....*....|....*....|.
gi 1080967136 243 TAGNASGINDGAAAMLVMTED 263
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
9-386 |
5.15e-121 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 356.24 E-value: 5.15e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 9 AYRTPIG-VFGGVFKDIPAYELGATVIRQIL-EHSQIDPNEINEVILGNVL-QAGQGQNPARIAAIHGGVPEAVPSFTVN 85
Cdd:PRK09052 13 ATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVaQVPGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPNSVGGVTVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 86 KVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMllknsrfgfkMGNQTLEDSMIADGLTDKFNDYHMGITAENLV 165
Cdd:PRK09052 93 RFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM----------MGNKPSMSPAIFARDENVGIAYGMGLTAEKVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 166 EQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDP---------LIISQDEGIRPQTTIDKLAQLRPAF 236
Cdd:PRK09052 163 EQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDLatgevdvktRTVDLDEGPRADTSLEGLAKLKPVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 237 KKDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFEL 316
Cdd:PRK09052 243 ANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIEL 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080967136 317 NEAFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLSDAK-PTGVASLCIGGGQGIA 386
Cdd:PRK09052 323 NEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNlKYGMVTMCVGTGMGAA 393
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-389 |
3.83e-117 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 346.61 E-value: 3.83e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIG-VFGGVFKDIPAYELGATVIRQILEH-SQIDPNEINEVILGNVLQAG-QGQNPARIAAIHGGVPe 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKvPALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 78 AVPSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSqspmllknsrfGFKMGNqtledsmiADGLTDKFN---- 153
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVS-----------RFAKGN--------SDSLPDTKNplfa 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 154 ---------------DYH--------------MGITAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEV 204
Cdd:PRK07851 141 eaqartaaraeggaeAWHdpredgllpdvyiaMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 205 PqrkgDPLIISQDEGIRPQTTIDKLAQLRPAFKKDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGV 284
Cdd:PRK07851 221 P----DGTVVSTDDGPRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 285 APSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLH 364
Cdd:PRK07851 297 SPEIMGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLN 376
|
410 420
....*....|....*....|....*.
gi 1080967136 365 QL-SDAKPTGVASLCIGGGQGIATVV 389
Cdd:PRK07851 377 NLqTHDKTFGLETMCVGGGQGMAMVL 402
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-384 |
2.87e-115 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 341.22 E-value: 2.87e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVP 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 81 SFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNS-RFGFKM---GNQTLEDSMIADGLTDKFNDYH 156
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDlRWGPKHllhKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 157 MGITAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVpqrkgdpliISQDEGIRpQTTIDKLAQLRPAF 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND---------LDRDEGIR-KTTMEDLAKLPPAF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 237 KKDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFEL 316
Cdd:PRK06366 231 DKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEH 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080967136 317 NEAFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLSDAK-PTGVASLCIGGGQG 384
Cdd:PRK06366 311 NEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHmKTGLATLCHGGGGA 379
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
20-392 |
6.44e-115 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 340.55 E-value: 6.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 20 VFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQ-----GQNPARIAAIhggvPEAVPSFTVNKVCGSGLKA 94
Cdd:PRK06445 26 VFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGEnwlygGRHPIFLARL----PYNIPAMAVDRQCASSLTT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 95 IQLAYQSIVAGDNEIVIAGGMESMSQSPMLlKNSRFGFKMGNQTLEDSMIADGLTDkfndYHMGITAENLVEQYQISRKE 174
Cdd:PRK06445 102 VSIGAMEIATGMADIVIAGGVEHMTRTPMG-DNPHIEPNPKLLTDPKYIEYDLTTG----YVMGLTAEKLAEEAGIKREE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 175 QDQFAFDSQQKASRAQQAGVFDAEIVPVEVpQRKGDPLIISQDEGIRPQTTIDKLAQLRPAFKKDGSVTAGNASGINDGA 254
Cdd:PRK06445 177 MDRWSLRSHQLAAKAIQEGYFKDEILPIEV-EVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKPDGVITAGNSSPLNSGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 255 AAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAFAAQSIAVNRELQLP 334
Cdd:PRK06445 256 SYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLD 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080967136 335 QDKVNVNGGAIALGHPIGASGARTLVSLLHQLS-DAKPTGVASLCIGGGQGIATVVSKY 392
Cdd:PRK06445 336 PETVNIKGGAIAIGHPLGATGARIVGTLARQLQiKGKDYGVATLCVGGGQGGAVVLERV 394
