|
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: 683.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVS 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 161 AENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVM-TQSNGQTLVVDTDEQPRTDASAEGLARLNPSFDSLG 239
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTiKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 240 SVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAF 319
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446578684 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIERD 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: 597.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVS 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLgNSQLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 161 AENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLVVDTDEQPRTDASAEGLARLNPSFDSLGS 240
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 241 VTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAFA 320
Cdd:COG0183 240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446578684 321 AQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 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: 588.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVS 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 161 AENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMT-QSNGQTLVVDTDEQPRTDASAEGLARLNPSFDSLG 239
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIpQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 240 SVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAF 319
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446578684 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIERD 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: 585.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 5 VIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVSAITI 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 85 NDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLvDSLVHDGLWDAFNDYHIGVTAENL 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 165 AREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLVVDTDEQPRTDASAEGLARLNPSFDSLGSVTAG 244
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 245 NASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAFAAQAL 324
Cdd:cd00751 240 NASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQAL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446578684 325 SVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 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 |
3.65e-175 |
|
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: 493.28 E-value: 3.65e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 6 IVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVSAITIN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 86 DVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDS-RTGAQLGNSQLVDSLVHDgLWDAFNDYHIGVTAENL 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 165 AREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLVVDTDEQPRTDASAEGLARLNPSFDSLGSVTAG 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 245 NASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAFAAQAL 324
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446578684 325 SVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIE 390
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-390 |
6.24e-155 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 442.23 E-value: 6.24e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVS 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 161 AENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPV-MTQSNGQTLVVDTDEQPRTDASAEGLARLNPSFDSLG 239
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVtIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 240 SVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAF 319
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446578684 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIE 390
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-391 |
2.91e-153 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 437.85 E-value: 2.91e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVL-TAGAGQNPARQSAIKGGLPNSV 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpTEPRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVhDGLWDAFNDYHIGV 159
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMV-GALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 160 TAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLVVDTDEQPRTDASAEGLARLNPSF-DSL 238
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFkKEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 239 GSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEA 318
Cdd:PRK09051 241 GTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446578684 319 FAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 391
Cdd:PRK09051 321 FAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-391 |
1.55e-145 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 418.34 E-value: 1.55e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 2 KDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVSA 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 82 ITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHIGVTA 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 162 ENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNG--QTLVVDTDEQPrTDASAEGLARLNPSFDS-L 238
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRgrPSVIVDKDEGL-GKFDPAKLRKLRPSFKEdG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 239 GSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEA 318
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446578684 319 FAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 391
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-390 |
5.58e-144 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 414.43 E-value: 5.58e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVS 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVlTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHG-SYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 161 AENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLVVDTDEQPRTDASAEGLARLNPSFDSLGS 240
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDKNGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 241 VTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAFA 320
Cdd:PRK06633 241 VTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 321 AQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06633 321 AQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-391 |
4.82e-143 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 412.46 E-value: 4.82e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQvlTAGAGQNPA--RQSAIKGGLPNS 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLvdslvHDGLWDA---FNDY 155
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQL-----HDRLARGretAGGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 156 HIGV------TAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPV-MTQSNGQTLVVDTDEQPRTDASAEGL 228
Cdd:PRK06205 154 RFPVpggmieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVtVPQRKGDPTVVDRDEHPRADTTLESL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 229 ARLNP---SFDSLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGW 305
Cdd:PRK06205 234 AKLRPimgKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 306 QLAEVDLIEANEAFAAQALSVGKMLEW---DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGG 382
Cdd:PRK06205 314 TLDDIDLIELNEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGG 393
|
....*....
gi 446578684 383 QGVALTIER 391
Cdd:PRK06205 394 QGLAAVFER 402
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-391 |
1.02e-134 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 391.24 E-value: 1.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERT-GVPAYAVDEVILGQVLTAGA-GQNPARQSAIKGGLPNS 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSrTGAQLGNSQLVDSLVHdglWDAFN---DY 155
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKA-DSAFSRQAEIFDTTIG---WRFVNplmKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 156 HIGV-----TAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPV-MTQSNGQTLVVDTDEQPRTDASAEGLA 229
Cdd:PRK09050 157 QYGVdsmpeTAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVtIPQKKGDPVVVDRDEHPRPETTLEALA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 230 RLNPSFDSLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAE 309
Cdd:PRK09050 237 KLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 310 VDLIEANEAFAAQALSVGKMLEW--DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVAL 387
Cdd:PRK09050 317 FDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIAL 396
|
....
