|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-392 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 689.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVS 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 161 AENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQRNGQSLVVDTDEQPRTDASAEGLARLDPTFDRLG 239
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVtIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 240 SVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEAF 319
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124112 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIERD 392
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-391 |
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: 598.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVS 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLgNSQLVDSLVHDGLWDAFNDYHMGVT 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 161 AENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQRNGQSLVVDTDEQPRTDASAEGLARLDPTFDRLGS 240
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 241 VTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEAFA 320
Cdd:COG0183 240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489124112 321 AQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:COG0183 320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-392 |
0e+00 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 596.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVS 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 161 AENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQRNGQSLVVDTDEQPRTDASAEGLARLDPTFDRLG 239
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIlIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 240 SVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEAF 319
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124112 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIERD 392
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIERD 393
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-391 |
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: 580.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 5 VIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVSAITI 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 85 NDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLvDSLVHDGLWDAFNDYHMGVTAENL 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 165 AREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQRNGQSLVVDTDEQPRTDASAEGLARLDPTFDRLGSVTAG 244
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 245 NASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEAFAAQAL 324
Cdd:cd00751 240 NASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQAL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124112 325 SVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:cd00751 320 ACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-390 |
1.00e-174 |
|
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: 492.13 E-value: 1.00e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 6 IVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVSAITIN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 86 DVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDS-RTGAQLGNSQLVDSLVHDgLWDAFNDYHMGVTAENL 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 165 AREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQRNGQSLVVDTDEQPRTDASAEGLARLDPTFDRLGSVTAG 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 245 NASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEAFAAQAL 324
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489124112 325 SVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIE 390
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-390 |
3.18e-157 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 448.01 E-value: 3.18e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVS 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 161 AENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQRNGQSLVVDTDEQPRTDASAEGLARLDPTFDRLG 239
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVtIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 240 SVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEAF 319
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489124112 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIE 390
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-391 |
3.72e-153 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 437.85 E-value: 3.72e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVL-TAGAGQNPARQSAINGGLPNTV 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpTEPRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVhDGLWDAFNDYHMGV 159
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMV-GALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 160 TAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQRNGQSLVVDTDEQPRTDASAEGLARLDPTFDR-L 238
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKeN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 239 GSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEA 318
Cdd:PRK09051 241 GTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124112 319 FAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:PRK09051 321 FAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-391 |
8.31e-151 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 431.82 E-value: 8.31e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 2 KEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVSA 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 82 ITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHMGVTA 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 162 ENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV--VTQRNGQSLVVDTDEQPrTDASAEGLARLDPTFDR-L 238
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVevPGGRGRPSVIVDKDEGL-GKFDPAKLRKLRPSFKEdG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 239 GSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEA 318
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124112 319 FAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-390 |
5.57e-146 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 419.44 E-value: 5.57e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVS 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVlTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHG-SYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 161 AENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQRNGQSLVvDTDEQPRTDASAEGLARLDPTFDRLG 239
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIeVTIKKTTSLF-DHDETVRPDTSLEILSKLRPAFDKNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 240 SVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEAF 319
Cdd:PRK06633 240 VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489124112 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIE 390
Cdd:PRK06633 320 AAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-391 |
8.74e-143 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 411.69 E-value: 8.74e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQvlTAGAGQNPA--RQSAINGGLPNT 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHdGLWDAFNDYH-- 156
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRLAR-GRETAGGRRFpv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 157 ---MGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQRNGQSLVVDTDEQPRTDASAEGLARLD 232
Cdd:PRK06205 158 pggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVtVPQRKGDPTVVDRDEHPRADTTLESLAKLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 233 P---TFDRLGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAD 309
Cdd:PRK06205 238 PimgKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 310 VDLIEANEAFAAQALSVGKMLEW---DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVA 386
Cdd:PRK06205 318 IDLIELNEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLA 397
|
....*
gi 489124112 387 LAIER 391
Cdd:PRK06205 398 AVFER 402
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-391 |
6.59e-135 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 391.62 E-value: 6.59e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERT-GVDVHAVDEVILGQVLTAGA-GQNPARQSAINGGLPNT 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSrTGAQLGNSQLVDS-----LVHDGLWDAFN 153
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKA-DSAFSRQAEIFDTtigwrFVNPLMKAQYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 154 DYHMGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQRNGQSLVVDTDEQPRTDASAEGLARLD 232
Cdd:PRK09050 160 VDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVtIPQKKGDPVVVDRDEHPRPETTLEALAKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 233 PTFDRLGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDL 312
Cdd:PRK09050 240 PVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 313 IEANEAFAAQALSVGKMLEW--DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIE 390
Cdd:PRK09050 320 IELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIE 399
|
.
gi 489124112 391 R 391
Cdd:PRK09050 400 R 400
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-391 |
4.04e-122 |
|
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.