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
11-391 |
5.17e-108 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 323.27 E-value: 5.17e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 11 RTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQ-GQNPARIAAIHGGVPEAVPSFTVNKVCG 89
Cdd:PRK08131 11 RSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTVNRLCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 90 SGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKN-----SRfGFKMGNQTLEDSMIADGLTDKFNDYHMGITAENL 164
Cdd:PRK08131 91 SGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKaesafSR-DAKVFDTTIGARFPNPKIVAQYGNDSMPETGDNV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 165 VEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQ-RKGDPLIISQDEGIRPQTTIDKLAQLRPAFKkDGSVT 243
Cdd:PRK08131 170 AAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgRKLPPKLVAEDEHPRPSSTVEALTKLKPLFE-GGVVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 244 AGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAFAAQ 323
Cdd:PRK08131 249 AGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEAFASQ 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080967136 324 SIAVNRELQLPQD--KVNVNGGAIALGHPIGASGARTLVSLLHQLSD-AKPTGVASLCIGGGQGIATVVSK 391
Cdd:PRK08131 329 VLGCLKGLGVDFDdpRVNPNGGAIAVGHPLGASGARLALTAARELQRrGKRYAVVSLCIGVGQGLAMVIER 399
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
8-389 |
3.17e-99 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 300.65 E-value: 3.17e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 8 EAYRTPIGVF--GGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAG-QGQNPARIAAIHGGVPEAVPSFTV 84
Cdd:PRK08242 8 DAVRTPRGKGkkDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPGVQI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 85 NKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMllknsrfGFKMGNQTLEDSMiadgltdKFNDYHM--GITAE 162
Cdd:PRK08242 88 NRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPM-------GSDGGAWAMDPST-------NFPTYFVpqGISAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 163 NLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEvpQRKGdPLIISQDEGIRPQTTIDKLAQLRPAFKKDGSV 242
Cdd:PRK08242 154 LIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK--DQNG-LTILDHDEHMRPGTTMESLAKLKPSFAMMGEM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 243 ---------------------TAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKAL 301
Cdd:PRK08242 231 ggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 302 KRSNKVINDVDIFELNEAFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQL--SDAKpTGVASLCI 379
Cdd:PRK08242 311 AKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELerRGKR-TALITLCV 389
|
410
....*....|
gi 1080967136 380 GGGQGIATVV 389
Cdd:PRK08242 390 GGGMGIATII 399
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-388 |
1.48e-98 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 298.61 E-value: 1.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIG-VFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAG-QGQNPARIAAIHGGVPEA 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 79 VPSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSqspmLLKNsrfgfKMGNQTLEDSMIADGLTDKFndYHMG 158
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIS----CVQN-----EMNRHMLREGWLVEHKPEIY--WSML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 159 ITAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDP---------LIISQDEGIRPQTTIDKL 229
Cdd:PRK07108 150 QTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKatgrlftkeVTVSADEGIRPDTTLEGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 230 AQLRPAFKkDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVIN 309
Cdd:PRK07108 230 SKIRSALP-GGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 310 DVDIFELNEAFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARtLVSllHQLSDAKPTG----VASLCIGGGQGI 385
Cdd:PRK07108 309 DIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGAR-LTG--HALIEGKRRGakyvVVTMCIGGGQGA 385
|
...
gi 1080967136 386 ATV 388
Cdd:PRK07108 386 AGL 388
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
26-389 |
2.31e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 296.54 E-value: 2.31e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 26 AYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVPSFTVNKVCGSGLKAIQLAYQSIVAG 105
Cdd:PRK08170 27 ASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 106 DNEIVIAGGMESMSQSPMLLKNSR---FGFKMGNQTLEDSMIA----------------DGLTDKFNDYHMGITAENLVE 166
Cdd:PRK08170 107 RADLVLAGGVEAMSHAPLLFSEKMvrwLAGWYAAKSIGQKLAAlgklrpsylapvigllRGLTDPVVGLNMGQTAEVLAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 167 QYQISRKEQDQFAFDSQQKASRAQQAGVFdAEIVPVEVPQRKgdplIISQDEGIRPQTTIDKLAQLRPAF-KKDGSVTAG 245
Cdd:PRK08170 187 RFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPLFDRDGK----FYDHDDGVRPDSSMEKLAKLKPFFdRPYGRVTAG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 246 NASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAFAAQSI 325
Cdd:PRK08170 262 NSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 326 AVNRELQ-----------------LPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLSDAKPT-GVASLCIGGGQGIAT 387
Cdd:PRK08170 342 ACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGTKrGIAAICIGGGQGGAM 421
|
..
