|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
3-394 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 637.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 3 QREVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTP 82
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 83 ALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGHAQMVDSVIHDGLWDAFNDYHMGIT 162
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 163 AENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALRVERDEQPR-DTSLEALTRLRPAFRKEG 241
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRpDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 242 TVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAF 321
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1217747202 322 AAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVERP 394
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
4-394 |
0e+00 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 586.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPA 83
Cdd:PRK05656 2 QDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 84 LTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGHAQMVDSVIHDGLWDAFNDYHMGITA 163
Cdd:PRK05656 82 MTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 164 ENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALRVERDEQPR-DTSLEALTRLRPAFRKEGT 242
Cdd:PRK05656 162 ENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRaGTTAESLAKLKPAFKKDGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 243 VTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFA 322
Cdd:PRK05656 242 VTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1217747202 323 AQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVERP 394
Cdd:PRK05656 322 AQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIERD 393
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
4-394 |
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: 582.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPA 83
Cdd:COG0183 2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 84 LTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLgHAQMVDSVIHDGLWDAFNDYHMGITA 163
Cdd:COG0183 82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGETA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 164 ENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALrVERDEQPR-DTSLEALTRLRPAFRKEGT 242
Cdd:COG0183 161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVV-VDRDEGPRpDTTLEKLAKLKPAFKKDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 243 VTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFA 322
Cdd:COG0183 240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1217747202 323 AQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVERP 394
Cdd:COG0183 320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
7-393 |
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: 557.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 7 VIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPALTI 86
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 87 NKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGHaQMVDSVIHDGLWDAFNDYHMGITAENL 166
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGL-NTLDGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 167 AEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALrVERDEQPR-DTSLEALTRLRPAFRKEGTVTA 245
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVV-VDRDEGPRpDTTLEKLAKLKPAFKKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 246 GNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFAAQA 325
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1217747202 326 LAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
8-392 |
3.14e-168 |
|
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: 475.56 E-value: 3.14e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 8 IVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPALTIN 87
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 88 KVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLM-AGARAGLRLGHAQMVDSVIHDgLWDAFNDYHMGITAENL 166
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVpRSLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 167 AEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGeALRVERDEQPR-DTSLEALTRLRPAFRKEGTVTA 245
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKG-PVTVSSDEGIRpNTTLEKLAKLKPAFDPDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 246 GNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFAAQA 325
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1217747202 326 LAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVE 392
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
4-392 |
2.85e-156 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 445.70 E-value: 2.85e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPA 83
Cdd:PRK08235 2 SKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 84 LTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGHAQMVDSVIHDGLWDAFNDYHMGITA 163
Cdd:PRK08235 82 ETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVYG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 164 ENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALRVERDEQPR-DTSLEALTRLRPAFRKEGT 242
Cdd:PRK08235 162 GEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRkDTTIEKLAKLKPVFDKTGT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 243 VTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFA 322
Cdd:PRK08235 242 ITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 323 AQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVE 392
Cdd:PRK08235 322 AVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
3-393 |
2.51e-150 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 430.54 E-value: 2.51e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 3 QREVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVL-TAGCGQNPARQTALNAGLPVTT 81
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpTEPRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGHAQMVDSVIhDGLWDAFNDYHMGI 161
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMV-GALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 162 TAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALrVERDEQPR-DTSLEALTRLRPAFRKE 240
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVV-FDTDEHVRaDTTLEDLAKLKPVFKKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 241 -GTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANE 319
Cdd:PRK09051 240 nGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1217747202 320 AFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
4-393 |
3.25e-149 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 427.97 E-value: 3.25e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPA 83
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 84 LTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGHAQMVDSVIHDGLWDAFNDYHMGITA 163
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 164 ENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKG-EALRVERDEQPRDTSLEALTRLRPAFRKE-G 241
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGrPSVIVDKDEGLGKFDPAKLRKLRPSFKEDgG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 242 TVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAF 321
Cdd:PLN02644 241 SVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1217747202 322 AAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:PLN02644 321 SVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
4-392 |
8.77e-144 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 414.04 E-value: 8.77e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPA 83
Cdd:PRK06633 3 KPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 84 LTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSpylMAGA--RAGLRLGHAQMVDSVIHDGLWDAFNDYHMGI 161
Cdd:PRK06633 83 YTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLG---MHGSyiRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 162 TAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALrVERDEQPR-DTSLEALTRLRPAFRKE 240
Cdd:PRK06633 160 TAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSL-FDHDETVRpDTSLEILSKLRPAFDKN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 241 GTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEA 320
Cdd:PRK06633 239 GVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1217747202 321 FAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVE 392
Cdd:PRK06633 319 FAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
4-393 |
3.27e-138 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 400.13 E-value: 3.27e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQvlTAGCGQNPA--RQTALNAGLPVTT 81
Cdd:PRK06205 2 RDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGHAQMvdsviHDGLWDA---FNDYH 158
Cdd:PRK06205 80 PGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQL-----HDRLARGretAGGRR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 159 MGI------TAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALRVERDEQPR-DTSLEALT 231
Cdd:PRK06205 155 FPVpggmieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRaDTTLESLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 232 RLRPAFRK---EGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWR 308
Cdd:PRK06205 235 KLRPIMGKqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 309 LEEVDLIEANEAFAAQALAVGKELGWEA---ERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQ 385
Cdd:PRK06205 315 LDDIDLIELNEAFAAQVLAVLKEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQ 394
|
....*...
gi 1217747202 386 GVALAVER 393
Cdd:PRK06205 395 GLAAVFER 402
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
4-393 |
3.58e-136 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 394.71 E-value: 3.58e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLA-QSGVAPQQIDEVILGQVLTAG-CGQNPARQTALNAGLPVTT 81
Cdd:PRK09050 2 TEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMArNPGVDWEAVDDVIYGCANQAGeDNRNVARMSALLAGLPVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLgHAQMVDSVIHdglWDAFNDY---- 157
Cdd:PRK09050 82 PGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSR-QAEIFDTTIG---WRFVNPLmkaq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 158 ----HMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALRVERDEQPR-DTSLEALTR 232
Cdd:PRK09050 158 ygvdSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRpETTLEALAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 233 LRPAFRKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEV 312
Cdd:PRK09050 238 LKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 313 DLIEANEAFAAQALAVGKELGW--EAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALA 390
Cdd:PRK09050 318 DVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALA 397
|
...
