|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-391 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 684.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVS 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLIDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 161 AENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVT-SELNGTPRLVDTDEQPRVDPSAEALASLLPTFDQQG 239
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTiKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 240 SVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEAF 319
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503992696 320 AAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
|
| 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: 607.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVS 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLgNSQLIDSLVHDGLWDAFNDYHMGVT 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 161 AENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTPRLVDTDEQPRVDPSAEALASLLPTFDQQGS 240
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 241 VTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEAFA 320
Cdd:COG0183 240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503992696 321 AQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:COG0183 320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-391 |
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 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVS 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLIDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 161 AENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVT-SELNGTPRLVDTDEQPRVDPSAEALASLLPTFDQQG 239
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILiPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 240 SVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEAF 319
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503992696 320 AAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| 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: 590.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 5 VIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVSAITI 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 85 NDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLiDSLVHDGLWDAFNDYHMGVTAENL 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 165 AREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTPRLVDTDEQPRVDPSAEALASLLPTFDQQGSVTAG 244
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 245 NASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEAFAAQAI 324
Cdd:cd00751 240 NASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQAL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503992696 325 SVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 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 |
3.95e-178 |
|
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: 500.60 E-value: 3.95e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 6 IVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVSAITIN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 86 DVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDS-RTGAQLGNSQLIDSLVHDgLWDAFNDYHMGVTAENL 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 165 AREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTPRLVDTDEQPRVDPSAEALASLLPTFDQQGSVTAG 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 245 NASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEAFAAQAI 324
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503992696 325 SVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVE 390
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-391 |
1.84e-157 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 448.64 E-value: 1.84e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVL-TAGTGQNPARQSAIRGGLPNTV 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpTEPRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLIDSLVhDGLWDAFNDYHMGV 159
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMV-GALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 160 TAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTPRLVDTDEQPRVDPSAEALASLLPTFDQ-Q 238
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKeN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 239 GSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEA 318
Cdd:PRK09051 241 GTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503992696 319 FAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:PRK09051 321 FAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-390 |
6.54e-157 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 447.24 E-value: 6.54e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVS 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLIDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 161 AENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVT-SELNGTPRLVDTDEQPRVDPSAEALASLLPTFDQQG 239
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTiPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 240 SVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEAF 319
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503992696 320 AAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVE 390
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-391 |
3.39e-152 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 435.29 E-value: 3.39e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 2 KDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVSA 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 82 ITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLIDSLVHDGLWDAFNDYHMGVTA 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 162 ENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVT-SELNGTP-RLVDTDEQP-RVDPsaEALASLLPTFDQQ 238
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEvPGGRGRPsVIVDKDEGLgKFDP--AKLRKLRPSFKED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 239 -GSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANE 317
Cdd:PLN02644 239 gGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503992696 318 AFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:PLN02644 319 AFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-390 |
4.57e-150 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 429.84 E-value: 4.57e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVS 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVlTDSRTGAQLGNSQLIDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHG-SYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 161 AENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTPRLVDTDEQPRVDPSAEALASLLPTFDQQGS 240
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDKNGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 241 VTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEAFA 320
Cdd:PRK06633 241 VTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 321 AQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVE 390
Cdd:PRK06633 321 AQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.58e-145 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 418.24 E-value: 2.58e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQvlTAGTGQNPA--RQSAIRGGLPNT 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLIDSLVHdGLWDAFNDYH-- 156
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRLAR-GRETAGGRRFpv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 157 ---MGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVT-SELNGTPRLVDTDEQPRVDPSAEALASLL 232
Cdd:PRK06205 158 pggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTvPQRKGDPTVVDRDEHPRADTTLESLAKLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 233 P---TFDQQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDE 309
Cdd:PRK06205 238 PimgKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 310 VDLIEANEAFAAQAISVGRVLEW---DERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVA 386
Cdd:PRK06205 318 IDLIELNEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLA 397
|
....*
gi 503992696 387 LAVER 391
Cdd:PRK06205 398 AVFER 402
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-391 |
3.62e-139 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 402.41 E-value: 3.62e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVER-SGVDPQSIDEVILGQVLTAGT-GQNPARQSAIRGGLPNT 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSrTGAQLGNSQLIDS-----LVHDGLWDAFN 153
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKA-DSAFSRQAEIFDTtigwrFVNPLMKAQYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 154 DYHMGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVT-SELNGTPRLVDTDEQPRVDPSAEALASLL 232
Cdd:PRK09050 160 VDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTiPQKKGDPVVVDRDEHPRPETTLEALAKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 233 PTFDQQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDL 312
Cdd:PRK09050 240 PVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 313 IEANEAFAAQAISVGRVLEW--DERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVE 390
Cdd:PRK09050 320 IELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIE 399
|
.