Pssm-ID: 131483 Cd Length: 400 Bit Score: 359.10 E-value: 4.04e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 2 KEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERT-GVDVHAVDEVILGQVLTAGA-GQNPARQSAINGGLPNTV 79
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRT----GAQLGNSQLVDSLVHDGLWDAFNDY 155
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSafsrSAKIEDTTIGWRFINPLMKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 156 HMGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQRNGQSLVVDTDEQPRTDASAEGLARLDPT 234
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVvIPQKKGEPTVVDQDEHPRPETTLEGLAKLKPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 235 FDRLGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIE 314
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489124112 315 ANEAFAAQALSVGKMLEW--DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:TIGR02430 321 LNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-262 |
4.46e-121 |
|
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: 351.22 E-value: 4.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 4 VVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVSAIT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVL-TDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHMGVTAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 163 NLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQRNGQsLVVDTDEQPRTDASAEGLARLDPTFDRLGSV 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVtVKGRKGK-PTVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
|
250 260
....*....|....*....|.
gi 489124112 242 TAGNASSINDGAAAVMMMSEA 262
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-391 |
5.89e-119 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 350.42 E-value: 5.89e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHS-AVELGSMVVRALLERT-GVDVHAVDEVILGQVL-TAGAGQNPARQSAINGGLPN 77
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAFRNVrAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQqTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 78 TVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSrapHVltdsrtgaqlGNSQLVDSLVHDGLWDAFNDYHM 157
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMG---HV----------PMNHGVDFHPGLSKNVAKAAGMM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 158 GVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQ-RNGQSLVVDTDEQPRTDASAEGLARLDPTFD 236
Cdd:PRK08947 148 GLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHdADGVLKLFDYDEVIRPETTVEALAALRPAFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 237 -RLGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEA 315
Cdd:PRK08947 228 pVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489124112 316 NEAFAAQALSVGK---MLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:PRK08947 308 NEAFAAQSLPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFER 386
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-390 |
1.74e-117 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 347.26 E-value: 1.74e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVS 80
Cdd:PRK06954 6 QDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYH-MGV 159
Cdd:PRK06954 86 CTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 160 TAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQRNGQSLVVDTDEQPRTdASAEGLARLDPTFDRLG 239
Cdd:PRK06954 166 FAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAFSKTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 240 SVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEAF 319
Cdd:PRK06954 245 TVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAF 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489124112 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIE 390
Cdd:PRK06954 325 AVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.76e-115 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 341.73 E-value: 1.76e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIG-CFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVL-TAGAGQNPARQSAINGGLPNT 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP---HVLTDsrtgaqlgNSQLVDSLvhdglwdafNDY 155
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPmmgHVVRP--------NPRLVEAA---------PEY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 156 HMGV--TAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQR----NGQ----SLVVDTDEQPRTDAS 224
Cdd:PRK07661 144 YMGMghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVdVTLRtvgeNNKlqeeTITFSQDEGVRADTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 225 AEGLARLDPTFDRLGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVG 304
Cdd:PRK07661 224 LEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 305 WQLADVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQG 384
Cdd:PRK07661 304 LELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMG 383
|
....*..
gi 489124112 385 VALAIER 391
Cdd:PRK07661 384 AAGVFEL 390
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-390 |
5.10e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 338.14 E-value: 5.10e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVS 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVL-TDSRTGAQ---LGNSQLVDSLVHDGLWDAFNDYH 156
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPKhllHKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 157 MGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVvtqrNGqslvVDTDEQPRTdASAEGLARLDPTFD 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPF----ND----LDRDEGIRK-TTMEDLAKLPPAFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 237 RLGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEAN 316
Cdd:PRK06366 232 KNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489124112 317 EAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIE 390
Cdd:PRK06366 312 EAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.02e-113 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 337.46 E-value: 1.02e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCF------QGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLtaGAGQN---PARQSAI 71
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFrpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENwlyGGRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 72 NGGLPNTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP-----HV------LTDSRtgaqlgnsqlv 140
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPmgdnpHIepnpklLTDPK----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 141 dsLVHdglWDAFNDYHMGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQRNGQSLVVDTDEQPR 220
Cdd:PRK06445 148 --YIE---YDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 221 TDASAEGLARLDPTFDRLGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCL 300
Cdd:PRK06445 223 PDTSLEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 301 ERVGWQLADVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIG 380
Cdd:PRK06445 303 EKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVG 382
|
410
....*....|.