gi 1217747202 391 VER 393
Cdd:PRK09050 398 IER 400
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
4-393 |
1.60e-124 |
|
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: 365.26 E-value: 1.60e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLA-QSGVAPQQIDEVILGQVLTAG-CGQNPARQTALNAGLPVTT 81
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLArNPQLDWAAIDDVIYGCANQAGeDNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGhAQMVDSVI-----HDGLWDAFND 156
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRS-AKIEDTTIgwrfiNPLMKALYGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 157 YHMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALRVERDEQPR-DTSLEALTRLRP 235
Cdd:TIGR02430 160 DSMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRpETTLEGLAKLKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 236 AFRKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLI 315
Cdd:TIGR02430 240 VVRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 316 EANEAFAAQALAVGKELGW--EAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:TIGR02430 320 ELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.12e-122 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 360.36 E-value: 1.12e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 1 MQQREVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVT 80
Cdd:PRK06954 4 VDQDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 81 TPALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGHAQMVDSVIHDGLWDAFNDYH-M 159
Cdd:PRK06954 84 VGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 160 GITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALrVERDEQPRDTSLEALTRLRPAFRK 239
Cdd:PRK06954 164 GTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTV-IDRDEQPFKANPEKIPTLKPAFSK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 240 EGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANE 319
Cdd:PRK06954 243 TGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINE 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1217747202 320 AFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVE 392
Cdd:PRK06954 323 AFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
6-264 |
3.77e-111 |
|
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: 325.80 E-value: 3.77e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 6 VVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPALT 85
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 86 INKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMA-GARAGLRLGHAQMVDSVIHDGLWDAFNDYHMGITAE 164
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 165 NLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEaLRVERDEQPR-DTSLEALTRLRPAFRKEGTV 243
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGK-PTVDKDEGIRpPTTAEPLAKLKPAFDKEGTV 239
|
250 260
....*....|....*....|.
gi 1217747202 244 TAGNASSLNDGAAVVLLMSAE 264
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
4-394 |
7.30e-111 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 330.00 E-value: 7.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVG-SFHGALAPLTAVELGTAAVQGLLAQS-GVAPQQIDEVILGQVL-TAGCGQNPARQTALNAGLPVT 80
Cdd:PRK08947 2 EDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQqTLEQGFNIARNAALLAGIPHS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 81 TPALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMsrspylmagaraglrlGHAQMVDSV-IHDGL--WDAFNDY 157
Cdd:PRK08947 82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM----------------GHVPMNHGVdFHPGLskNVAKAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 158 HMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALRVERDEQPR-DTSLEALTRLRPA 236
Cdd:PRK08947 146 MMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRpETTVEALAALRPA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 237 FR-KEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLI 315
Cdd:PRK08947 226 FDpVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 316 EANEAFAAQALAVGKELGWE---AERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVE 392
Cdd:PRK08947 306 ELNEAFAAQSLPCLKDLGLLdkmDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
..
gi 1217747202 393 RP 394
Cdd:PRK08947 386 RV 387
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
4-388 |
2.61e-106 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 318.62 E-value: 2.61e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVG-SFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVL-TAGCGQNPARQTALNAGLPVTT 81
Cdd:PRK07661 2 REAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGHAQmvdsvihdglwdafNDYHMGI 161
Cdd:PRK07661 82 PAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVRPNPRLVEAA--------------PEYYMGM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 162 --TAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQ--------PKGEALRVERDEQPR-DTSLEAL 230
Cdd:PRK07661 148 ghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLrtvgennkLQEETITFSQDEGVRaDTTLEIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 231 TRLRPAFRKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLE 310
Cdd:PRK07661 228 GKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELS 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1217747202 311 EVDLIEANEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVA 388
Cdd:PRK07661 308 DIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAA 385
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
5-393 |
5.97e-106 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 318.10 E-value: 5.97e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 5 EVVIVAATRTPVG-SFHGALAPLTAVELGTAAVQGLLAQ-SGVAPQQIDEVILGQVLTAGC-GQNPARQTALNAGLPvTT 81
Cdd:PRK07851 3 EAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKvPALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYD-FL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSP--------------YLMAGARAGLRlghAQMVDSVIH 147
Cdd:PRK07851 82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAkgnsdslpdtknplFAEAQARTAAR---AEGGAEAWH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 148 D-----GLWDAFndYHMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPqpkgEALRVERDEQP 222
Cdd:PRK07851 159 DpredgLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP----DGTVVSTDDGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 223 R-DTSLEALTRLRPAFRKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRC 301
Cdd:PRK07851 233 RaGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 302 LEKAGWRLEEVDLIEANEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCI 381
Cdd:PRK07851 313 LARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCV 392
|
410
....*....|..
gi 1217747202 382 GGGQGVALAVER 393
Cdd:PRK07851 393 GGGQGMAMVLER 404
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
4-394 |
7.35e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 314.74 E-value: 7.35e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSF------HGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLtaGCGQN---PARQTALN 74
Cdd:PRK06445 2 EDVYLVDFARTAFSRFrpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENwlyGGRHPIFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 75 AGLPVTTPALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPylmAGARAGLRLGHAQMVDS-VIHdglWDA 153
Cdd:PRK06445 80 ARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP---MGDNPHIEPNPKLLTDPkYIE---YDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 154 FNDYHMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVpQPKGEALRVERDEQPR-DTSLEALTR 232
Cdd:PRK06445 154 TTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-EVEGKKKVVDVDQSVRpDTSLEKLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 233 LRPAFRKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEV 312
Cdd:PRK06445 233 LPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 313 DLIEANEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVE 392
Cdd:PRK06445 313 DLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLE 392
|
..
gi 1217747202 393 RP 394
Cdd:PRK06445 393 RV 394
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
4-392 |
2.44e-103 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 310.79 E-value: 2.44e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPA 83
Cdd:PRK06366 2 KDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 84 LTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAgarAGLRLGHAQMV-------DSVIHDGLWDAFND 156
Cdd:PRK06366 82 YTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLP---SDLRWGPKHLLhknykidDAMLVDGLIDAFYF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 157 YHMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTvpqpkgealRVERDEQPRDTSLEALTRLRPA 236
Cdd:PRK06366 159 EHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------DLDRDEGIRKTTMEDLAKLPPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 237 FRKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIE 316
Cdd:PRK06366 230 FDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1217747202 317 ANEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVE 392
Cdd:PRK06366 310 HNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-393 |
4.06e-103 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 310.40 E-value: 4.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 1 MQQREVVIVAATRTPVGSFH-GALAPLTAVELGTAAVQGLLAQ-SGVAPQQIDEVILGQVL-TAGCGQNPARQTALNAGL 77
Cdd:PRK09052 3 KQLQDAYIVAATRTPVGKAPrGMFKNTRPDDLLAHVLRSAVAQvPGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 78 PVTTPALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYlmagaraglrLGHAQMVDSVIHDGLWDAFNDY 157
Cdd:PRK09052 83 PNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM----------MGNKPSMSPAIFARDENVGIAY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 158 HMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTV----PQPKGEALR-----VERDEQPR-DTSL 227
Cdd:PRK09052 153 GMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEIterfPDLATGEVDvktrtVDLDEGPRaDTSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 228 EALTRLRPAFRKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGW 307
Cdd:PRK09052 233 EGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 308 RLEEVDLIEANEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGV 387
Cdd:PRK09052 313 KQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGA 392
|
....*.