gi 1080967136 388 VV 389
Cdd:PRK08170 422 LL 423
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-393 |
4.15e-94 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 286.28 E-value: 4.15e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 3 RIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQIlehSQIDPNEINEVILGNVLqaGQGQNPARIAAIHGGVPEAVPSF 82
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL---SKGMEREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 83 TVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLlKNSRFGfkmgnqtledsmiadglTDKFNDYHMGITAE 162
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQ-NRARFS-----------------PETIGDPDMGVAAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 163 NLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVevpqrkgDPLIisqDEGIRPQTTIDKLAQ-LRPAFKKDGS 241
Cdd:PRK06690 139 YVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF-------NGLL---DESIKKEMNYERIIKrTKPAFLHNGT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 242 VTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAFA 321
Cdd:PRK06690 209 VTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFA 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080967136 322 AQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLS--DAKpTGVASLCIGGGQGIATVVSKYE 393
Cdd:PRK06690 289 SKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKreDMK-YGIATLGIGGGIGLALLFEKVE 361
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
6-389 |
1.45e-91 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 280.85 E-value: 1.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 6 LAEAY-----RTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAG-QGQNPARIAAIHGGVPEAV 79
Cdd:PRK06504 1 MAEAYivaaaRTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 80 PSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLkNSRFGFKMG-NQTLEDSMIADGLTDKFNDYhMG 158
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGS-PSTLPAKNGlGHYKSPGMEERYPGIQFSQF-TG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 159 itAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDPLIISQDEGIRPQTTIDKLAQLRPaFKK 238
Cdd:PRK06504 159 --AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKL-IAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 239 DGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNE 318
Cdd:PRK06504 236 GGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080967136 319 AFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLSD-AKPTGVASLCIGGGQGIATVV 389
Cdd:PRK06504 316 AFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQrGKRYGLQTMCEGGGMANVTIV 387
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-389 |
6.10e-90 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 276.22 E-value: 6.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAG-QGQNPARIAAIHGGVPEAV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 80 PSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMllkNSRFGFKMGNQTLEDSMIADGltDKFNdyhmgi 159
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPL---GANAGPGRGLPRPDSWDIDMP--NQFE------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 160 TAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVP------QRKGDPLIISQDEGIRpQTTIDKLAQLR 233
Cdd:PRK07850 150 AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPvldeegQPTGETRLVTRDQGLR-DTTMEGLAGLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 234 PAFKkDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDI 313
Cdd:PRK07850 229 PVLE-GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080967136 314 FELNEAFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLSDA-KPTGVASLCIGGGQGIATVV 389
Cdd:PRK07850 308 VEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTdKSTALITMCAGGALSTGTII 384
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
6-389 |
1.59e-88 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 272.74 E-value: 1.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 6 LAEAY-----RTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAG-QGQNPARIAAIHGGVPEAV 79
Cdd:PRK07801 1 MAEAYivdavRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpQAGNIARTSWLAAGLPEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 80 PSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPM---LLKNSRFGFKmgNQTLEdsmiADGLTDKFNDYH 156
Cdd:PRK07801 81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPIssaMTAGEQLGFT--SPFAE----SKGWLHRYGDQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 157 MG--ITAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVpqrkgdpliISQDEGIRpQTTIDKLAQLRP 234
Cdd:PRK07801 155 VSqfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPR-ETSLEKMAGLKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 235 aFKKDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIF 314
Cdd:PRK07801 225 -LVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVV 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080967136 315 ELNEAFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQLS-DAKPTGVASLCIGGGQGIATVV 389
Cdd:PRK07801 304 EINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELErTGGRYGLQTMCEGGGTANVTII 379
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
3-389 |
2.00e-84 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 263.38 E-value: 2.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 3 RIVLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVPSF 82
Cdd:PRK08963 6 RIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 83 TVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKnsrfgfKMGNQTLEDSMIADGLTDKFN--------- 153
Cdd:PRK08963 86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVS------KKLARALVDLNKARTLGQRLKlfsrlrlrd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 154 ---------DY----HMGITAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGdplIISQDEGI 220
Cdd:PRK08963 160 llpvppavaEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ---PLEEDNNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 221 RPQTTIDKLAQLRPAF-KKDGSVTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAP-SIMGIGPVEAIH 298
Cdd:PRK08963 237 RGDSTLEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 299 KALKRSNKVINDVDIFELNEAFAAQSIA----------VNRELQLPQ-------DKVNVNGGAIALGHPIGASGARTLVS 361
Cdd:PRK08963 317 LALERAGLTLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLGRSQaigevdmSKFNVLGGSIAYGHPFAATGARMITQ 396
|
410 420
....*....|....*....|....*....
gi 1080967136 362 LLHQLSD-AKPTGVASLCIGGGQGIATVV 389
Cdd:PRK08963 397 TLHELRRrGGGLGLTTACAAGGLGAAMVL 425
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-389 |
2.15e-81 |
|
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: 254.73 E-value: 2.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 7 AEAYRTPIGVFGGV---FKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVPSFT 83
Cdd:cd00826 1 AGAAMTAFGKFGGEngaDANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 84 VNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSqspmllknsrfgfkmgnqtledsmiadgltdkfndyhmgITAEN 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME---------------------------------------TSAEN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 164 LVEQYQI--------SRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVEVPQRKGDPLIISqDEGIRPQT--TIDKLAQLR 233
Cdd:cd00826 122 NAKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDA-DEYIQFGDeaSLDEIAKLR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 234 PAFKKDGSVTAGNASGINDGAAAMLVMTEDKA-------KALGLQPIAVLDSFGASGVAPS----IMGIGPVEAIHKALK 302
Cdd:cd00826 201 PAFDKEDFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 303 RSNKVINDVDIFELNEAFAAQSIAVNRELQL-PQDK-----------------VNVNGGAIALGHPIGASGARTLVSLLH 364
Cdd:cd00826 281 KAGLGIGDLDLIEAHDAFAANACATNEALGLcPEGQggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCF 360
|
410 420 430
....*....|....*....|....*....|.