gi 503992696 391 R 391
Cdd:PRK09050 400 R 400
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-391 |
2.95e-125 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 366.60 E-value: 2.95e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHS-AVELGSVVVKALVERS-GVDPQSIDEVILGQVL-TAGTGQNPARQSAIRGGLPN 77
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAFRNVrAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQqTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 78 TVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSrapHVLTD---------SRTGAQLGNSqlidslvhdgl 148
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMG---HVPMNhgvdfhpglSKNVAKAAGM----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 149 wdafndyhMGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTS-ELNGTPRLVDTDEQPRVDPSAEA 227
Cdd:PRK08947 147 --------MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGhDADGVLKLFDYDEVIRPETTVEA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 228 LASLLPTFD-QQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWK 306
Cdd:PRK08947 219 LAALRPAFDpVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 307 LDEVDLIEANEAFAAQAISVGRVLEWDER---RVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQ 383
Cdd:PRK08947 299 ISDIDVFELNEAFAAQSLPCLKDLGLLDKmdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQ 378
|
....*...
gi 503992696 384 GVALAVER 391
Cdd:PRK08947 379 GIATVFER 386
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-391 |
2.05e-123 |
|
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: 362.18 E-value: 2.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 2 KDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVER-SGVDPQSIDEVILGQVLTAGT-GQNPARQSAIRGGLPNTV 79
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRT----GAQLGNSQLIDSLVHDGLWDAFNDY 155
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSafsrSAKIEDTTIGWRFINPLMKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 156 HMGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVT-SELNGTPRLVDTDEQPRVDPSAEALASLLPT 234
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVViPQKKGEPTVVDQDEHPRPETTLEGLAKLKPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 235 FDQQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIE 314
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503992696 315 ANEAFAAQAISVGRVLEW--DERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:TIGR02430 321 LNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
4-390 |
1.17e-122 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 360.36 E-value: 1.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 4 VVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVSAIT 83
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLIDSLVHDGLWDAFNDYH-MGVTAE 162
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 163 NLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTPRLVDTDEQPRvDPSAEALASLLPTFDQQGSVT 242
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPF-KANPEKIPTLKPAFSKTGTVT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 243 AGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEAFAAQ 322
Cdd:PRK06954 248 AANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVV 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503992696 323 AISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVE 390
Cdd:PRK06954 328 TMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-390 |
1.30e-120 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 354.70 E-value: 1.30e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVS 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVL-TDSRTGAQ---LGNSQLIDSLVHDGLWDAFNDYH 156
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPKhllHKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 157 MGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSelngtprlVDTDEQPRvDPSAEALASLLPTFD 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND--------LDRDEGIR-KTTMEDLAKLPPAFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 237 QQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEAN 316
Cdd:PRK06366 232 KNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503992696 317 EAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVE 390
Cdd:PRK06366 312 EAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-262 |
2.53e-120 |
|
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: 349.29 E-value: 2.53e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 4 VVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVSAIT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVL-TDSRTGAQLGNSQLIDSLVHDGLWDAFNDYHMGVTAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 163 NLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTPRLVDTDEQPRVDPSAEALASLLPTFDQQGSVT 242
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
|
250 260
....*....|....*....|
gi 503992696 243 AGNASSINDGAAAVMMMSEA 262
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-386 |
2.43e-118 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 349.05 E-value: 2.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIG-CFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVL-TAGTGQNPARQSAIRGGLPNT 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAP---HVLTDsrtgaqlgNSQLIDSLvhdglwdafNDY 155
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPmmgHVVRP--------NPRLVEAA---------PEY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 156 HMGV--TAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSEL-----NGTPR----LVDTDEQPRVDPS 224
Cdd:PRK07661 144 YMGMghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLrtvgeNNKLQeetiTFSQDEGVRADTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 225 AEALASLLPTFDQQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAG 304
Cdd:PRK07661 224 LEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 305 WKLDEVDLIEANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQG 384
Cdd:PRK07661 304 LELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMG 383
|
..