gi 489124112 381 GGQGVALAIER 391
Cdd:PRK06445 383 GGQGGAVVLER 393
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-392 |
2.48e-110 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 330.96 E-value: 2.48e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 3 EVVIVGALRTPI-----GCFQGTLArhsaVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQ-NPARQSAINGGLP 76
Cdd:PLN02287 47 DVVIVAAYRTPIckakrGGFKDTYP----DDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 77 NTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHdglwdafndyh 156
Cdd:PLN02287 123 ETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP----------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 157 MGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQR------NGQSLVVDTDEQPRTDASAEGLAR 230
Cdd:PLN02287 192 MGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIvdpktgEEKPIVISVDDGIRPNTTLADLAK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 231 LDPTFDRLGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADV 310
Cdd:PLN02287 272 LKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 311 DLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMvKRR---AHKGLATLCIGGGQGVAL 387
Cdd:PLN02287 352 DLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEM-KRRgkdCRFGVVSMCIGTGMGAAA 430
|
....*
gi 489124112 388 AIERD 392
Cdd:PLN02287 431 VFERG 435
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-391 |
3.58e-109 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 325.80 E-value: 3.58e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAV-ELGSMVVRALLERT-GVDVHAVDEVILGQVL-TAGAGQNPARQSAINGGLPN 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGKAPRGMFKNTRPdDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 78 TVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvltdsrtgaQLGNSQLVDSLVHDGLWDAFNDYHM 157
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP----------MMGNKPSMSPAIFARDENVGIAYGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 158 GVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQR-----NGQSLV----VDTDEQPRTDASAEG 227
Cdd:PRK09052 155 GLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYeITERfpdlaTGEVDVktrtVDLDEGPRADTSLEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 228 LARLDPTFDRLGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQL 307
Cdd:PRK09052 235 LAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 308 ADVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVAL 387
Cdd:PRK09052 315 DDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAG 394
|
....
gi 489124112 388 AIER 391
Cdd:PRK09052 395 IFER 398
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-391 |
5.02e-107 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 320.68 E-value: 5.02e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQ--GTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAG-AGQNPARQSAINGGLPN 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 78 TVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvltdsrTGAQlGNSQLVDSLVhdglwdAFNDYHM 157
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP-------MGSD-GGAWAMDPST------NFPTYFV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 158 --GVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQrNGQsLVVDTDEQPRTDASAEGLARLDPTF 235
Cdd:PRK08242 147 pqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQ-NGL-TILDHDEHMRPGTTMESLAKLKPSF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 236 DRLGSV---------------------TAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVY 294
Cdd:PRK08242 225 AMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 295 ATRRCLERVGWQLADVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGL 374
Cdd:PRK08242 305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTAL 384
|
410
....*....|....*..
gi 489124112 375 ATLCIGGGQGVALAIER 391
Cdd:PRK08242 385 ITLCVGGGMGIATIIER 401
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-391 |
7.65e-106 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 317.49 E-value: 7.65e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGA-GQNPARQSAINGGLPNTV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLT-------------DSRTGAQLGNSQLVDSlvhd 146
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGkaesafsrdakvfDTTIGARFPNPKIVAQ---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 147 glwdaFNDYHMGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVP--VVTQRNGQSLVVDTDEQPRTDAS 224
Cdd:PRK08131 157 -----YGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPieVPQGRKLPPKLVAEDEHPRPSST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 225 AEGLARLDPTFDRlGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVG 304
Cdd:PRK08131 232 VEALTKLKPLFEG-GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 305 WQLADVDLIEANEAFAAQALSVGKML--EWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGG 382
Cdd:PRK08131 311 LTLDDMDIIEINEAFASQVLGCLKGLgvDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVG 390
|
....*....
gi 489124112 383 QGVALAIER 391
Cdd:PRK08131 391 QGLAMVIER 399
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.10e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 317.33 E-value: 1.10e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIG-CFQGTLARHSAVELGSMVVRALLERT-GVDVHAVDEVILGQVLTAG-AGQNPARQSAINGGLPn 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 78 TVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDS--------------RTG--AQLGNSQLVD 141
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSlpdtknplfaeaqaRTAarAEGGAEAWHD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 142 SLVHDGLWDAFndYHMGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVvTQRNGQslVVDTDEQPRT 221
Cdd:PRK07851 160 PREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPV-TLPDGT--VVSTDDGPRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 222 DASAEGLARLDPTFDRLGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLE 301
Cdd:PRK07851 235 GTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 302 RVGWQLADVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGG 381
Cdd:PRK07851 315 RAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGG 394
|
410
....*....|
gi 489124112 382 GQGVALAIER 391
Cdd:PRK07851 395 GQGMAMVLER 404
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-391 |
4.20e-102 |
|
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: 307.64 E-value: 4.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 3 EVVIVGALRTPIGCFQGTLARHSAVE-LGSMVVRALLER-TGVDVHAVDEVILGQV-LTAGAGQNPARQSAINGGLPNTV 79
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTRAEdLSAHLMSKLLARnPKVDPAEVEDIYWGCVqQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvltdsrtgaqlgnSQLVDSLVHDGLWDAFNDYHMGV 159
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPM-------------MHGVDFHPGMSLHVAKAAGMMGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 160 TAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQ-RNGQSLVVDTDEQPRTDASAEGLARLDPTFDRL 238
Cdd:TIGR02445 148 TAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHdADGFLKQFDYDEVIRPETTVESLAALRPAFDPK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 239 -GSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANE 317