gi 446578684 388 TIER 391
Cdd:PRK09050 397 AIER 400
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-262 |
1.35e-124 |
|
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: 360.08 E-value: 1.35e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 4 VVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVSAIT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVL-TDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHIGVTAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 163 NLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLVVDTDEQPRTDASAEGLARLNPSFDSLGSVT 242
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
|
250 260
....*....|....*....|
gi 446578684 243 AGNASSINDGAAAVMMMSEA 262
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-391 |
8.79e-121 |
|
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: 355.63 E-value: 8.79e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 2 KDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERT-GVPAYAVDEVILGQVLTAGA-GQNPARQSAIKGGLPNSV 79
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRT----GAQLGNSQLVDSLVHDGLWDAFNDY 155
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSafsrSAKIEDTTIGWRFINPLMKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 156 HIGVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPV-MTQSNGQTLVVDTDEQPRTDASAEGLARLNPS 234
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVvIPQKKGEPTVVDQDEHPRPETTLEGLAKLKPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 235 FDSLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIE 314
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446578684 315 ANEAFAAQALSVGKMLEW--DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 391
Cdd:TIGR02430 321 LNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-391 |
2.72e-117 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 346.18 E-value: 2.72e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPI-----GCFRGAlaghSAVELGSLVVKALIERT-GVPAYAVDEVILGQVL-TAGAGQNPARQSAIKG 73
Cdd:PRK08947 1 MEDVVIVDAIRTPMgrskgGAFRNV----RAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQqTLEQGFNIARNAALLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 74 GLPNSVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSrapHVltdsrtgaqlGNSQLVDSLVHDGLWDAFN 153
Cdd:PRK08947 77 GIPHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMG---HV----------PMNHGVDFHPGLSKNVAKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 154 DYHIGVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQ-SNGQTLVVDTDEQPRTDASAEGLARLN 232
Cdd:PRK08947 144 AGMMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHdADGVLKLFDYDEVIRPETTVEALAALR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 233 PSFDSL-GSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVD 311
Cdd:PRK08947 224 PAFDPVnGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDID 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 312 LIEANEAFAAQALSVGK---MLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALT 388
Cdd:PRK08947 304 VFELNEAFAAQSLPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATV 383
|
...
gi 446578684 389 IER 391
Cdd:PRK08947 384 FER 386
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
4-390 |
4.16e-115 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 341.10 E-value: 4.16e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 4 VVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVSAIT 83
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYH-IGVTAE 162
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 163 NLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLVVDTDEQPRTdASAEGLARLNPSFDSLGSVT 242
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAFSKTGTVT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 243 AGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAFAAQ 322
Cdd:PRK06954 248 AANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVV 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446578684 323 ALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06954 328 TMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.06e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 339.80 E-value: 1.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIG-CFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVL-TAGAGQNPARQSAIKGGLPNS 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP---HVLTDsrtgaqlgNSQLVDSLvhdglwdafNDY 155
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPmmgHVVRP--------NPRLVEAA---------PEY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 156 HIGV--TAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPV-MTQ----SNGQ----TLVVDTDEQPRTDAS 224
Cdd:PRK07661 144 YMGMghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVdVTLrtvgENNKlqeeTITFSQDEGVRADTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 225 AEGLARLNPSFDSLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVG 304
Cdd:PRK07661 224 LEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 305 WQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQG 384
Cdd:PRK07661 304 LELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMG 383
|
....*..
gi 446578684 385 VALTIER 391
Cdd:PRK07661 384 AAGVFEL 390
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-390 |
1.26e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 334.67 E-value: 1.26e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVS 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVL-TDSRTGAQ---LGNSQLVDSLVHDGLWDAFNDYH 156
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPKhllHKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 157 IGVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTqsngqtlvVDTDEQPRTdASAEGLARLNPSFD 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND--------LDRDEGIRK-TTMEDLAKLPPAFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 237 SLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEAN 316
Cdd:PRK06366 232 KNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446578684 317 EAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06366 312 EAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-391 |
4.70e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 328.22 E-value: 4.70e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFR------GALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLtaGAGQN---PARQSAI 71
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRpkdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENwlyGGRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 72 KGGLPNSVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP-----HV------LTDSRtgaqlgnsqlv 140
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPmgdnpHIepnpklLTDPK----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 141 dsLVHdglWDAFNDYHIGVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLVVDTDEQPR 220
Cdd:PRK06445 148 --YIE---YDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 221 TDASAEGLARLNPSFDSLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCL 300
Cdd:PRK06445 223 PDTSLEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 301 ERVGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIG 380
Cdd:PRK06445 303 EKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVG 382
|
410
....*....|.