gi 1080967136 365 QL------SDAKPTGVASLCIGGGQGIATVV 389
Cdd:cd00826 361 ELkgeagkRQGAGAGLALLCIGGGGGAAMCI 391
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.51e-70 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 226.97 E-value: 2.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTP--IGVFG-GVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAG-QGQNPARIAAIHGGVP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPrgIGKVGkGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGkQGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 77 EAVPSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSpmllknSRFGFKMGNQTLEDSMIADG---LTDKFN 153
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYT------AAMAAEDMAAGKPPLGMGSGnlrLRALHP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 154 DYHMGITAENLVEQYQISRKEQDQFAFDSQQKASRAQQAGVFDAEIVPVevpQRKGDPLIISQDEGIRPQTTIDKLAQLR 233
Cdd:PRK06025 155 QSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV---YRDDGSVALDHEEFPRPQTTAEGLAALK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 234 PAFKK-------DGSVT-------------------AGNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVAPS 287
Cdd:PRK06025 232 PAFTAiadypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 288 IMGIGPVEAIHKALKRSNKVINDVDIFELNEAFAAQSIAVNRELQLPQDKVNVNGGAIALGHPIGASGARTLVSLLHQL- 366
Cdd:PRK06025 312 LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELe 391
|
410 420
....*....|....*....|....*.
gi 1080967136 367 -SDAKpTGVASLCIGGGQGIATVVSK 391
Cdd:PRK06025 392 rRGLK-RGLVTMCAAGGMAPAIIIER 416
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
270-391 |
1.02e-49 |
|
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: 163.58 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 270 LQPIAVLDSFGASGVAPSIMGIGPVEAIHKALKRSNKVINDVDIFELNEAFAAQSIAVNRELQLPQDKVNVNGGAIALGH 349
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1080967136 350 PIGASGARTLVSLLHQLS-DAKPTGVASLCIGGGQGIATVVSK 391
Cdd:pfam02803 81 PLGASGARILVTLLHELKrRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
47-391 |
4.78e-46 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 163.15 E-value: 4.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 47 EINEVILGNVLQAGQGQNPARIAAIHGGVPEAVPSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPM--- 123
Cdd:PRK09268 52 RLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIavn 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 124 ------LLKNSRfgfkmgNQTLEDSMIA--------------------DGLTdkfndyhMGITAENLVEQYQISRKEQDQ 177
Cdd:PRK09268 132 eglrkiLLELNR------AKTTGDRLKAlgklrpkhlapeiprngeprTGLS-------MGEHAAITAKEWGISREAQDE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 178 FAFDSQQKASRAQQAGVFDAEIVPVevpqrkgdpLIISQDEGIRPQTTIDKLAQLRPAFKK--DGSVTAGNASGINDGAA 255
Cdd:PRK09268 199 LAAASHQNLAAAYDRGFFDDLITPF---------LGLTRDNNLRPDSSLEKLAKLKPVFGKggRATMTAGNSTPLTDGAS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 256 AMLVMTEDKAKALGLQPIAVL-DSFGA-----SGVAPSIMgiGPVEAIHKALKRSNKVINDVDIFELNEAFAAQSIAV-- 327
Cdd:PRK09268 270 VVLLASEEWAAEHGLPVLAYLvDAETAavdfvHGKEGLLM--APAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATlk 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 328 --------NRELQLP-------QDKVNVNGGAIALGHPIGASGARTLVSLLHQLSDA-KPTGVASLCIGGGQGIATVVSK 391
Cdd:PRK09268 348 awedeeycRERLGLDaplgsidRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEKgSGRGLISICAAGGQGVTAILER 427
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
12-389 |
3.18e-21 |
|
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: 93.87 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 12 TPIGVFGGVfkdiPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPeAVPSFTVNKVCGSG 91
Cdd:cd00829 6 TPFGRRSDR----SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLL-GKPATRVEAAGASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 92 LKAIQLAYQSIVAGDNEIVIAGGMESMSQSPmllKNSRFGFKMGNQTLEDSMIADGLTdkFNDY-------HM---GITA 161
Cdd:cd00829 81 SAAVRAAAAAIASGLADVVLVVGAEKMSDVP---TGDEAGGRASDLEWEGPEPPGGLT--PPALyalaarrYMhryGTTR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 162 ENLveqYQISRKeqdqfAFDSQQKASRAQQAGVFDAEIV----PVevpqrkGDPLiisqdegirpqttidklaqlrpafk 237
Cdd:cd00829 156 EDL---AKVAVK-----NHRNAARNPYAQFRKPITVEDVlnsrMI------ADPL------------------------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 238 kdgsvTAGNASGINDGAAAMLVMTEDKAKALGLQPIAVLdsfgASGVAPSIMGIGPVEAIH----------KALKRSNKV 307
Cdd:cd00829 197 -----RLLDCCPVSDGAAAVVLASEERARELTDRPVWIL----GVGAASDTPSLSERDDFLsldaarlaarRAYKMAGIT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 308 INDVDIFELNEAFAAQSIAVNREL---------------------QLPqdkVNVNGGAIALGHPIGASGARTLVSLLHQL 366
Cdd:cd00829 268 PDDIDVAELYDCFTIAELLALEDLgfcekgeggklvregdtaiggDLP---VNTSGGLLSKGHPLGATGLAQAVEAVRQL 344
|
410 420
....*....|....*....|....*....