gi 1217747202 388 ALAVER 393
Cdd:PRK09052 393 AGIFER 398
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
8-393 |
1.09e-99 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 301.70 E-value: 1.09e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 8 IVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAG-CGQNPARQTALNAGLPVTTPALTI 86
Cdd:PRK08131 6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGeDSRNVARNALLLAGLPVTVPGQTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 87 NKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLgHAQMVDSVI-----HDGLWDAFNDYHMGI 161
Cdd:PRK08131 86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSR-DAKVFDTTIgarfpNPKIVAQYGNDSMPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 162 TAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQ-PKGEALRVERDEQPR-DTSLEALTRLRPAFrK 239
Cdd:PRK08131 165 TGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgRKLPPKLVAEDEHPRpSSTVEALTKLKPLF-E 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 240 EGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANE 319
Cdd:PRK08131 244 GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINE 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1217747202 320 AFAAQALAVGKELG--WEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:PRK08131 324 AFASQVLGCLKGLGvdFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIER 399
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
4-393 |
3.06e-97 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 297.45 E-value: 3.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPV-GSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQ-NPARQTALNAGLPVTT 81
Cdd:PLN02287 46 DDVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGLRLGHAQMVDSVIHdglwdafndyhMGI 161
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP-----------MGI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 162 TAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVT--VPQPKGEALR---VERDEQPR-DTSLEALTRLRP 235
Cdd:PLN02287 195 TSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHtkIVDPKTGEEKpivISVDDGIRpNTTLADLAKLKP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 236 AFRKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLI 315
Cdd:PLN02287 275 VFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 316 EANEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRR--EVNKGLAMLCIGGGQGVALAVER 393
Cdd:PLN02287 355 EINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRgkDCRFGVVSMCIGTGMGAAAVFER 434
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
5-394 |
5.83e-95 |
|
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: 289.15 E-value: 5.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 5 EVVIVAATRTPVG-SFHGALAPLTAVELGTAAVQGLLAQ-SGVAPQQIDEVILGQV-LTAGCGQNPARQTALNAGLPVTT 81
Cdd:TIGR02445 1 DVVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVqQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMsrspylmagaraglrlGHAQM---VDSVIHDGLWDAFNDYH 158
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHM----------------GHVPMmhgVDFHPGMSLHVAKAAGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 159 MGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALRVERDEQPR-DTSLEALTRLRPAF 237
Cdd:TIGR02445 145 MGLTAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRpETTVESLAALRPAF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 238 R-KEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIE 316
Cdd:TIGR02445 225 DpKNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 317 ANEAFAAQALAVGKELGW---EAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:TIGR02445 305 LNEAFAAQALPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
.
gi 1217747202 394 P 394
Cdd:TIGR02445 385 V 385
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
4-393 |
9.57e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 287.30 E-value: 9.57e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPA 83
Cdd:PRK08170 3 RPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 84 LTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYL-----------MAGAR---------AGLRLGHAQMVD 143
Cdd:PRK08170 83 WTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLfsekmvrwlagWYAAKsigqklaalGKLRPSYLAPVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 144 SVIHdGLWDAFNDYHMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAqEITPVTVPQPKgeaLRVERDEQPR 223
Cdd:PRK08170 163 GLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDRDGK---FYDHDDGVRP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 224 DTSLEALTRLRPAF-RKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCL 302
Cdd:PRK08170 238 DSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 303 EKAGWRLEEVDLIEANEAFAAQALA----------VGKELGWEA-------ERVNVNGGAIALGHPIGASGCRILVSLLY 365
Cdd:PRK08170 318 QRHGLTLEDLDLWEINEAFAAQVLAclaawadeeyCREQLGLDGalgeldrERLNVDGGAIALGHPVGASGARIVLHLLH 397
|
410 420
....*....|....*....|....*...
gi 1217747202 366 EMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:PRK08170 398 ALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
5-393 |
3.65e-92 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 282.54 E-value: 3.65e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 5 EVVIVAATRTPVGSFH--GALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAG-CGQNPARQTALNAGLPVTT 81
Cdd:PRK08242 3 EAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGAraglrlghAQMVDSVIhdglwdAFNDYHM-- 159
Cdd:PRK08242 83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGG--------AWAMDPST------NFPTYFVpq 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 160 GITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTvpQPKGEALrVERDEQPR-DTSLEALTRLRPAFR 238
Cdd:PRK08242 149 GISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK--DQNGLTI-LDHDEHMRpGTTMESLAKLKPSFA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 239 KEGTV---------------------TAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPA 297
Cdd:PRK08242 226 MMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 298 ARRCLEKAGWRLEEVDLIEANEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLA 377
Cdd:PRK08242 306 TRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALI 385
|
410
....*....|....*.