gi 446578684 381 GGQGVALTIER 391
Cdd:PRK06445 383 GGQGGAVVLER 393
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-392 |
6.51e-110 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 329.80 E-value: 6.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 3 DVVIVGALRTPIgCF--RGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQ-NPARQSAIKGGLPNSV 79
Cdd:PLN02287 47 DVVIVAAYRTPI-CKakRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHdglwdafndyhIGV 159
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP-----------MGI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 160 TAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQ------SNGQTLVVDTDEQPRTDASAEGLARLNP 233
Cdd:PLN02287 195 TSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKivdpktGEEKPIVISVDDGIRPNTTLADLAKLKP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 234 SFDSLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLI 313
Cdd:PLN02287 275 VFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 314 EANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRN--ARKGLATLCIGGGQGVALTIER 391
Cdd:PLN02287 355 EINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFER 434
|
.
gi 446578684 392 D 392
Cdd:PLN02287 435 G 435
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.87e-109 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 326.46 E-value: 2.87e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFR--GALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAG-AGQNPARQSAIKGGLPN 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 78 SVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvltdsrTGAQlGNSQLVDSLVhdglwdAFNDYHI 157
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP-------MGSD-GGAWAMDPST------NFPTYFV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 158 --GVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQsNGQTlVVDTDEQPRTDASAEGLARLNPSF 235
Cdd:PRK08242 147 pqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQ-NGLT-ILDHDEHMRPGTTMESLAKLKPSF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 236 DSLGSV---------------------TAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVY 294
Cdd:PRK08242 225 AMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 295 ATRRCLERVGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGL 374
Cdd:PRK08242 305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTAL 384
|
410
....*....|....*..
gi 446578684 375 ATLCIGGGQGVALTIER 391
Cdd:PRK08242 385 ITLCVGGGMGIATIIER 401
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-391 |
1.69e-108 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 324.26 E-value: 1.69e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIG-CFRGALAGHSAVELGSLVVKALIERT-GVPAYAVDEVILGQVL-TAGAGQNPARQSAIKGGLPN 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 78 SVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvltdsrtgaQLGNSQLVDSLVHDGLWDAFNDYHI 157
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP----------MMGNKPSMSPAIFARDENVGIAYGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 158 GVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNG----------QTLVVDTDEQPRTDASAEG 227
Cdd:PRK09052 155 GLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatgevdvKTRTVDLDEGPRADTSLEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 228 LARLNPSFDSLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQL 307
Cdd:PRK09052 235 LAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 308 AEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVAL 387
Cdd:PRK09052 315 DDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAG 394
|
....
gi 446578684 388 TIER 391
Cdd:PRK09052 395 IFER 398
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-391 |
1.42e-107 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 322.11 E-value: 1.42e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGA-GQNPARQSAIKGGLPNSV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLT-------------DSRTGAQLGNSQLVDSLVHD 146
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGkaesafsrdakvfDTTIGARFPNPKIVAQYGND 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 147 GLWDafndyhigvTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQT--LVVDTDEQPRTDAS 224
Cdd:PRK08131 161 SMPE---------TGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLppKLVAEDEHPRPSST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 225 AEGLARLNPSFDSlGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVG 304
Cdd:PRK08131 232 VEALTKLKPLFEG-GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 305 WQLAEVDLIEANEAFAAQALSVGKML--EWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGG 382
Cdd:PRK08131 311 LTLDDMDIIEINEAFASQVLGCLKGLgvDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVG 390
|
....*....