gi 503992696 385 VA 386
Cdd:PRK07661 384 AA 385
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.53e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 339.39 E-value: 1.53e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPigcfqgaLSRHS-------------AVELGSVVVKALVERSGVDPQSIDEVILGQVLtaGTGQN--- 64
Cdd:PRK06445 1 LEDVYLVDFARTA-------FSRFRpkdpqkdvfnnirPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENwly 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 65 PARQSAIRGGLPNTVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltdsrtgaqLGNSQLIDslV 144
Cdd:PRK06445 72 GGRHPIFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP-----------MGDNPHIE--P 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 145 HDGL--------WDAFNDYHMGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTPRLVDTD 216
Cdd:PRK06445 139 NPKLltdpkyieYDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 217 EQPRVDPSAEALASLLPTFDQQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHAT 296
Cdd:PRK06445 219 QSVRPDTSLEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPAS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 297 RRCLERAGWKLDEVDLIEANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLAT 376
Cdd:PRK06445 299 KKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVAT 378
|
410
....*....|....*.
gi 503992696 377 LCIGGGQGVALAVERE 392
Cdd:PRK06445 379 LCVGGGQGGAVVLERV 394
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-391 |
1.61e-114 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 339.67 E-value: 1.61e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVE--LGSVVVKALVERSGVDPQSIDEVILGQVL-TAGTGQNPARQSAIRGGLPN 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGKAPRGMFKNTRPDdlLAHVLRSAVAQVPGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 78 TVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltdsrtgaQLGNSQLIDSLVHDGLWDAFNDYHM 157
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP----------MMGNKPSMSPAIFARDENVGIAYGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 158 GVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPV----------TSELNGTPRLVDTDEQPRVDPSAEA 227
Cdd:PRK09052 155 GLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYeiterfpdlaTGEVDVKTRTVDLDEGPRADTSLEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 228 LASLLPTFDQQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKL 307
Cdd:PRK09052 235 LAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 308 DEVDLIEANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVAL 387
Cdd:PRK09052 315 DDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAG 394
|
....
gi 503992696 388 AVER 391
Cdd:PRK09052 395 IFER 398
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-392 |
6.49e-112 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 334.81 E-value: 6.49e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 3 DVVIVGALRTPIgCF--QGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQ-NPARQSAIRGGLPNTV 79
Cdd:PLN02287 47 DVVIVAAYRTPI-CKakRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLIDSLVHdglwdafndyhMGV 159
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP-----------MGI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 160 TAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSEL------NGTPRLVDTDEQPRVDPSAEALASLLP 233
Cdd:PLN02287 195 TSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIvdpktgEEKPIVISVDDGIRPNTTLADLAKLKP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 234 TFDQQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLI 313
Cdd:PLN02287 275 VFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 314 EANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKR--DARKGLATLCIGGGQGVALAVER 391
Cdd:PLN02287 355 EINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRgkDCRFGVVSMCIGTGMGAAAVFER 434
|
.