gi 1217747202 378 MLCIGGGQGVALAVER 393
Cdd:PRK08242 386 TLCVGGGMGIATIIER 401
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
5-393 |
3.71e-92 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 282.00 E-value: 3.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 5 EVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAG-CGQNPARQTALNAGLPVTTPA 83
Cdd:PRK07850 3 NPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHVGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 84 LTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYlmaGARAGLRLGHAQMVDSVIhdglwDAFNDYHmgiTA 163
Cdd:PRK07850 83 TTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPL---GANAGPGRGLPRPDSWDI-----DMPNQFE---AA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 164 ENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVP------QPKGEALRVERDEQPRDTSLEALTRLRPAf 237
Cdd:PRK07850 152 ERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPvldeegQPTGETRLVTRDQGLRDTTMEGLAGLKPV- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 238 RKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEA 317
Cdd:PRK07850 231 LEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEI 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1217747202 318 NEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:PRK07850 311 NEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
4-393 |
2.30e-89 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 274.66 E-value: 2.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGcGQ--NPARQTALNAGLPVTT 81
Cdd:PRK07801 2 AEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQagNIARTSWLAAGLPEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPylMAGAR-AGLRLGhaqMVDSVIHDGLWDA-FNDYHM 159
Cdd:PRK07801 81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMtAGEQLG---FTSPFAESKGWLHrYGDQEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 160 G--ITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTvpqpkgealRVERDEQPRDTSLEALTRLRPaF 237
Cdd:PRK07801 156 SqfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG---------GVTVDEGPRETSLEKMAGLKP-L 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 238 RKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEA 317
Cdd:PRK07801 226 VEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEI 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1217747202 318 NEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:PRK07801 306 NEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
2-393 |
3.82e-84 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 263.00 E-value: 3.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 2 QQREVVIVAATRTPVG----SFHGalapLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGL 77
Cdd:PRK08963 3 QGDRIAIVSGLRTPFAkqatAFHG----IPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 78 PVTTPALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAG--ARAGLRLGHA----QMVDSVIHDGLW 151
Cdd:PRK08963 79 NVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKklARALVDLNKArtlgQRLKLFSRLRLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 152 D------AFNDY----HMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPqPKGEALrvERDEQ 221
Cdd:PRK08963 159 DllpvppAVAEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVP-PYKQPL--EEDNN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 222 PR-DTSLEALTRLRPAF-RKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDP-AIMGIGPAPAA 298
Cdd:PRK08963 236 IRgDSTLEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 299 RRCLEKAGWRLEEVDLIEANEAFAAQALA----------VGKELGWEA-------ERVNVNGGAIALGHPIGASGCRILV 361
Cdd:PRK08963 316 PLALERAGLTLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLGRSQaigevdmSKFNVLGGSIAYGHPFAATGARMIT 395
|
410 420 430
....*....|....*....|....*....|..
gi 1217747202 362 SLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:PRK08963 396 QTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
5-393 |
1.47e-81 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 255.04 E-value: 1.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 5 EVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAG-CGQNPARQTALNAGLPVTTPA 83
Cdd:PRK06504 3 EAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESVPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 84 LTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAG---ARAGLRLGHAQMVDSVIHDGLWDAFndyhMG 160
Cdd:PRK06504 83 TSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPStlpAKNGLGHYKSPGMEERYPGIQFSQF----TG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 161 itAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEALRVERDEQPR-DTSLEALTRLRPaFRK 239
Cdd:PRK06504 159 --AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRfDATLEGIAGVKL-IAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 240 EGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANE 319
Cdd:PRK06504 236 GGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1217747202 320 AFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:PRK06504 316 AFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
5-392 |
1.61e-81 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 253.92 E-value: 1.61e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 5 EVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLlaqSGVAPQQIDEVILGQVLtaGCGQNPARQTALNAGLPVTTPAL 84
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL---SKGMEREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 85 TINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYlmaGARAGLRLghaqmvdsvihdglwDAFNDYHMGITAE 164
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF---QNRARFSP---------------ETIGDPDMGVAAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 165 NLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTvpQPKGEALRVERDEQPrdtsleALTRLRPAFRKEGTVT 244
Cdd:PRK06690 139 YVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN--GLLDESIKKEMNYER------IIKRTKPAFLHNGTVT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 245 AGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFAAQ 324
Cdd:PRK06690 211 AGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASK 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1217747202 325 ALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVE 392
Cdd:PRK06690 291 VVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
5-388 |
2.37e-81 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 254.69 E-value: 2.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 5 EVVIVAATRTPVG-SFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGC-GQNPARQTALNAGLPVTTP 82
Cdd:PRK07108 3 EAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVTVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 83 ALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSrspylmagaraglrLGHAQMVDSVIHDGlWDAFND----YH 158
Cdd:PRK07108 83 GMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIS--------------CVQNEMNRHMLREG-WLVEHKpeiyWS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 159 MGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVP---------QPKGEALRVERDEQPR-DTSLE 228
Cdd:PRK07108 148 MLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTagvadkatgRLFTKEVTVSADEGIRpDTTLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 229 ALTRLRPAFrKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWR 308
Cdd:PRK07108 228 GVSKIRSAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 309 LEEVDLIEANEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVA 388
Cdd:PRK07108 307 VDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
9-392 |
6.38e-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: 253.57 E-value: 6.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 9 VAATRTPVGSF---HGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPALT 85
Cdd:cd00826 1 AGAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 86 INKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSpylmagARAGLRLGHaqmvdsvihdgLWDAFNDYHMgitaen 165
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETS------AENNAKEKH-----------IDVLINKYGM------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 166 laekyaisREEQDRFALRSQQKAQAAQQAGRFAQEITPVTVPQPKGEaLRVERDEQPR---DTSLEALTRLRPAFRKEGT 242
Cdd:cd00826 138 --------RACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGD-IHSDADEYIQfgdEASLDEIAKLRPAFDKEDF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 243 VTAGNASSLNDGAAVVLLMSAEKAAALRLPV-------LARIAGYASSGVDPA----IMGIGPAPAARRCLEKAGWRLEE 311
Cdd:cd00826 209 LTAGNACGLNDGAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 312 VDLIEANEAFAAQALAVGKELGWEAER------------------VNVNGGAIALGHPIGASGCRILVSLLYEMQRREVN 373
Cdd:cd00826 289 LDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGK 368
|
410 420
....*....|....*....|....
gi 1217747202 374 -----KGLAMLCIGGGQGVALAVE 392
Cdd:cd00826 369 rqgagAGLALLCIGGGGGAAMCIE 392
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
5-393 |
6.92e-63 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 207.32 E-value: 6.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 5 EVVIVAATRTPVG---SFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGC-GQNPARQTALNAGLPVT 80
Cdd:PRK06025 3 EAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYDIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 81 TPALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMS-------------RSPYLMAGARAGLRLGHAQMvdsvih 147
Cdd:PRK06025 83 ASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaamaaedmaagKPPLGMGSGNLRLRALHPQS------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 148 dglwdafndyHMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVTvpQPKGeALRVERDEQPR-DTS 226
Cdd:PRK06025 157 ----------HQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY--RDDG-SVALDHEEFPRpQTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 227 LEALTRLRPAFRK-------EGTVT-------------------AGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGY 280
Cdd:PRK06025 224 AEGLAALKPAFTAiadypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAM 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 281 ASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASGCRIL 360
Cdd:PRK06025 304 ANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILI 383
|
410 420 430
....*....|....*....|....*....|...