gi 1080967136 367 S-DAKPTGVASLCIG-----GGQGIATVV 389
Cdd:cd00829 345 RgEAGARQVPGARVGlahniGGTGSAAVV 373
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
26-389 |
4.56e-20 |
|
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: 88.66 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 26 AYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEaVPSFTVNKVCGSGLKAIQLAYQSIVAG 105
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISG-GPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 106 DNEIVIAGGMESmsqspmllknsrfgfkmgnqtledsmiadgltdkfndyhmgitaenlveqyqisrkeqdqfafdsqqk 185
Cdd:cd00327 86 KADIVLAGGSEE-------------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 186 asraqqagvfdaeivpvevpqrkgdpliisqdegirpqttidklaqlrpafkkdgsvtagnaSGINDGAAAMLVMTEDKA 265
Cdd:cd00327 98 --------------------------------------------------------------FVFGDGAAAAVVESEEHA 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 266 KALGLQPIAVLDSFGASGVAPS----IMGIGPVEAIHKALKRSNKVINDVDIFELNEAFAAQSIAVNRELQLPQDKV--- 338
Cdd:cd00327 116 LRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrsp 195
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080967136 339 NVNGGAIALGHPIGASGARTLVSLLHQL-------SDAKP-TGVASLCIGGGQGIATVV 389
Cdd:cd00327 196 AVSATLIMTGHPLGAAGLAILDELLLMLehefippTPREPrTVLLLGFGLGGTNAAVVL 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-373 |
4.00e-18 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 85.33 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 1 MSRIVLAEAYRTPIGVFGGV-FKDIpAYELGatviRQILEHSQIDPNEINEVILGNVLqAGQ--GQ-NPARIAAIHGGVP 76
Cdd:PRK06064 1 MRDVAIIGVGQTKFGELWDVsLRDL-AVEAG----LEALEDAGIDGKDIDAMYVGNMS-AGLfvSQeHIAALIADYAGLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 77 EaVPSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLKNSRFGfKMGNQTLEDSMiadGLTdkFNDYH 156
Cdd:PRK06064 75 P-IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIA-RAGDYEWEEFF---GAT--FPGLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 157 mGITAENLVEQYQISRKEQDQFAFDSQQKASR---AQqagvFdaeivpvevpQRKgdpliISQDEGIRPQTTIDKLAQLr 233
Cdd:PRK06064 148 -ALIARRYMHKYGTTEEDLALVAVKNHYNGSKnpyAQ----F----------QKE-----ITVEQVLNSPPVADPLKLL- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 234 pafkkdgsvtagNASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFGASGVA-----PSIMGIGP-VEAIHKALKRSNKV 307
Cdd:PRK06064 207 ------------DCSPITDGAAAVILASEEKAKEYTDTPVWIKASGQASDTIalhdrKDFTTLDAaVVAAEKAYKMAGIE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 308 INDVDIFELNEAFA-AQSIAVN--------------RELQLPQD---KVNVNGGAIALGHPIGASGARTLVSLLHQLSDA 369
Cdd:PRK06064 275 PKDIDVAEVHDCFTiAEILAYEdlgfakkgeggklaREGQTYIGgdiPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGE 354
|
....