Cdd:TIGR02445 228 nGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124112 318 AFAAQALSVGK---MLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:TIGR02445 308 AFAAQALPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.51e-100 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 302.78 E-value: 2.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAG--AGqNPARQSAINGGLPNT 78
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpqAG-NIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvLTDSRT-GAQLGnsqLVDSLVHDGLWDA-FNDYH 156
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTaGEQLG---FTSPFAESKGWLHrYGDQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 157 MG--VTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVvtqrNGqslvVDTDEQPRtDASAEGLARLDPT 234
Cdd:PRK07801 155 VSqfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV----GG----VTVDEGPR-ETSLEKMAGLKPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 235 FDRlGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIE 314
Cdd:PRK07801 226 VEG-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVE 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124112 315 ANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:PRK07801 305 INEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.04e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 297.70 E-value: 1.04e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVS 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDS--RTGAQLGNSQ-LVDSLVH------------ 145
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKmvRWLAGWYAAKsIGQKLAAlgklrpsylapv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 146 ----DGLWDAFNDYHMGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKdEIVPVVTqRNGQslVVDTDEQPRT 221
Cdd:PRK08170 162 igllRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFD-RDGK--FYDHDDGVRP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 222 DASAEGLARLDPTFDR-LGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCL 300
Cdd:PRK08170 238 DSSMEKLAKLKPFFDRpYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 301 ERVGWQLADVDLIEANEAFAAQALSV-----------------GKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVH 363
Cdd:PRK08170 318 QRHGLTLEDLDLWEINEAFAAQVLAClaawadeeycreqlgldGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLH 397
|
410 420
....*....|....*....|....*...
gi 489124112 364 EMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:PRK08170 398 ALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-391 |
5.35e-97 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 294.32 E-value: 5.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGA-GQNPARQSAINGGLPNTV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvlTDSRTGAQLGNSQlvdslVHDGLWDAFNDYhmgV 159
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP---LGANAGPGRGLPR-----PDSWDIDMPNQF---E 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 160 TAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVT-------QRNGQSLVVDTDEQPRtDASAEGLARLD 232
Cdd:PRK07850 150 AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQApvldeegQPTGETRLVTRDQGLR-DTTMEGLAGLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 233 PTFDRlGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDL 312
Cdd:PRK07850 229 PVLEG-GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489124112 313 IEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:PRK07850 308 VEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-392 |
8.01e-91 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 279.95 E-value: 8.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 4 VVIVGALRTPigcF--QGTLARH-SAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVS 80
Cdd:PRK08963 7 IAIVSGLRTP---FakQATAFHGiPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP--------HVLTDSRTGAQLGnsQLVDSLVHDGLWD-- 150
Cdd:PRK08963 84 AYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaRALVDLNKARTLG--QRLKLFSRLRLRDll 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 151 ----AFNDY----HMGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQRNGQSLvvDTDEQPRTD 222
Cdd:PRK08963 162 pvppAVAEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPL--EEDNNIRGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 223 ASAEGLARLDPTFDR-LGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDP---ALMGiaPVYATRR 298
Cdd:PRK08963 240 STLEDYAKLRPAFDRkHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwqdMLLG--PAYATPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 299 CLERVGWQLADVDLIEANEAFAAQALSVGKML-----------------EWDERRVNVNGGAIALGHPIGASGCRILVSL 361
Cdd:PRK08963 318 ALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQT 397
|
410 420 430
....*....|....*....|....*....|.
gi 489124112 362 VHEMVKRRAHKGLATLCIGGGQGVALAIERD 392
Cdd:PRK08963 398 LHELRRRGGGLGLTTACAAGGLGAAMVLEVE 428
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-391 |
4.00e-90 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 276.99 E-value: 4.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAG-AGQNPARQSAINGGLPNTV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDS---RTGAQLGNSQLVDSLVHDGLWDAFndyh 156
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTlpaKNGLGHYKSPGMEERYPGIQFSQF---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 157 MGvtAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPV-VTQRNGQSLVVDTDEQPRTDASAEGLARLDPTF 235
Cdd:PRK06504 157 TG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLeITRADGSGEMHTVDEGIRFDATLEGIAGVKLIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 236 DRlGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEA 315
Cdd:PRK06504 235 EG-GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEV 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489124112 316 NEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:PRK06504 314 NEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-386 |
3.56e-87 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 269.33 E-value: 3.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIG-CFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGA-GQNPARQSAINGGLPNT 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP-----HVLTDSrtgaqlgnsqlvdslvhdglWDAFN 153
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQnemnrHMLREG--------------------WLVEH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 154 D----YHMGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVvTQRNG-----------QSLVVDTDEQ 218
Cdd:PRK07108 141 KpeiyWSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPI-TVTAGvadkatgrlftKEVTVSADEG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 219 PRTDASAEGLARLDPTFDRlGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGIAPVYATRR 298
Cdd:PRK07108 220 IRPDTTLEGVSKIRSALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 299 CLERVGWQLADVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLC 378
Cdd:PRK07108 299 LLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMC 378
|
....*...