gi 446578684 383 QGVALTIER 391
Cdd:PRK08131 391 QGLAMVIER 399
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.10e-104 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 313.18 E-value: 2.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAG--AGqNPARQSAIKGGLPNS 78
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpqAG-NIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvLTDSRT-GAQLGnsqLVDSLVHDGLWDA-FNDYH 156
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTaGEQLG---FTSPFAESKGWLHrYGDQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 157 IG--VTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVmtqsNGqtlvVDTDEQPRtDASAEGLARLNPS 234
Cdd:PRK07801 155 VSqfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV----GG----VTVDEGPR-ETSLEKMAGLKPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 235 FDSlGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIE 314
Cdd:PRK07801 226 VEG-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVE 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446578684 315 ANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 391
Cdd:PRK07801 305 INEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-391 |
6.51e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 307.70 E-value: 6.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIG-CFRGALAGHSAVELGSLVVKALIERtgVPAYA---VDEVILGQVLTAG-AGQNPARQSAIKGGL 75
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDK--VPALDptdIDDLMLGCGLPGGeQGFNMARVVAVLLGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 76 PNsVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDS--------------RTG--AQLGNSQL 139
Cdd:PRK07851 79 DF-LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSlpdtknplfaeaqaRTAarAEGGAEAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 140 VDSLVHDGLWDAFndYHIGVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVmTQSNGQtlVVDTDEQP 219
Cdd:PRK07851 158 HDPREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPV-TLPDGT--VVSTDDGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 220 RTDASAEGLARLNPSFDSLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRC 299
Cdd:PRK07851 233 RAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 300 LERVGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCI 379
Cdd:PRK07851 313 LARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCV 392
|
410
....*....|..
gi 446578684 380 GGGQGVALTIER 391
Cdd:PRK07851 393 GGGQGMAMVLER 404
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-391 |
4.61e-101 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 304.72 E-value: 4.61e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGA-GQNPARQSAIKGGLPNSV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvlTDSRTGAQLGNSQlvdslVHDGLWDAFNDYhigV 159
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP---LGANAGPGRGLPR-----PDSWDIDMPNQF---E 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 160 TAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMT-------QSNGQTLVVDTDEQPRtDASAEGLARLN 232
Cdd:PRK07850 150 AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQApvldeegQPTGETRLVTRDQGLR-DTTMEGLAGLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 233 PSFDSlGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDL 312
Cdd:PRK07850 229 PVLEG-GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446578684 313 IEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 391
Cdd:PRK07850 308 VEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-391 |
2.02e-100 |
|
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: 303.02 E-value: 2.02e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 3 DVVIVGALRTPIGCFRGALAGHSAVE-LGSLVVKALIER-TGVPAYAVDEVILGQV-LTAGAGQNPARQSAIKGGLPNSV 79
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTRAEdLSAHLMSKLLARnPKVDPAEVEDIYWGCVqQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvltdsrtgaqlgnSQLVDSLVHDGLWDAFNDYHIGV 159
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPM-------------MHGVDFHPGMSLHVAKAAGMMGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 160 TAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQ-SNGQTLVVDTDEQPRTDASAEGLARLNPSFDSL 238
Cdd:TIGR02445 148 TAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHdADGFLKQFDYDEVIRPETTVESLAALRPAFDPK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 239 -GSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANE 317
Cdd:TIGR02445 228 nGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446578684 318 AFAAQALSVGK---MLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 391
Cdd:TIGR02445 308 AFAAQALPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.86e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 294.23 E-value: 1.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVS 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDS--RTGAQLGNSQ-LVDSLVH------------ 145
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKmvRWLAGWYAAKsIGQKLAAlgklrpsylapv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 146 ----DGLWDAFNDYHIGVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKdEIVPVMTqSNGQtlVVDTDEQPRT 221
Cdd:PRK08170 162 igllRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFD-RDGK--FYDHDDGVRP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 222 DASAEGLARLNPSFDS-LGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCL 300
Cdd:PRK08170 238 DSSMEKLAKLKPFFDRpYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 301 ERVGWQLAEVDLIEANEAFAAQALSV-----------------GKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVH 363
Cdd:PRK08170 318 QRHGLTLEDLDLWEINEAFAAQVLAClaawadeeycreqlgldGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLH 397
|
410 420
....*....|....*....|....*...