gi 1080967136 370 KPTG 373
Cdd:PRK06064 355 AEKG 358
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
14-368 |
1.63e-12 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 68.33 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 14 IGVFG------GVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAVPsFTVNKV 87
Cdd:PRK12578 3 VAVIGvgnskfGRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVP-LRVEAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 88 CGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQ--SPMLLKnsrFGFKMGNQTLEDSMIadGLTdkFNDYHmGITAENLV 165
Cdd:PRK12578 82 CATGLAASLTAYTAVASGLVDMAIAVGVDKMTEvdTSTSLA---IGGRGGNYQWEYHFY--GTT--FPTYY-ALYATRHM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 166 EQYQISRKEQDQFAFDSQQKASRAQQAGvFDAEIVPVEVPQRKgdplIISQdegirPQTTIDklaqlrpafkkdgsvtag 245
Cdd:PRK12578 154 AVYGTTEEQMALVSVKAHKYGAMNPKAH-FQKPVTVEEVLKSR----AISW-----PIKLLD------------------ 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 246 nASGINDGAAAMLVMTEDKAKALGLQPIAVLDSFG----ASGVAPSIMGIG---PVEAIHKALKRSNKVINDVDIFELNE 318
Cdd:PRK12578 206 -SCPISDGSATAIFASEEKVKELKIDSPVWITGIGyandYAYVARRGEWVGfkaTQLAARQAYNMAKVTPNDIEVATVHD 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080967136 319 AFAAQSIAVNRELQLPQD----------------KVNVN--GGAIALGHPIGASGARTLVSLLHQLSD 368
Cdd:PRK12578 285 AFTIAEIMGYEDLGFTEKgkggkfieegqsekggKVGVNlfGGLKAKGHPLGATGLSMIYEITKQLRD 352
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
28-390 |
6.50e-10 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 60.47 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 28 ELGATVIRQILEHSQIDPNEINEVILGNV---LQAGQGQNPARIAAIHGGVpEAVPSFTVNKVCGSGLKAIQLAYQSIVA 104
Cdd:PRK06289 28 DLTREVVDGTLAAAGVDADDIEVVHVGNFfgeLFAGQGHLGAMPATVHPAL-WGVPASRHEAACASGSVATLAAMADLRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 105 GDNEIVIAGGMESMSQSPMLLKNSRFGFK-------MGNQTLEDSMIADgLTDKFnDYHMGITAENLVEQYQIsrkeqdq 177
Cdd:PRK06289 107 GRYDVALVVGVELMKTVPGDVAAEHLGAAawtghegQDARFPWPSMFAR-VADEY-DRRYGLDEEHLRAIAEI------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 178 fAFDSQQKASRAQQAGVFdaeivpveVPQRKGDPliisqDEGIRPQTtidklaqlrpafkkDGSVTAGNASGINDGAAAM 257
Cdd:PRK06289 178 -NFANARRNPNAQTRGWA--------FPDEATND-----DDATNPVV--------------EGRLRRQDCSQVTDGGAGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 258 LVMTEDKAKAL-GLQPIAVLDSFG-------------ASGVAPSIMgigP--VEAIHKALKRSNKVINDVDIFELNEAFA 321
Cdd:PRK06289 230 VLASDAYLRDYaDARPIPRIKGWGhrtaplgleqkldRSAGDPYVL---PhvRQAVLDAYRRAGVGLDDLDGFEVHDCFT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 322 AQSIAVNREL---------------------QLPqdkVNVNGGAIALGHPIGASGARTLVSLLHQLSDAK-------PTG 373
Cdd:PRK06289 307 PSEYLAIDHIgltgpgeswkaiengeiaiggRLP---INPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAgdyqvegAKT 383
|
410
....*....|....*..
gi 1080967136 374 VASLCIGGgqGIATVVS 390
Cdd:PRK06289 384 FGTLNIGG--STTTTVS 398
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
34-356 |
2.60e-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: 52.16 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 34 IRQILEHSQIDPNEINE----VILG----------NVLQAGQGQNPARI------AAIHGGVPEAV--------PSFTVN 85
Cdd:cd00834 79 AEEALADAGLDPEELDPerigVVIGsgigglatieEAYRALLEKGPRRVspffvpMALPNMAAGQVairlglrgPNYTVS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 86 KVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSQSPMLLknsrfGFkmgnqtleDSMIAdgltdkfndyhmgitaenlv 165
Cdd:cd00834 159 TACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLA-----GF--------AALRA-------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 166 eqyqISRKeqdqfaFDSQQKASRAqqagvFDAEivpvevpqRKGdpLIISqdEGirpqttidklaqlrpafkkdgsvtag 245
Cdd:cd00834 206 ----LSTR------NDDPEKASRP-----FDKD--------RDG--FVLG--EG-------------------------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 246 nasgindgaAAMLVMTE-DKAKALGLQPIAVLDSFGASG-----VAPSIMGIGPVEAIHKALKRSNKVINDVDIF----- 314
Cdd:cd00834 233 ---------AGVLVLESlEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDYInahgt 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1080967136 315 --ELNEafAAQSIAVNRELQLPQDKVNVNG--GAIalGHPIGASGA 356
Cdd:cd00834 304 stPLND--AAESKAIKRVFGEHAKKVPVSStkSMT--GHLLGAAGA 345
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
29-390 |
3.94e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 51.49 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 29 LGATVIRQILEHSQIDPNEINEVILGnVLQAG-QGQN-PARIAAihGGVPE--AVPSFTVNKVCGSGLKAIQLAYQSIVA 104
Cdd:PRK07516 25 LIVRVAREALAHAGIAAGDVDGIFLG-HFNAGfSPQDfPASLVL--QADPAlrFKPATRVENACATGSAAVYAALDAIEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 105 GDNEIVIAGGMESMSQSP------MLLKNSRFGfkmgnqtlEDSMIADGLTDKFndyhmGITAENLVEQYqisRKEQDQF 178
Cdd:PRK07516 102 GRARIVLVVGAEKMTATPtaevgdILLGASYLK--------EEGDTPGGFAGVF-----GRIAQAYFQRY---GDQSDAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 179 AfdsqQKASRAQQAGVfdaeivpvevpqrkGDPLiisqdegirpqttidklAQLRPAFKKD--GSVTAGN---------- 246
Cdd:PRK07516 166 A----MIAAKNHANGV--------------ANPY-----------------AQMRKDLGFEfcRTVSEKNplvagplrrt 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 247 -ASGINDGAAAMLVMTEDKAKALglqPIAVldSFGASGVAPSIMGI---------GPVEAIHKALKRSNKVINDVDIFEL 316
Cdd:PRK07516 211 dCSLVSDGAAALVLADAETARAL---QRAV--RFRARAHVNDFLPLsrrdplafeGPRRAWQRALAQAGVTLDDLSFVET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 317 NEAF------------------AAQSIA---VNRELQLPqdkVNVNGGAIALGHPIGASGartlVSlLH----------- 364
Cdd:PRK07516 286 HDCFtiaelieyeamglappgqGARAIRegwTAKDGKLP---VNPSGGLKAKGHPIGATG----VS-MHvlaamqltgea 357
|
410 420
....*....|....*....|....*....