gi 489124112 379 IGGGQGVA 386
Cdd:PRK07108 379 IGGGQGAA 386
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-390 |
5.52e-86 |
|
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: 266.67 E-value: 5.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 7 VGALRTPIGCFQGTLARHS---AVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVSAIT 83
Cdd:cd00826 1 AGAAMTAFGKFGGENGADAndlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSraphvlTDSRTGAQlgnsqlvdslvhdglwdafnDYHMGVtaen 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME------TSAENNAK--------------------EKHIDV---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 164 LAREYGiSRELQDAYALHSQHKARMAIDAGRFKDEIVPVVTQRNGQSLVVDTDEQPR--TDASAEGLARLDPTFDRLGSV 241
Cdd:cd00826 131 LINKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQfgDEASLDEIAKLRPAFDKEDFL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 242 TAGNASSINDGAAAVMMMSEAKAQELNLPV-------LARIRAFASVGVDPA----LMGIAPVYATRRCLERVGWQLADV 310
Cdd:cd00826 210 TAGNACGLNDGAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 311 DLIEANEAFAAQALSVGKMLEWDERR------------------VNVNGGAIALGHPIGASGCRILVSLVHEMVKRR--- 369
Cdd:cd00826 290 DLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAgkr 369
|
410 420
....*....|....*....|...
gi 489124112 370 --AHKGLATLCIGGGQGVALAIE 390
Cdd:cd00826 370 qgAGAGLALLCIGGGGGAAMCIE 392
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-390 |
4.06e-80 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 250.07 E-value: 4.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 3 EVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALleRTGVDvHAVDEVILGQVLtaGAGQNPARQSAINGGLPNTVSAI 82
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGME-REIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 83 TINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvltdsRTGAQLGNsqlvdslvhdglwDAFNDYHMGVTAE 162
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF-----QNRARFSP-------------ETIGDPDMGVAAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 163 NLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVvtqrNGQSlvvdtDEQPRTDASAEGL-ARLDPTFDRLGSV 241
Cdd:PRK06690 139 YVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF----NGLL-----DESIKKEMNYERIiKRTKPAFLHNGTV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 242 TAGNASSINDGAAAVMMMSEAKAQELNL-PVLARIRAfASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEAFA 320
Cdd:PRK06690 210 TAGNSCGVNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFA 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 321 AQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIE 390
Cdd:PRK06690 289 SKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-391 |
8.91e-79 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 248.54 E-value: 8.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIG---CFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGA-GQNPARQSAINGGLP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 77 NTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvlTDSRTGAQLGNSQLVDSlVHDGLWDAFNDYH 156
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAA--MAAEDMAAGKPPLGMGS-GNLRLRALHPQSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 157 MGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVVtqRNGQSLVVDTDEQPRTDASAEGLARLDPTFD 236
Cdd:PRK06025 158 QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY--RDDGSVALDHEEFPRPQTTAEGLAALKPAFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 237 RLGSVT--------------------------AGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAFASVGVDPALMGI 290
Cdd:PRK06025 236 AIADYPlddkgttyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 291 APVYATRRCLERVGWQLADVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRRA 370
Cdd:PRK06025 316 APVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGL 395
|
410 420
....*....|....*....|.
gi 489124112 371 HKGLATLCIGGGQGVALAIER 391
Cdd:PRK06025 396 KRGLVTMCAAGGMAPAIIIER 416
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
269-391 |
1.32e-66 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 207.11 E-value: 1.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 269 LPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGH 348
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489124112 349 PIGASGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-391 |
4.34e-60 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 200.51 E-value: 4.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVS 80
Cdd:PRK09268 6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDS------------------RTGAQLGNSQLVDS 142
Cdd:PRK09268 86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGlrkillelnrakttgdrlKALGKLRPKHLAPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 143 LVHD-----GLwdafndyHMGVTAENLAREYGISRELQDAYALHSQHKARMAIDAGRFKDEIVPVvtqrngqsLVVDTDE 217