gi 446578684 364 EMVKRNARKGLATLCIGGGQGVALTIER 391
Cdd:PRK08170 398 ALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.83e-93 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 285.08 E-value: 2.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAG-AGQNPARQSAIKGGLPNSV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTdsrtgAQLGNSQLVDSLVHDGLWDAFNDYHIG- 158
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP-----STLPAKNGLGHYKSPGMEERYPGIQFSq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 159 -VTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPV-MTQSNGQTLVVDTDEQPRTDASAEGLARLNPSFD 236
Cdd:PRK06504 156 fTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLeITRADGSGEMHTVDEGIRFDATLEGIAGVKLIAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 237 SlGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEAN 316
Cdd:PRK06504 236 G-GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVN 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446578684 317 EAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 391
Cdd:PRK06504 315 EAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-392 |
9.95e-91 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 279.56 E-value: 9.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 4 VVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVSAIT 83
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP--------HVLTDSRTGAQLGnsQLVDSLVHDGLWD----- 150
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaRALVDLNKARTLG--QRLKLFSRLRLRDllpvp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 151 -AFNDYHIGV----TAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLvvDTDEQPRTDASA 225
Cdd:PRK08963 165 pAVAEYSTGLrmgdTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPL--EEDNNIRGDSTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 226 EGLARLNPSFD-SLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDP---ALMGiaPVYATRRCLE 301
Cdd:PRK08963 243 EDYAKLRPAFDrKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwqdMLLG--PAYATPLALE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 302 RVGWQLAEVDLIEANEAFAAQALSVGKML-----------------EWDERRVNVNGGAIALGHPIGASGCRILVSLVHE 364
Cdd:PRK08963 321 RAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHE 400
|
410 420
....*....|....*....|....*...
gi 446578684 365 MVKRNARKGLATLCIGGGQGVALTIERD 392
Cdd:PRK08963 401 LRRRGGGLGLTTACAAGGLGAAMVLEVE 428
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-386 |
1.29e-88 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 273.18 E-value: 1.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIG-CFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGA-GQNPARQSAIKGGLPNS 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP-----HVLTDSrtgaqlgnsqlvdslvhdglWDAFN 153
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQnemnrHMLREG--------------------WLVEH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 154 DYHIGV----TAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVP----------VMTQSNGQTLVVDTDEQP 219
Cdd:PRK07108 141 KPEIYWsmlqTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPitvtagvadkATGRLFTKEVTVSADEGI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 220 RTDASAEGLARLNPSFDSlGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRC 299
Cdd:PRK07108 221 RPDTTLEGVSKIRSALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 300 LERVGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCI 379
Cdd:PRK07108 300 LKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCI 379
|
....*..
gi 446578684 380 GGGQGVA 386
Cdd:PRK07108 380 GGGQGAA 386
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-390 |
1.85e-85 |
|
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: 265.13 E-value: 1.85e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 7 VGALRTPIGCF---RGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVSAIT 83
Cdd:cd00826 1 AGAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSraphvlTDSRTGAQlgnsqlvdslvhdglwdafnDYHIGVtaen 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME------TSAENNAK--------------------EKHIDV---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 164 LAREYGiSRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLVVDTDE--QPRTDASAEGLARLNPSFDSLGSV 241
Cdd:cd00826 131 LINKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEyiQFGDEASLDEIAKLRPAFDKEDFL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 242 TAGNASSINDGAAAVMMMSEAKA-------RALNLPVLARIRAFASVGVDPA----LMGIAPVYATRRCLERVGWQLAEV 310
Cdd:cd00826 210 TAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 311 DLIEANEAFAAQALSVGKMLEWDERR------------------VNVNGGAIALGHPIGASGCRILVSLVHEMVKRN--- 369
Cdd:cd00826 290 DLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAgkr 369
|
410 420
....*....|....*....|...
gi 446578684 370 --ARKGLATLCIGGGQGVALTIE 390
Cdd:cd00826 370 qgAGAGLALLCIGGGGGAAMCIE 392
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
5-390 |
3.24e-80 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 250.45 E-value: 3.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 5 VIVGALRTPIGCFRGALAGHSAVELGSLVVKAL---IERtgvpayAVDEVILGQVLtaGAGQNPARQSAIKGGLPNSVSA 81
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFLskgMER------EIDDVILGNVV--GPGGNVARLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 82 ITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvltdsRTGAQLGNsqlvdslvhdglwDAFNDYHIGVTA 161
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF-----QNRARFSP-------------ETIGDPDMGVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 162 ENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVmtqsNGQTlvvdtDEQPRTDASAEGL-ARLNPSFDSLGS 240
Cdd:PRK06690 138 EYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF----NGLL-----DESIKKEMNYERIiKRTKPAFLHNGT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 241 VTAGNASSINDGAAAVMMMSEAKARALNL-PVLARIRAfASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAF 319
Cdd:PRK06690 209 VTAGNSCGVNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAF 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446578684 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06690 288 ASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.51e-79 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 250.08 E-value: 2.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIG---CFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGA-GQNPARQSAIKGGLP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 77 NSVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvlTDSRTGAQLGNSQLVDSlVHDGLWDAFNDYH 156
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAA--MAAEDMAAGKPPLGMGS-GNLRLRALHPQSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 157 IGVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNgqTLVVDTDEQPRTDASAEGLARLNPSFD 236
Cdd:PRK06025 158 QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDG--SVALDHEEFPRPQTTAEGLAALKPAFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 237 SLGSVT--------------------------AGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGI 290
Cdd:PRK06025 236 AIADYPlddkgttyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 291 APVYATRRCLERVGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNA 370
Cdd:PRK06025 316 APVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGL 395
|
410 420
....*....|....*....|.