gi 1217747202 361 VSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:PRK06025 384 GTVLDELERRGLKRGLVTMCAAGGMAPAIIIER 416
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
271-393 |
1.66e-62 |
|
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: 196.71 E-value: 1.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 271 LPVLARIAGYASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFAAQALAVGKELGWEAERVNVNGGAIALGH 350
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1217747202 351 PIGASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
2-393 |
2.99e-59 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 198.20 E-value: 2.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 2 QQREVVIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTT 81
Cdd:PRK09268 5 TVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSP---------YLMAGARA-----------GLRLGH--- 138
Cdd:PRK09268 85 PAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPiavneglrkILLELNRAkttgdrlkalgKLRPKHlap 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 139 AQMVDSVIHDGLwdafndyHMGITAENLAEKYAISREEQDRFALRSQQKAQAAQQAGRFAQEITPVtvpqpkgeaLRVER 218
Cdd:PRK09268 165 EIPRNGEPRTGL-------SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF---------LGLTR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 219 DEQPR-DTSLEALTRLRPAFRK--EGTVTAGNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDpAIMG---- 291
Cdd:PRK09268 229 DNNLRpDSSLEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVD-FVHGkegl 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 292 -IGPAPAARRCLEKAGWRLEEVDLIEANEAFAAQALAVGK----------ELGWEA-------ERVNVNGGAIALGHPIG 353
Cdd:PRK09268 308 lMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKawedeeycreRLGLDAplgsidrSKLNVNGSSLAAGHPFA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1217747202 354 ASGCRILVSLLYEMQRREVNKGLAMLCIGGGQGVALAVER 393
Cdd:PRK09268 388 ATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
27-391 |
1.24e-24 |
|
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: 101.37 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 27 TAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPvTTPALTINKVCGSGLKAVHLAVQAIRS 106
Cdd:cd00327 6 TASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 107 GDADAVIAGGqesmsrspylmagaraglrlghaqmvdsvihdglwdafndyhmgitaenlaekyaisreeqdrfalrsqq 186
Cdd:cd00327 85 GKADIVLAGG---------------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 187 kaqaaqqagrfaqeitpvtvpqpkgealrverdeqprdtslealtrlrpafrkegtvtaGNASSLNDGAAVVLLMSAEKA 266
Cdd:cd00327 95 -----------------------------------------------------------SEEFVFGDGAAAAVVESEEHA 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 267 AALRLPVLARIAGYASSGVD----PAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFAAQALAVGKELGWEAERV--- 339
Cdd:cd00327 116 LRRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrsp 195
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1217747202 340 NVNGGAIALGHPIGASGCRILVSLLYEMQRREV-------NKGLAMLCIGGGQGVALAV 391
Cdd:cd00327 196 AVSATLIMTGHPLGAAGLAILDELLLMLEHEFIpptprepRTVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
20-391 |
3.31e-20 |
|
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: 91.17 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 20 HGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTtPALTINKVCGSGLKAVHL 99
Cdd:cd00829 8 FGRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGK-PATRVEAAGASGSAAVRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 100 AVQAIRSGDADAVIAGGQESMSRSPYlmaGARAGLRLGHAQMVDSVIHDGLwdAFNDYHmGITAENLAEKYAISREEQDR 179
Cdd:cd00829 87 AAAAIASGLADVVLVVGAEKMSDVPT---GDEAGGRASDLEWEGPEPPGGL--TPPALY-ALAARRYMHRYGTTREDLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 180 FALRSqqkaqaaqqagrfaqeitpvtvpqpKGEALR----VERDEQPRDTSLEA------LTRLrpafrkegtvtagNAS 249
Cdd:cd00829 161 VAVKN-------------------------HRNAARnpyaQFRKPITVEDVLNSrmiadpLRLL-------------DCC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 250 SLNDGAAVVLLMSAEKAAALRLPvLARIAG-------YASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFA 322
Cdd:cd00829 203 PVSDGAAAVVLASEERARELTDR-PVWILGvgaasdtPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 323 AQALA-------VGKELGWEAER-----------VNVNGGAIALGHPIGASGcrilVSLLYEMQR--------REV-NKG 375
Cdd:cd00829 282 IAELLaledlgfCEKGEGGKLVRegdtaiggdlpVNTSGGLLSKGHPLGATG----LAQAVEAVRqlrgeagaRQVpGAR 357
|
410
....*....|....*.
gi 1217747202 376 LAMLCIGGGQGVALAV 391
Cdd:cd00829 358 VGLAHNIGGTGSAAVV 373
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
4-386 |
6.02e-13 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 69.54 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVELGTAAvqglLAQSGVAPQQIDEVILGQVLTAG-CGQ-NPARQTALNAGLPvTT 81
Cdd:PRK06064 2 RDVAIIGVGQTKFGELWDVSLRDLAVEAGLEA----LEDAGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYAGLA-PI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPY---LMAGARAGlrlghaqmvdsvihDGLWDAFndyh 158
Cdd:PRK06064 77 PATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTpdaTEAIARAG--------------DYEWEEF---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 159 MGITAENLA--------EKYAISREEQDRFALRSQQKAqaaqqagrfaqeitpvtVPQPKGEalrverdeqprdtsleal 230
Cdd:PRK06064 139 FGATFPGLYaliarrymHKYGTTEEDLALVAVKNHYNG-----------------SKNPYAQ------------------ 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 231 trlrpaFRKEGTV-------------TAGNASSLNDGAAVVLLMSAEKAAALRL-PVLARIAGYASSGVD----PAIMGI 292
Cdd:PRK06064 184 ------FQKEITVeqvlnsppvadplKLLDCSPITDGAAAVILASEEKAKEYTDtPVWIKASGQASDTIAlhdrKDFTTL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 293 GPAP-AARRCLEKAGWRLEEVDLIEANEAFA-AQALA------VGKELGWEAER-----------VNVNGGAIALGHPIG 353
Cdd:PRK06064 258 DAAVvAAEKAYKMAGIEPKDIDVAEVHDCFTiAEILAyedlgfAKKGEGGKLARegqtyiggdipVNPSGGLKAKGHPVG 337
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1217747202 354 ASGCRILVS----LLYEM---QRREVNKGLAMLCIGGGQG 386
Cdd:PRK06064 338 ATGVSQAVEivwqLRGEAekgRQQVIGAGYGLTHNVGGTG 377
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
30-371 |
8.68e-12 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 66.02 E-value: 8.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 30 ELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPVTTPaLTINKVCGSGLKAVHLAVQAIRSGDA 109
Cdd:PRK12578 23 ELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVP-LRVEAMCATGLAASLTAYTAVASGLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 110 DAVIAGGQESMSR---SPYLMAGARAGLRLGHAQMVDSVIhDGLWDAFNDYHM---GITAENLA------EKYAiSREEQ 177
Cdd:PRK12578 102 DMAIAVGVDKMTEvdtSTSLAIGGRGGNYQWEYHFYGTTF-PTYYALYATRHMavyGTTEEQMAlvsvkaHKYG-AMNPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 178 DRFAlrsqqkaqaaqqagrfaqeiTPVTVPqpkgEALRVERDEQPrdtsLEALtrlrpafrkegtvtagNASSLNDGAAV 257