Cdd:PRK09268 166 IPRNgeprtGL-------SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF--------LGLTRDN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 218 QPRTDASAEGLARLDPTFDR--LGSVTAGNASSINDGAAAVMMMSEAKAQELNLPVLARIRAF--ASV----GVDPALMg 289
Cdd:PRK09268 231 NLRPDSSLEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetAAVdfvhGKEGLLM- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 290 iAPVYATRRCLERVGWQLADVDLIEANEAFAAQALSVGKMLEWDE-----------------RRVNVNGGAIALGHPIGA 352
Cdd:PRK09268 310 -APAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEycrerlgldaplgsidrSKLNVNGSSLAAGHPFAA 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 489124112 353 SGCRILVSLVHEMVKRRAHKGLATLCIGGGQGVALAIER 391
Cdd:PRK09268 389 TGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
26-389 |
6.49e-22 |
|
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: 93.66 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 26 AVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNtVSAITINDVCGSGLKALHLATQAIQCG 105
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISG-GPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 106 EADIVIAGGqenmsraphvltdsrtgaqlgnsqlvdslvhdglwdafndyhmgvtaenlareygisrelqdayalhsqhk 185
Cdd:cd00327 86 KADIVLAGG----------------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 186 armaidagrfkdeivpvvtqrngqslvvdtdeqprtdasaeglarldptfdrlgsvtaGNASSINDGAAAVMMMSEAKAQ 265
Cdd:cd00327 95 ----------------------------------------------------------SEEFVFGDGAAAAVVESEEHAL 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 266 ELNLPVLARIRAFASVGVD----PALMGIAPVYATRRCLERVGWQLADVDLIEANEAFAAQALSVGKMLEWDE---RRVN 338
Cdd:cd00327 117 RRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPdgvRSPA 196
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489124112 339 VNGGAIALGHPIGASGCRILVSLVHEM-------VKRRAHKGLATLCIGGGQGVALAI 389
Cdd:cd00327 197 VSATLIMTGHPLGAAGLAILDELLLMLehefippTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-373 |
1.78e-18 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 86.10 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGsmvvRALLERTGVDVHAVDEVILGQVLTAG-AGQ-NPARQSAINGGLPNt 78
Cdd:PRK06064 1 MRDVAIIGVGQTKFGELWDVSLRDLAVEAG----LEALEDAGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYAGLAP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLgnsqlvdslvhDGLWDAFndyhMG 158
Cdd:PRK06064 76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAG-----------DYEWEEF----FG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 159 VTAENL----AR----EYGISRELQDAYALHSQHKARMAIDAgRFKDEIvpvvtqrngqslvvDTDEQPRTDASAEGLAR 230
Cdd:PRK06064 141 ATFPGLyaliARrymhKYGTTEEDLALVAVKNHYNGSKNPYA-QFQKEI--------------TVEQVLNSPPVADPLKL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 231 LDptfdrlgsvtagnASSINDGAAAVMMMSEAKAQEL-NLPVlaRIRAFASVGVDPAL------MGI-APVYATRRCLER 302
Cdd:PRK06064 206 LD-------------CSPITDGAAAVILASEEKAKEYtDTPV--WIKASGQASDTIALhdrkdfTTLdAAVVAAEKAYKM 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 303 VGWQLADVDLIEANEAFA-AQALSV-----------GKMLEWDERR------VNVNGGAIALGHPIGASGCRILVSLVHE 364
Cdd:PRK06064 271 AGIEPKDIDVAEVHDCFTiAEILAYedlgfakkgegGKLAREGQTYiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQ 350
|
....*....
gi 489124112 365 MvKRRAHKG 373
Cdd:PRK06064 351 L-RGEAEKG 358
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
25-367 |
1.42e-14 |
|
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: 74.22 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 25 SAVELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSAINGGLPNTVsAITINDVCGSGLKALHLATQAIQC 104
Cdd:cd00829 15 SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKP-ATRVEAAGASGSAAVRAAAAAIAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 105 GEADIVIAGGQENMSRAPhvlTDSRTGAQLGNSQLVDSLVHDGLwdAFNDYHMGVTAENLAReYGISRElqdAYALhsqh 184
Cdd:cd00829 94 GLADVVLVVGAEKMSDVP---TGDEAGGRASDLEWEGPEPPGGL--TPPALYALAARRYMHR-YGTTRE---DLAK---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 185 karmaidagrfkdeiVPVVTQRNGQslvvdtdEQP----RTDASAEGLARLDPTFDRLgsvTAGNASSINDGAAAVMMMS 260
Cdd:cd00829 161 ---------------VAVKNHRNAA-------RNPyaqfRKPITVEDVLNSRMIADPL---RLLDCCPVSDGAAAVVLAS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 261 EAKAQELNLPvLARIRAFAsVGVDPALMG--------IAPVYATRRCLERVGWQLADVDLIE------ANEAFAAQAL-- 324
Cdd:cd00829 216 EERARELTDR-PVWILGVG-AASDTPSLSerddflslDAARLAARRAYKMAGITPDDIDVAElydcftIAELLALEDLgf 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489124112 325 ----SVGKMLEWDERR------VNVNGGAIALGHPIGASGcrilVSLVHEMVK 367
Cdd:cd00829 294 cekgEGGKLVREGDTAiggdlpVNTSGGLLSKGHPLGATG----LAQAVEAVR 342
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-354 |
1.20e-12 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 68.82 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPIGcfqgtlaRHSAVELGSMVVRAL---LERTGVDVHAVDEVILGQVltaGAGQNP-ARQSA----IN 72