gi 446578684 371 RKGLATLCIGGGQGVALTIER 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 |
4.35e-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: 205.95 E-value: 4.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 269 LPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGH 348
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446578684 349 PIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 391
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.77e-58 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 195.50 E-value: 2.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVS 80
Cdd:PRK09268 6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDS------------------RTGAQLGNSQLVDS 142
Cdd:PRK09268 86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGlrkillelnrakttgdrlKALGKLRPKHLAPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 143 LVHD-----GLwdafndyHIGVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVmtqsngqtLVVDTDE 217
Cdd:PRK09268 166 IPRNgeprtGL-------SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF--------LGLTRDN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 218 QPRTDASAEGLARLNPSFD--SLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAF--ASV----GVDPALMg 289
Cdd:PRK09268 231 NLRPDSSLEKLAKLKPVFGkgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetAAVdfvhGKEGLLM- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 290 iAPVYATRRCLERVGWQLAEVDLIEANEAFAAQALSVGKMLEWDE-----------------RRVNVNGGAIALGHPIGA 352
Cdd:PRK09268 310 -APAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEycrerlgldaplgsidrSKLNVNGSSLAAGHPFAA 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 446578684 353 SGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIER 391
Cdd:PRK09268 389 TGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
22-389 |
1.05e-23 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 98.67 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 22 AGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPnSVSAITINDVCGSGLKALHLATQA 101
Cdd:cd00327 3 LGITASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 102 IQCGEADIVIAGGqenmsraphvltdsrtgaqlgnsqlvdslvhdglwdafndyhigvtaenlareygisrqlqdayals 181
Cdd:cd00327 82 VQNGKADIVLAGG------------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 182 sqqkaraaidagrfkdeivpvmtqsngqtlvvdtdeqprtdasaeglarlnpsfdslgsvtaGNASSINDGAAAVMMMSE 261
Cdd:cd00327 95 --------------------------------------------------------------SEEFVFGDGAAAAVVESE 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 262 AKARALNLPVLARIRAFASVGVD----PALMGIAPVYATRRCLERVGWQLAEVDLIEANEAFAAQALSVGKMLEWDE--- 334
Cdd:cd00327 113 EHALRRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPdgv 192
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446578684 335 RRVNVNGGAIALGHPIGASGCRILVSLVHEM-------VKRNARKGLATLCIGGGQGVALTI 389
Cdd:cd00327 193 RSPAVSATLIMTGHPLGAAGLAILDELLLMLehefippTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-373 |
6.65e-14 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 72.62 E-value: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGcfrgalaGHSAVELGSLVVKAL---IERTGVPAYAVDEVILGQVLTAG-AGQ-NPARQSAIKGGL 75
Cdd:PRK06064 1 MRDVAIIGVGQTKFG-------ELWDVSLRDLAVEAGleaLEDAGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYAGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 76 PNsVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLgnsqlvdslvhDGLWDAFNdy 155
Cdd:PRK06064 74 AP-IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAG-----------DYEWEEFF-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 156 hiGVTAENL----AREYgisrqlQDAYALSSQQKARAAIDA---------GRFKDEIvpvmtqsngqTLvvdtDEQPRTD 222
Cdd:PRK06064 140 --GATFPGLyaliARRY------MHKYGTTEEDLALVAVKNhyngsknpyAQFQKEI----------TV----EQVLNSP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 223 ASAEGLaRLnpsFDSlgsvtagnaSSINDGAAAVMMMSEAKARAL-NLPVlaRIRAFASVGVDPAL------MGI-APVY 294
Cdd:PRK06064 198 PVADPL-KL---LDC---------SPITDGAAAVILASEEKAKEYtDTPV--WIKASGQASDTIALhdrkdfTTLdAAVV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 295 ATRRCLERVGWQLAEVDLIEANEAFA-AQALSV-----------GKMLEWDERR------VNVNGGAIALGHPIGASGCR 356
Cdd:PRK06064 263 AAEKAYKMAGIEPKDIDVAEVHDCFTiAEILAYedlgfakkgegGKLAREGQTYiggdipVNPSGGLKAKGHPVGATGVS 342
|
410
....*....|....*..