gi 1080967136 365 ---QLSDAKPTGVASLcigGGQGIATVVS 390
Cdd:PRK07516 358 ggmQIPGAKLAGVFNM---GGAAVANYVS 383
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
4-124 |
1.29e-05 |
|
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: 46.78 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 4 IVLAEAYRTPIGVFGGVFkdipAYELGATVIRQileHSQIDPNEInevilgnvlqAGQGQN--PARIAA---IHGgvpea 78
Cdd:cd00833 104 YSPESLAGSRTGVFVGAS----SSDYLELLARD---PDEIDAYAA----------TGTSRAflANRISYffdLRG----- 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1080967136 79 vPSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGG---------MESMSQSPML 124
Cdd:cd00833 162 -PSLTVDTACSSSLVALHLACQSLRSGECDLALVGGvnlilspdmFVGFSKAGML 215
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
38-118 |
2.52e-05 |
|
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: 45.32 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 38 LEHSQIDPNEINEVILGNVLQAGQGQNPARIAAIHGGVPEAV------------------------PSFTVNKVCGSGLK 93
Cdd:pfam00109 99 LEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPRRGspfavgtmpsviagrisyflglrgPSVTVDTACSSSLV 178
|
90 100
....*....|....*....|....*
gi 1080967136 94 AIQLAYQSIVAGDNEIVIAGGMESM 118
Cdd:pfam00109 179 AIHAAVQSIRSGEADVALAGGVNLL 203
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-113 |
2.91e-05 |
|
"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: 45.50 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 5 VLAEAYRTPIGVFGGVFKDIPAYELGATVIRQILEHSQIDPNEINEVILGNVLQAGQGQNPA-RIAAIHGGVPeaVPSFT 83
Cdd:cd00827 27 VDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAAtYLAELLGLTN--AEAFD 104
|
90 100 110
....*....|....*....|....*....|..
gi 1080967136 84 VNKVCGSGLKAIQLAYQSIVAGDNE--IVIAG 113
Cdd:cd00827 105 LKQACYGGTAALQLAANLVESGPWRyaLVVAS 136
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
80-356 |
3.41e-05 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 45.47 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 80 PSFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGGMESMSqSPMLLKnsrfGFkmgnqtleDSMIAdgltdkfndyhmgi 159
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAI-TPLGLA----GF--------DALGA-------------- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 160 taenlveqyqISRKEqdqfafDSQQKASRAqqagvFDAEivpvevpqRKGdpLIISqdEGirpqttidklaqlrpafkkd 239
Cdd:COG0304 206 ----------LSTRN------DDPEKASRP-----FDKD--------RDG--FVLG--EG-------------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 240 gsvtagnasgindgaAAMLVM-TEDKAKALGLQPIAVLDSFGASG-----VAPSIMGIGPVEAIHKALKRSNKVINDVDI 313
Cdd:COG0304 233 ---------------AGVLVLeELEHAKARGAKIYAEVVGYGASSdayhiTAPAPDGEGAARAMRAALKDAGLSPEDIDY 297
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1080967136 314 F-------ELNEafAAQSIAVNRELQLPQDKVNVNggAI--ALGHPIGASGA 356
Cdd:COG0304 298 InahgtstPLGD--AAETKAIKRVFGDHAYKVPVS--STksMTGHLLGAAGA 345
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
248-366 |
8.96e-05 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 44.50 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 248 SGINDGAAAMLVMTEDKAKALGLQPI-AVLDSFGASGVAPSIMGIGPVE---------AIHKALKRSNKVINDVDIFELN 317
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEIKSLACASGNLYEDPPDatrmftsraAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080967136 318 EAFAAQSIAVNRELQLPQD------------------KVNVNGGAIALGHPIGASGARTLVSLLHQL 366
Cdd:PTZ00455 336 DCFTIAELLMYEALGIAEYghakdlirngatalegriPVNTGGGLLSFGHPVGATGVKQIMEVYRQM 402
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
252-366 |