Cdd:PRK07516 1 MMTASIVGWAHTPFG-------KLDAETLESLIVRVAreaLAHAGIAAGDVDGIFLGHF---NAGFSPqDFPASlvlqAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 73 GGLPNtVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvltdsrtGAQLGNSQLVDSLVHDGlwdaf 152
Cdd:PRK07516 71 PALRF-KPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP--------TAEVGDILLGASYLKEE----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 153 ndyhmGVTAENLAREYG-ISRELQDAYALHSQHKARMAidagrfkdeivpVVTQRNGqslVVDTDEQPRTDasaeglarL 231
Cdd:PRK07516 137 -----GDTPGGFAGVFGrIAQAYFQRYGDQSDALAMIA------------AKNHANG---VANPYAQMRKD--------L 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 232 DPTFDRLGS----VTAG-----NASSINDGAAAVMMMSEAKAQELNLPVlaRIRAFASVG-------VDPALMGiAPVYA 295
Cdd:PRK07516 189 GFEFCRTVSeknpLVAGplrrtDCSLVSDGAAALVLADAETARALQRAV--RFRARAHVNdflplsrRDPLAFE-GPRRA 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124112 296 TRRCLERVGWQLADVDLIEANEAF------------------AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASG 354
Cdd:PRK07516 266 WQRALAQAGVTLDDLSFVETHDCFtiaelieyeamglappgqGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATG 342
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
28-368 |
4.12e-11 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 64.10 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 28 ELGSMVVRALLERTGVDVHAVDEVILGQVLTAGAGQNPA----RQSAINGGLPNTVSAitindVCGSGLKALHLATQAIQ 103
Cdd:PRK12578 23 ELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPApivaEYSGLTGKVPLRVEA-----MCATGLAASLTAYTAVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 104 CGEADIVIAGGQENMSRaphvlTDSRT----GAQLGNSQlvdslvhdglWdafnDYHMgvtaenlareYGISreLQDAYA 179
Cdd:PRK12578 98 SGLVDMAIAVGVDKMTE-----VDTSTslaiGGRGGNYQ----------W----EYHF----------YGTT--FPTYYA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 180 LHSqhKARMAIDAGRFKD-EIVPVVTQRNGQSlvvDTDEQPRTDASAEglarldptfDRLGS------VTAGNASSINDG 252
Cdd:PRK12578 147 LYA--TRHMAVYGTTEEQmALVSVKAHKYGAM---NPKAHFQKPVTVE---------EVLKSraiswpIKLLDSCPISDG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 253 AAAVMMMSEAKAQELNL-----------------------------PVLARIRAFASVGVDPALMGIAPVYATRRCLERV 303
Cdd:PRK12578 213 SATAIFASEEKVKELKIdspvwitgigyandyayvarrgewvgfkaTQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIM 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489124112 304 GWQlaDVDLIEANEAfaaqalsvGKMLEWDERR------VNVNGGAIALGHPIGASGcrilVSLVHEMVKR 368
Cdd:PRK12578 293 GYE--DLGFTEKGKG--------GKFIEEGQSEkggkvgVNLFGGLKAKGHPLGATG----LSMIYEITKQ 349
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
33-114 |
7.93e-06 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 46.86 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 33 VVRALLERTGVDVHAVDEVILGQVLTAGAGQNPARQSA------------INGGLPNTVS------------AITINDVC 88
Cdd:pfam00109 94 AAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLdedggprrgspfAVGTMPSVIAgrisyflglrgpSVTVDTAC 173
|
90 100
....*....|....*....|....*.
gi 489124112 89 GSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:pfam00109 174 SSSLVAIHAAVQSIRSGEADVALAGG 199
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
34-354 |
2.61e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 46.04 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 34 VRALLERTGVDVHAVDEVILGQVltagAGQNPARQSAING----GLPntvsAITINDVCGSGLKALHLATQAIQCGEADI 109
Cdd:PRK08256 30 GRAALADAGIDYDAVQQAYVGYV----YGDSTSGQRALYEvgmtGIP----IVNVNNNCSTGSTALFLARQAVRSGAADC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 110 VIAGGQENMSRaphvltdsrtGAqlgnsqlvdslvhdgLWDAFNDyhmgvTAENLAREYGISRELQDAYALHSqhKARMA 189
Cdd:PRK08256 102 ALALGFEQMQP----------GA---------------LGSVWDD-----RPSPLERFDKALAELQGFDPAPP--ALRMF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 190 IDAGR-------FKDEIVPVVTQRNGQSLVVDTDEQPRTDASAEGLARLDPTFDRLgsvTAGNASSINDGAAAVMMMSEA 262
Cdd:PRK08256 150 GGAGRehmekygTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPL---TRLQCCPPTCGAAAAIVCSEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 263 KAQELNLPVLARIRA------FASVGVDPALMGIAPVYATRRCLERV----GWQLADVDLIEANEAFAAQAL-------- 324
Cdd:PRK08256 227 FARKHGLDRAVEIVAqamttdTPSTFDGRSMIDLVGYDMTRAAAQQVyeqaGIGPEDIDVVELHDCFSANELltyealgl 306
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489124112 325 ----SVGKMLEWDER----RVNVN--GGAIALGHPIGASG 354
Cdd:PRK08256 307 cpegEAEKFIDDGDNtyggRWVVNpsGGLLSKGHPLGATG 346
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
32-114 |
4.13e-05 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 45.24 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 32 MVVRALLERTGVDVHAVDE----VILGQ------VLTAGAGQNPARQSAINGG---LPNTVS--------AITINDVCGS 90
Cdd:cd00833 93 EVAWEALEDAGYSPESLAGsrtgVFVGAsssdylELLARDPDEIDAYAATGTSrafLANRISyffdlrgpSLTVDTACSS 172
|
90 100
....*....|....*....|....