gi 446578684 357 ILVSLVHEMvKRNARKG 373
Cdd:PRK06064 343 QAVEIVWQL-RGEAEKG 358
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
25-389 |
7.00e-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: 72.30 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 25 SAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNsVSAITINDVCGSGLKALHLATQAIQC 104
Cdd:cd00829 15 SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 105 GEADIVIAGGQENMSRAPhvlTDSRTGAQLGNSQLVDSLVHDGLwdAFNDYHIGVTAENLAReYGISRqlqDAYALSSQQ 184
Cdd:cd00829 94 GLADVVLVVGAEKMSDVP---TGDEAGGRASDLEWEGPEPPGGL--TPPALYALAARRYMHR-YGTTR---EDLAKVAVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 185 KARAAIDAGR--FKDEIvpVMTQSNGQTLVVDtdeqPrtdasaeglarlnpsfdslgsVTAGNASSINDGAAAVMMMSEA 262
Cdd:cd00829 165 NHRNAARNPYaqFRKPI--TVEDVLNSRMIAD----P---------------------LRLLDCCPVSDGAAAVVLASEE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 263 KARALNLPvLARIRAFAsVGVDPALMG--------IAPVYATRRCLERVGWQLAEVDLIE------ANEAFAAQAL---- 324
Cdd:cd00829 218 RARELTDR-PVWILGVG-AASDTPSLSerddflslDAARLAARRAYKMAGITPDDIDVAElydcftIAELLALEDLgfce 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 325 --SVGKMLEWDERR------VNVNGGAIALGHPIGASGcrilVSLVHEMVK-----------RNARKGLATLCIGGGQGV 385
Cdd:cd00829 296 kgEGGKLVREGDTAiggdlpVNTSGGLLSKGHPLGATG----LAQAVEAVRqlrgeagarqvPGARVGLAHNIGGTGSAA 371
|
....
gi 446578684 386 ALTI 389
Cdd:cd00829 372 VVTI 375
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-354 |
4.24e-11 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 63.81 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 1 MKDVVIVGALRTPIGcfrgalaGHSAVELGSLVVKAL---IERTGVPAYAVDEVILGQvLTAGAGQNPARQSAIKGGLPN 77
Cdd:PRK07516 1 MMTASIVGWAHTPFG-------KLDAETLESLIVRVAreaLAHAGIAAGDVDGIFLGH-FNAGFSPQDFPASLVLQADPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 78 --SVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvltdsrtGAQLGNSQLVDSLVHDGlwdafndy 155
Cdd:PRK07516 73 lrFKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP--------TAEVGDILLGASYLKEE-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 156 hiGVTAENLAREYG-ISRQLQDAYAlsSQQKARAAIDAgrfkdeivpvmtqSNGQTLVVDTDEQPRTDASAEGLARL--- 231
Cdd:PRK07516 137 --GDTPGGFAGVFGrIAQAYFQRYG--DQSDALAMIAA-------------KNHANGVANPYAQMRKDLGFEFCRTVsek 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 232 NPsfdslgsVTAG-----NASSINDGAAAVMMMSEAKARALNLPVlaRIRAFASVG-------VDPALMGiAPVYATRRC 299
Cdd:PRK07516 200 NP-------LVAGplrrtDCSLVSDGAAALVLADAETARALQRAV--RFRARAHVNdflplsrRDPLAFE-GPRRAWQRA 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446578684 300 LERVGWQLAEVDLIEANEAF------------------AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASG 354
Cdd:PRK07516 270 LAQAGVTLDDLSFVETHDCFtiaelieyeamglappgqGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATG 342
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
28-368 |
1.57e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 56.01 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 28 ELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPA----RQSAIKGGLPNSVSAitindVCGSGLKALHLATQAIQ 103
Cdd:PRK12578 23 ELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPApivaEYSGLTGKVPLRVEA-----MCATGLAASLTAYTAVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 104 CGEADIVIAGGQENMSRaphvlTDSRT----GAQLGNSQlvdslvhdglWDaFNDYhiGVTAENLAREYGiSRQLQdAYA 179
Cdd:PRK12578 98 SGLVDMAIAVGVDKMTE-----VDTSTslaiGGRGGNYQ----------WE-YHFY--GTTFPTYYALYA-TRHMA-VYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 180 LSSQQKARAAIDAGRFKdeivpvmtqsngqtlVVDTDEQPRTDASAEglarlnpsfDSLGS------VTAGNASSINDGA 253
Cdd:PRK12578 158 TTEEQMALVSVKAHKYG---------------AMNPKAHFQKPVTVE---------EVLKSraiswpIKLLDSCPISDGS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 254 AAVMMMSEAKARALNL-----------------------------PVLARIRAFASVGVDPALMGIAPVYATRRCLERVG 304
Cdd:PRK12578 214 ATAIFASEEKVKELKIdspvwitgigyandyayvarrgewvgfkaTQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMG 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446578684 305 WQlaevDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGcrilVSLVHEMVKR 368
Cdd:PRK12578 294 YE----DLGFTEKGKGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATG----LSMIYEITKQ 349
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
81-114 |
3.21e-05 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 44.93 E-value: 3.21e-05
10 20 30
....*....|....*....|....*....|....