2.82e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 42.73 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 252 DGAAAMLVMTEDKAKALGLQPIAVLDSFGAS-----GVAPSIMGIGPVEAIHKALKRSNKVINDVDIF-------ELNEA 319
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFGLTcdayhMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQ 289
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1080967136 320 FAAQSIAvnrelQLPQDKVNVNGGAIALGHPIGASGAR----TLVSLLHQL 366
Cdd:PRK05952 290 REANLIQ-----ALFPHRVAVSSTKGATGHTLGASGALgvafSLLALRHQQ 335
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
250-355 |
6.54e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 41.60 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 250 INDGAAAMLVMTEDKAKALGLQP--IAVLD------SFGASGVAPSimgigpvEAIHKALKRSNKV-INDVDIFELNEAF 320
Cdd:PRK07937 204 ITDGAAAVVLAAGDRARELRERPawITGIEhriespSLGARDLTRS-------PSTALAAEAATGGdAGGVDVAELHAPF 276
|
90 100 110
....*....|....*....|....*....|....*.
gi 1080967136 321 AAQSIAVNRELQLPQD-KVNVNGGAIAlGHPIGASG 355
Cdd:PRK07937 277 THQELILREALGLGDKtKVNPSGGALA-ANPMFAAG 311
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
11-114 |
1.12e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 41.40 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 11 RTPIGVFGGVFkdipAYELGATVIRqilehsqiDPNEINE-VILGN---VLqagqgqnPARIAAI---HGgvpeavPSFT 83
Cdd:COG3321 115 GSRTGVFVGAS----SNDYALLLLA--------DPEAIDAyALTGNaksVL-------AGRISYKldlRG------PSVT 169
|
90 100 110
....*....|....*....|....*....|.
gi 1080967136 84 VNKVCGSGLKAIQLAYQSIVAGDNEIVIAGG 114
Cdd:COG3321 170 VDTACSSSLVAVHLACQSLRSGECDLALAGG 200
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
233-369 |
1.26e-03 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 40.50 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 233 RPAFK-KDGSVTAGnasgindGAAAMLVMTEDKAKALGLQPIAVL-------DSFGASGVAPsimGIGPVEAIHKALKRS 304
Cdd:cd00828 218 RPFDEtRDGFVEAE-------GAGVLVLERAELALARGAPIYGRVagtasttDGAGRSVPAG---GKGIARAIRTALAKA 287
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080967136 305 NKVINDVDIFEL----------NEAFAAQSIAVNRELQLPQDKVNVNggaiaLGHPIGASG----ARTLVSLLHQLSDA 369
Cdd:cd00828 288 GLSLDDLDVISAhgtstpandvAESRAIAEVAGALGAPLPVTAQKAL-----FGHSKGAAGalqlIGALQSLEHGLIPP 361
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
252-356 |
3.93e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 39.00 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 252 DGAAAMLVMTEDKAKALGLQPIAVLDSFGASG-----VAPSIMGIGPVEAIHKALKRSNKVINDVDIF-------ELNEA 319
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDYInahgtstPAGDK 311
|
90 100 110
....*....|....*....|....*....|....*..
gi 1080967136 320 FAAQsiAVNRELQLPQDKVNVNGGAIALGHPIGASGA 356
Cdd:PRK07314 312 AETQ--AIKRVFGEHAYKVAVSSTKSMTGHLLGAAGA 346
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
252-372 |
4.58e-03 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 38.91 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080967136 252 DGAAAMLVMTEDKAKALGLQPIAVLDSFGASG-----VAPSIMGIGPVEAIHKALKRSNKV-INDVDIF-------ELNE 318
Cdd:PTZ00050 239 EGAGILVLEELEHALRRGAKIYAEIRGYGSSSdahhiTAPHPDGRGARRCMENALKDGANInINDVDYVnahatstPIGD 318
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080967136 319 AFAAQSIA-VNRELQLPQDKVNVNGGAIalGHPIGASGA----RTLVSLLHQLsdAKPT 372
Cdd:PTZ00050 319 KIELKAIKkVFGDSGAPKLYVSSTKGGL--GHLLGAAGAvesiVTILSLYEQI--IPPT 373
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
81-114 |
8.80e-03 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 37.69 E-value: 8.80e-03
10 20 30
....*....|....*....|....*....|....
gi 1080967136 81 SFTVNKVCGSGLKAIQLAYQSIVAGDNEIVIAGG 114
Cdd:smart00825 90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
|
|
| |