gi 489124112 91 GLKALHLATQAIQCGEADIVIAGG 114
Cdd:cd00833 173 SLVALHLACQSLRSGECDLALVGG 196
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
81-114 |
2.65e-04 |
|
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: 42.32 E-value: 2.65e-04
10 20 30
....*....|....*....|....*....|....
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:smart00825 90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
185-354 |
3.95e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 41.98 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 185 KARMAIDAGRFKDEIVPVVTQRNgqslvvdtdeqpRTDASAEGLARLDPTFDRLGS-------VTAGNASSINDGAAAVM 257
Cdd:PRK07937 145 QARAGLDAGKWTEEQMAEVAARS------------RADARRNPSAEPSISVDELLArpyfadpLRRHDIAPITDGAAAVV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 258 MMSEAKAQELnLPVLARIRAFASvGVDPALMG---IAPVYATRRCLERV-GWQLADVDLIEANEAFAAQALSVGKMLEWD 333
Cdd:PRK07937 213 LAAGDRAREL-RERPAWITGIEH-RIESPSLGardLTRSPSTALAAEAAtGGDAGGVDVAELHAPFTHQELILREALGLG 290
|
170 180
....*....|....*....|..
gi 489124112 334 ER-RVNVNGGAIAlGHPIGASG 354
Cdd:PRK07937 291 DKtKVNPSGGALA-ANPMFAAG 311
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
82-119 |
6.64e-04 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 41.66 E-value: 6.64e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489124112 82 ITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMS 119
Cdd:cd00828 156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
1-381 |
7.32e-04 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 41.21 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 1 MKEVVIVGALRTPigcFQGTLARHSA--VELGSMVVRALLERTGVDVHAVDEVILGQVltagAGQNPARQSAInGGLPNT 78
Cdd:PRK06289 2 SDDVWVLGGYQSD---FARNWTKEGRdfADLTREVVDGTLAAAGVDADDIEVVHVGNF----FGELFAGQGHL-GAMPAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 79 VS-------AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvltDSRTGAQLGNSQLVDslvHDG---- 147
Cdd:PRK06289 74 VHpalwgvpASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVP----GDVAAEHLGAAAWTG---HEGqdar 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 148 -LW-DAFNDyhmgvTAENLAREYGISRElqdayalHSQHKARMAIDAGRfkdeivpvvtqRNGQSlvvdtdeQPRTDASA 225
Cdd:PRK06289 147 fPWpSMFAR-----VADEYDRRYGLDEE-------HLRAIAEINFANAR-----------RNPNA-------QTRGWAFP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 226 EGLARLDptfDRLGSVTAG-----NASSINDGAAAVMMMSEAKAQEL-NLPVLARIRAFasvGVDPALMGIAPVYA---- 295
Cdd:PRK06289 197 DEATNDD---DATNPVVEGrlrrqDCSQVTDGGAGVVLASDAYLRDYaDARPIPRIKGW---GHRTAPLGLEQKLDrsag 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 296 -------TRRCLE----RVGWQLADVDLIEANEAFAA------------------QALSVGKMLEWDERRVNVNGGAIAL 346
Cdd:PRK06289 271 dpyvlphVRQAVLdayrRAGVGLDDLDGFEVHDCFTPseylaidhigltgpgeswKAIENGEIAIGGRLPINPSGGLIGG 350
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 489124112 347 GHPIGASGCRILVSLVHEMVKR------RAHKGLATLCIGG 381
Cdd:PRK06289 351 GHPVGASGVRMLLDAAKQVTGTagdyqvEGAKTFGTLNIGG 391
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
81-114 |
1.31e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 41.01 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|....
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:COG3321 167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGG 200
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
251-354 |
3.47e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 39.26 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124112 251 DGAAAVMMMSEAKAQELNLPVLARIRAF-----ASVGVDPALMGIAPVYATRRCLERVGWQLADVDLIEA-------NEA 318
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAhgtatrlNDQ 289
|
90 100 110
....*....|....*....|....*....|....*.
gi 489124112 319 FAAQALSvgkmlEWDERRVNVNGGAIALGHPIGASG 354
Cdd:PRK05952 290 REANLIQ-----ALFPHRVAVSSTKGATGHTLGASG 320
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
81-116 |
5.88e-03 |
|
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: 38.67 E-value: 5.88e-03
10 20 30
....*....|....*....|....*....|....*.
gi 489124112 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQE 116
Cdd:cd00834 154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| |