Cdd:PRK12578 180 AHFQ--------------------KPVTVE----EVLKSRAISWP----IKLL----------------DSCPISDGSAT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 258 VLLMSAEKAAALRL--PVLARIAGYASSGVDPAIMG--IG---PAPAARRCLEKAGWRLEEVDLIEANEAFAAQALAVGK 330
Cdd:PRK12578 216 AIFASEEKVKELKIdsPVWITGIGYANDYAYVARRGewVGfkaTQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYE 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1217747202 331 ELGW-------------EAER-----VNVNGGAIALGHPIGASGcrilVSLLYEM--QRRE 371
Cdd:PRK12578 296 DLGFtekgkggkfieegQSEKggkvgVNLFGGLKAKGHPLGATG----LSMIYEItkQLRD 352
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
67-356 |
7.60e-10 |
|
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: 60.24 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 67 PARQTALNAGLpvTTPALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSrSPYLMAGaraglrlgHAQMvdsvi 146
Cdd:cd00834 140 AAGQVAIRLGL--RGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALI-TPLTLAG--------FAAL----- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 147 hdglwdafndyhmgitaenlaekYAISREEQDrfalrsqqkaqaaqqagrfaqeitpvtvPQpkgEALR---VERDeqpr 223
Cdd:cd00834 204 -----------------------RALSTRNDD----------------------------PE---KASRpfdKDRD---- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 224 dtslealtrlrpafrkeGTVtagnassLNDGAAVVLLMSAEKAAALRLPVLARIAGYASSG-----VDPAIMGIGPAPAA 298
Cdd:cd00834 226 -----------------GFV-------LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAM 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1217747202 299 RRCLEKAGWRLEEVDLI-------EANEafAAQALAVGKELGWEAERVNVNGGAIALGHPIGASG 356
Cdd:cd00834 282 RAALADAGLSPEDIDYInahgtstPLND--AAESKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAG 344
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
6-356 |
1.26e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 56.11 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 6 VVIVAATRTPVGSfhgaLAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNA--GLpVTTPA 83
Cdd:PRK07516 4 ASIVGWAHTPFGK----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAGFSPQDFPASLVLQAdpAL-RFKPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 84 LTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPylmaGARAGLRLGHA--QMVDSVIHDGLWDAFndyhmGI 161
Cdd:PRK07516 79 TRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP----TAEVGDILLGAsyLKEEGDTPGGFAGVF-----GR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 162 TAENLAEKYAISREEQDRFALRSQQKAqaaqqagrfaqeitpvtVPQPKGEaLRVERDEQPRDTSLEALTRLRPAFRKEg 241
Cdd:PRK07516 150 IAQAYFQRYGDQSDALAMIAAKNHANG-----------------VANPYAQ-MRKDLGFEFCRTVSEKNPLVAGPLRRT- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 242 tvtagNASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYAS-----SGVDPAIMGiGPAPAARRCLEKAGWRLEEVDLIE 316
Cdd:PRK07516 211 -----DCSLVSDGAAALVLADAETARALQRAVRFRARAHVNdflplSRRDPLAFE-GPRRAWQRALAQAGVTLDDLSFVE 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1217747202 317 ANEAFA--------AQALA-------VGKElGWEAER----VNVNGGAIALGHPIGASG 356
Cdd:PRK07516 285 THDCFTiaelieyeAMGLAppgqgarAIRE-GWTAKDgklpVNPSGGLKAKGHPIGATG 342
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
82-134 |
2.87e-08 |
|
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: 54.18 E-value: 2.87e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYLMAGARAGL 134
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGM 217
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
67-356 |
8.22e-08 |
|
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: 53.95 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 67 PARQTALNAGLpvTTPALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSrSPYLMAGaraglrlghaqmvdsvi 146
Cdd:COG0304 140 AAGHVSIRFGL--KGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAI-TPLGLAG----------------- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 147 hdglWDAfndyhMGitaenlaekyAISReeqdrfalrsqqkaqaaqqagrfaqeitpvtvpqpkgealrveRDEQPRDTS 226
Cdd:COG0304 200 ----FDA-----LG----------ALST-------------------------------------------RNDDPEKAS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 227 lealtrlRPaFRKE--GTVTAGnasslndGAAVVLLMSAEKAAALRLPVLARIAGYASSG-----VDPAIMGIGPAPAAR 299
Cdd:COG0304 218 -------RP-FDKDrdGFVLGE-------GAGVLVLEELEHAKARGAKIYAEVVGYGASSdayhiTAPAPDGEGAARAMR 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1217747202 300 RCLEKAGWRLEEVDLI-------EANEafAAQALAVGKELGWEAERVNVNggAI--ALGHPIGASG 356
Cdd:COG0304 283 AALKDAGLSPEDIDYInahgtstPLGD--AAETKAIKRVFGDHAYKVPVS--STksMTGHLLGAAG 344
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
82-116 |
1.19e-07 |
|
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: 53.33 E-value: 1.19e-07
10 20 30
....*....|....*....|....*....|....*
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGG 116
Cdd:cd00833 162 PSLTVDTACSSSLVALHLACQSLRSGECDLALVGG 196
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
30-361 |
1.55e-07 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 52.77 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 30 ELGTAAVQGLLAQSGVAPQQIDEVILGQV---LTAGCGQNPARQTALNAGLpVTTPALTINKVCGSGLKAVHLAVQAIRS 106
Cdd:PRK06289 28 DLTREVVDGTLAAAGVDADDIEVVHVGNFfgeLFAGQGHLGAMPATVHPAL-WGVPASRHEAACASGSVATLAAMADLRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 107 GDADAVIAGGQESMSRSPylmaGARAGLRLGHAQMVDSVIHDG--LW-DAFNDyhmgitaenLAEKYAiSREEQDRFALR 183
Cdd:PRK06289 107 GRYDVALVVGVELMKTVP----GDVAAEHLGAAAWTGHEGQDArfPWpSMFAR---------VADEYD-RRYGLDEEHLR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 184 sqqkaqaaqqagrfaqEITPVTVPQPKGEALRVERDEQPRDTSLEALTRLRPAFrkEGTVTAGNASSLNDGAAVVLLMSA 263
Cdd:PRK06289 173 ----------------AIAEINFANARRNPNAQTRGWAFPDEATNDDDATNPVV--EGRLRRQDCSQVTDGGAGVVLASD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 264 EKAAAL-RLPVLARIAGY-------------ASSGVDPAIMgigpaPAARRCLE----KAGWRLEEVDLIEANEAFAAQA 325
Cdd:PRK06289 235 AYLRDYaDARPIPRIKGWghrtaplgleqklDRSAGDPYVL-----PHVRQAVLdayrRAGVGLDDLDGFEVHDCFTPSE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1217747202 326 LAVGKELG-------WEA-----------ERVNVNGGAIALGHPIGASGCRILV 361
Cdd:PRK06289 310 YLAIDHIGltgpgesWKAiengeiaiggrLPINPSGGLIGGGHPVGASGVRMLL 363
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
251-356 |
1.33e-06 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 50.17 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 251 LNDGAAVVLLMSAEKAAALRLPVLARIAGYASSG-----VDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEA-------N 318
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDYINAhgtstpaG 309
|
90 100 110
....*....|....*....|....*....|....*...