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:pfam00109 166 SVTVDTACSSSLVAIHAAVQSIRSGEADVALAGG 199
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
75-114 |
4.04e-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: 4.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446578684 75 LPNSVS--------AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:cd00833 149 LANRISyffdlrgpSLTVDTACSSSLVALHLACQSLRSGECDLALVGG 196
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
61-114 |
1.97e-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: 42.70 E-value: 1.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446578684 61 AGQNPAR-QSAIKG---GLPNSVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:smart00825 66 AGIDPESlRGSRTGvfvGVSSSDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
176-354 |
3.21e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 42.37 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 176 DAYALSSQQkARAAIDAGRFKDE-IVPVMTQSngqtlvvdtdeqpRTDASAEGLARLNPSFDSLGS-------VTAGNAS 247
Cdd:PRK07937 137 DSVSMAGLQ-ARAGLDAGKWTEEqMAEVAARS-------------RADARRNPSAEPSISVDELLArpyfadpLRRHDIA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 248 SINDGAAAVMMMSEAKARALnLPVLARIRAFASvGVDPALMG---IAPVYATRRCLERV-GWQLAEVDLIEANEAFAAQA 323
Cdd:PRK07937 203 PITDGAAAVVLAAGDRAREL-RERPAWITGIEH-RIESPSLGardLTRSPSTALAAEAAtGGDAGGVDVAELHAPFTHQE 280
|
170 180 190
....*....|....*....|....*....|..
gi 446578684 324 LSVGKMLEWDER-RVNVNGGAIAlGHPIGASG 354
Cdd:PRK07937 281 LILREALGLGDKtKVNPSGGALA-ANPMFAAG 311
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
82-119 |
6.97e-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: 6.97e-04
10 20 30
....*....|....*....|....*....|....*...
gi 446578684 82 ITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMS 119
Cdd:cd00828 156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
247-381 |
7.48e-04 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 41.21 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 247 SSINDGAAAVMMMSEAKARAL-NLPVLARIRAFasvGVDPALMGIAPVYA-----------TRRCLE----RVGWQLAEV 310
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDYaDARPIPRIKGW---GHRTAPLGLEQKLDrsagdpyvlphVRQAVLdayrRAGVGLDDL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578684 311 DLIEANEAFAA------------------QALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKR---- 368
Cdd:PRK06289 297 DGFEVHDCFTPseylaidhigltgpgeswKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTagdy 376
|
170
....*....|....*.
gi 446578684 369 ---NARKGLaTLCIGG 381
Cdd:PRK06289 377 qveGAKTFG-TLNIGG 391
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
81-114 |
1.26e-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: 1.26e-03
10 20 30
....*....|....*....|....*....|....
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:COG3321 167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGG 200
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
82-120 |
6.21e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 38.34 E-value: 6.21e-03
10 20 30
....*....|....*....|....*....|....*....
gi 446578684 82 ITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSR 120
Cdd:PRK08256 74 VNVNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQP 112
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
81-116 |
6.56e-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: 38.29 E-value: 6.56e-03
10 20 30
....*....|....*....|....*....|....*.
gi 446578684 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQE 116
Cdd:cd00834 154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| |