gi 1217747202 319 EAFAAQAlaVGKELGWEAERVNVNGGAIALGHPIGASG 356
Cdd:PRK07314 310 DKAETQA--IKRVFGEHAYKVAVSSTKSMTGHLLGAAG 345
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
83-116 |
2.28e-06 |
|
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: 48.86 E-value: 2.28e-06
10 20 30
....*....|....*....|....*....|....
gi 1217747202 83 ALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGG 116
Cdd:smart00825 90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
82-356 |
6.34e-06 |
|
"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: 47.82 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMsrSPYLMAGARAglrlghaqmvdsvihdglwdafndyhMGI 161
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDP--LEEGLSGFAN--------------------------MGA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 162 TAENLAEKYAISReeqdrfalrsqqkaqaaqqagrfaqeitpvtvpqpkgealrverdeqprdtslealtrlRPAFRKEG 241
Cdd:cd00828 206 LSTAEEEPEEMSR-----------------------------------------------------------PFDETRDG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 242 TVTAGnasslndGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAPAARRCLE----KAGWRLEEVDLIEA 317
Cdd:cd00828 227 FVEAE-------GAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGIARAIRtalaKAGLSLDDLDVISA 299
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1217747202 318 -----NEAFAAQALAVGKELGWEAERVNVNGGAIALGHPIGASG 356
Cdd:cd00828 300 hgtstPANDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAG 343
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
27-122 |
1.05e-05 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 46.78 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 27 TAVELGTAAVQGLLAQSGVAPQQIDEVILGQVLTAGCGQNPARQTALNAGLPvTTPALTINKVCGSGLKAVHLAVQAIRS 106
Cdd:PRK12879 52 YTSDLAIKAAERALARAGLDAEDIDLIIVATTTPDYLFPSTASQVQARLGIP-NAAAFDINAACAGFLYGLETANGLITS 130
|
90
....*....|....*.
gi 1217747202 107 GDADAVIAGGQESMSR 122
Cdd:PRK12879 131 GLYKKVLVIGAERLSK 146
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
82-116 |
1.31e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 47.56 E-value: 1.31e-05
10 20 30
....*....|....*....|....*....|....*
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGG 116
Cdd:COG3321 166 PSVTVDTACSSSLVAVHLACQSLRSGECDLALAGG 200
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
31-356 |
1.52e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 46.82 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 31 LGTAAVQGLLAQSGVAPQQIDEVILGQVLTAG-CGQNPARQTALnAGLPVTTpaltINKVCGSGLKAVHLAVQAIRSGDA 109
Cdd:PRK08256 25 MAAEAGRAALADAGIDYDAVQQAYVGYVYGDStSGQRALYEVGM-TGIPIVN----VNNNCSTGSTALFLARQAVRSGAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 110 DAVIAGGQESMSRspylmaGARAGLRLGHAQMVDSviHDGLWDAFNDY----------------HM---GITAENLAEKY 170
Cdd:PRK08256 100 DCALALGFEQMQP------GALGSVWDDRPSPLER--FDKALAELQGFdpappalrmfggagreHMekyGTTAETFAKIG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 171 AISReeqdRFALRSqqkaqaaqqagrfaqeitpvtvpqpkgeALRVERDEQPRDTSLEA------LTRLRpafrkegtvt 244
Cdd:PRK08256 172 VKAR----RHAANN----------------------------PYAQFRDEYTLEDVLASpmiwgpLTRLQ---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 245 agnASSLNDGAAVVLLMSAEKAAALRLPVLARIAGYA-----SSGVDP--AIMGIG---PAPAARRCLEKAGWRLEEVDL 314
Cdd:PRK08256 210 ---CCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQAmttdtPSTFDGrsMIDLVGydmTRAAAQQVYEQAGIGPEDIDV 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 315 IEANEAFAAQALAVGKELGW----EAER--------------VNVNGGAIALGHPIGASG 356
Cdd:PRK08256 287 VELHDCFSANELLTYEALGLcpegEAEKfiddgdntyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
4-367 |
1.56e-05 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 46.56 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 4 REVVIVAATRTPVGSFHGALAPLTAVElgtaAVQGLLAQSGVAPQQIDEVILG---QVLTAGCGQNPARQTALNAGLPVT 80
Cdd:PRK06157 7 DKVAILGMGCTKFGERWDAGAEDLMVE----AFLEALADAGIEPKDIDAAWFGthyDEIGSGKSGTPLSRALRLPNIPVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 81 TpaltINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSRSPYlmAGARAGLRLGHAQMVDSVihdglWDAFNDYHMG 160
Cdd:PRK06157 83 R----VENFCATGSEAFRGAVYAVASGAYDIALALGVEKLKDTGY--GGLPVANPGTLADMTMPN-----VTAPGNFAQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 161 ITAenLAEKYAISREEQDRfalrsqqkaqaaqqagrfaqEITPVTVPQPKGEALRVE---RDEQPRDTSLEAltrlrPaf 237
Cdd:PRK06157 152 ASA--YAAKYGVSREDLKR--------------------AMAHVSVKSHANGARNPKahlRKAVTEEQVLKA-----P-- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 238 RKEGTVTAGNASSLNDGAAVVLLMSAEKAAALRL--PV------LARIAGYASSGVD------PAImgigpAPAARRCLE 303
Cdd:PRK06157 203 MIAGPLGLFDCCGVSDGAAAAIVTTPEIARALGKkdPVyvkalqLAVSNGWELQYNGwdgsyfPTT-----RIAARKAYR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 304 KAGWR--LEEVDLIEANEAFAAQALAVGKELG-------WEAER-----------VNVNGGAIALGHPIGASGCRilvsL 363
Cdd:PRK06157 278 EAGITdpREELSMAEVHDCFSITELVTMEDLGlsergqaWRDVLdgffdadgglpCQIDGGLKCFGHPIGASGLR----M 353
|
....
gi 1217747202 364 LYEM 367
Cdd:PRK06157 354 LYEM 357
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
251-356 |
4.58e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 45.04 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 251 LNDGAAVVLLMSAEKAAALRLPVLARIAGY-----ASSGVDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEA-------N 318
Cdd:PRK05952 208 LGEGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAhgtatrlN 287
|
90 100 110
....*....|....*....|....*....|....*...
gi 1217747202 319 EAFAAQALAVgkelgWEAERVNVNGGAIALGHPIGASG 356
Cdd:PRK05952 288 DQREANLIQA-----LFPHRVAVSSTKGATGHTLGASG 320
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
11-122 |
1.39e-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: 43.30 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 11 ATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILgqvltagCGQNPARQT---------ALNAGlpvTT 81
Cdd:cd00830 33 RTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIV-------ATSTPDYLFpataclvqaRLGAK---NA 102
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1217747202 82 PALTINKVCGSGLKAVHLAVQAIRSGDADAVIAGGQESMSR 122
Cdd:cd00830 103 AAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSR 143
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
27-122 |
2.40e-04 |
|
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: 42.79 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 27 TAVELGTAAVQGLLAQSGVAPQQIDEVILG-----QVL--TAgcgqnpAR-QTALNAglpVTTPALTINKVCGSGLKAVH 98
Cdd:COG0332 50 TTSDLAVEAARKALEAAGIDPEDIDLIIVAtvtpdYLFpsTA------CLvQHKLGA---KNAAAFDINAACSGFVYALS 120
|
90 100
....*....|....*....|....*
gi 1217747202 99 LAVQAIRSGDADAV-IAGGqESMSR 122
Cdd:COG0332 121 VAAALIRSGQAKNVlVVGA-ETLSR 144
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
7-114 |
4.05e-04 |
|
"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: 42.03 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 7 VIVAATRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQvlTAGCGQNPARQTALNA--GLPVTTPAL 84
Cdd:cd00827 27 VDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVAT--ESPIDKGKSAATYLAEllGLTNAEAFD 104
|
90 100 110
....*....|....*....|....*....|
gi 1217747202 85 TINkVCGSGLKAVHLAVQAIRSGDADAVIA 114
Cdd:cd00827 105 LKQ-ACYGGTAALQLAANLVESGPWRYALV 133
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
12-122 |
5.91e-04 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 41.60 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 12 TRTPVGSFHGALAPLTAVELGTAAVQGLLAQSGVAPQQIDEVILGQV-------LTAgcgqnPARQTALNAglpVTTPAL 84
Cdd:PRK09352 36 TRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVATTtpdyafpSTA-----CLVQARLGA---KNAAAF 107
|
90 100 110
....*....|....*....|....*....|....*....
gi 1217747202 85 TINKVCgSG-LKAVHLAVQAIRSGDADAVIAGGQESMSR 122
Cdd:PRK09352 108 DLSAAC-SGfVYALSTADQFIRSGAYKNVLVIGAEKLSR 145
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
251-356 |
1.47e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 40.48 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 251 LNDGAAVVLLMSAEKAAALRLPVLARI--AGYASSG---VDPAIMGIGPAPAARRCLEKAGWRLEEVDLIEANEAFA--- 322
Cdd:PRK07910 240 FGEGGALMVIETEEHAKARGANILARImgASITSDGfhmVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTsvg 319
|
90 100 110
....*....|....*....|....*....|....*.
gi 1217747202 323 --AQALAVGKELGweAERVNVNGGAIALGHPIGASG 356
Cdd:PRK07910 320 dvAEGKAINNALG--GHRPAVYAPKSALGHSVGAVG 353
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
274-372 |
1.94e-03 |
|
Beta-ketoacyl synthase, C-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.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 37.93 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 274 LARIAGYASSGVDPAIMGIGPAPAA-----RRCLEKAGWRLEEVDLIEAN-----EAFAAQALAVGKELGWEAERVNVNG 343
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGqaraiRRALADAGVDPEDVDYVEAHgtgtpLGDPIEAEALKRVFGSGARKQPLAI 80
|
90 100 110
....*....|....*....|....*....|.
gi 1217747202 344 GAI--ALGHPIGASGCRILVSLLYEMQRREV 372
Cdd:pfam02801 81 GSVksNIGHLEGAAGAAGLIKVVLALRHGVI 111
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
253-333 |
2.50e-03 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 39.65 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 253 DGAAVVLLMSAEKAAALRLPVLARIAGYASSGVDPAIMGIGPAP--AARRCLEKAGWRLEEVDLIEAN-----EAFAAQA 325
Cdd:cd00832 229 EGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPPGLarAIRLALADAGLTPEDVDVVFADaagvpELDRAEA 308
|
....*...
gi 1217747202 326 LAVGKELG 333
Cdd:cd00832 309 AALAAVFG 316
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
254-368 |
5.82e-03 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 38.47 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 254 GAAVVLLMSAEKAAALRLPVLARIAGY-----ASSGVDPAImgIGPAPAARRCLEKAGWRLEEVDLIEANeafaaqalAV 328
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWsmrldANRGPDPSL--EGEMRVIRAALRRAGLGPEDIDYVNPH--------GT 309
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1217747202 329 GKELGWEAE----------RVNVNGGAIALGHPIGASGCRILVSLLYEMQ 368
Cdd:PRK07103 310 GSPLGDETElaalfasglaHAWINATKSLTGHGLSAAGIVELIATLLQMR 359
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
249-368 |
6.18e-03 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 38.72 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217747202 249 SSLNDGAAVVLLMSAEKAAALRL-PVLARIAGYASSGV-------DP--AIMGIGPAPAARRCLEKAGWRLEEVDLIEAN 318
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLsPNDSRLVEIKSLACasgnlyeDPpdATRMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1217747202 319 EAFAAQALAVGKELGW-------EAER-----------VNVNGGAIALGHPIGASGCRILVSLLYEMQ 368
Cdd:PTZ00455 336 DCFTIAELLMYEALGIaeyghakDLIRngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
|
|
| |