gi 503992696 392 E 392
Cdd:PLN02287 435 G 435
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-391 |
7.99e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 333.12 E-value: 7.99e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIG-CFQGALSRHSAVELGSVVVKALVER-SGVDPQSIDEVILGQVLTAG-TGQNPARQSAIRGGLPn 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKvPALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 78 TVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDS--------------RTG--AQLGNSQLID 141
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSlpdtknplfaeaqaRTAarAEGGAEAWHD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 142 SLVHDGLWDAFndYHMGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSElNGTprLVDTDEQPRV 221
Cdd:PRK07851 160 PREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP-DGT--VVSTDDGPRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 222 DPSAEALASLLPTFDQQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLE 301
Cdd:PRK07851 235 GTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 302 RAGWKLDEVDLIEANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGG 381
Cdd:PRK07851 315 RAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGG 394
|
410
....*....|
gi 503992696 382 GQGVALAVER 391
Cdd:PRK07851 395 GQGMAMVLER 404
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-391 |
1.40e-107 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 322.11 E-value: 1.40e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGT-GQNPARQSAIRGGLPNTV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLT-------------DSRTGAQLGNSQLIDSlvhd 146
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGkaesafsrdakvfDTTIGARFPNPKIVAQ---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 147 glwdaFNDYHMGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNG--TPRLVDTDEQPRVDPS 224
Cdd:PRK08131 157 -----YGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRklPPKLVAEDEHPRPSST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 225 AEALASLLPTFDQqGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAG 304
Cdd:PRK08131 232 VEALTKLKPLFEG-GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 305 WKLDEVDLIEANEAFAAQAISVGRVL--EWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGG 382
Cdd:PRK08131 311 LTLDDMDIIEINEAFASQVLGCLKGLgvDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVG 390
|
....*....
gi 503992696 383 QGVALAVER 391
Cdd:PRK08131 391 QGLAMVIER 399
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-391 |
1.90e-106 |
|
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: 318.42 E-value: 1.90e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 3 DVVIVGALRTPIGCFQGALSRHSAVE-LGSVVVKALVER-SGVDPQSIDEVILGQV-LTAGTGQNPARQSAIRGGLPNTV 79
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTRAEdLSAHLMSKLLARnPKVDPAEVEDIYWGCVqQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHvltdsrtgaqlgnSQLIDSLVHDGLWDAFNDYHMGV 159
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPM-------------MHGVDFHPGMSLHVAKAAGMMGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 160 TAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTS-ELNGTPRLVDTDEQPRVDPSAEALASLLPTFD-Q 237
Cdd:TIGR02445 148 TAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGhDADGFLKQFDYDEVIRPETTVESLAALRPAFDpK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 238 QGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANE 317
Cdd:TIGR02445 228 NGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503992696 318 AFAAQAISVGR---VLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:TIGR02445 308 AFAAQALPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.95e-104 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 313.36 E-value: 2.95e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQ--GALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAG-TGQNPARQSAIRGGLPN 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 78 TVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvlTDSRTGAQLGNSQLidslvhdglwdAFNDYHM 157
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP---MGSDGGAWAMDPST-----------NFPTYFV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 158 --GVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTprLVDTDEQPRVDPSAEALASLLPTF 235
Cdd:PRK08242 147 pqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLT--ILDHDEHMRPGTTMESLAKLKPSF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 236 DQQGSV---------------------TAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVH 294
Cdd:PRK08242 225 AMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 295 ATRRCLERAGWKLDEVDLIEANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGL 374
Cdd:PRK08242 305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTAL 384
|
410
....*....|....*..
gi 503992696 375 ATLCIGGGQGVALAVER 391
Cdd:PRK08242 385 ITLCVGGGMGIATIIER 401
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-391 |
4.21e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 307.40 E-value: 4.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGtGQ--NPARQSAIRGGLPNT 78
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQagNIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvLTDSRT-GAQLGnsqLIDSLVHDGLWDA-FNDYH 156
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTaGEQLG---FTSPFAESKGWLHrYGDQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 157 MG--VTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSelngtprlVDTDEQPRvDPSAEALASLLPT 234
Cdd:PRK07801 155 VSqfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG--------VTVDEGPR-ETSLEKMAGLKPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 235 FDQqGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIE 314
Cdd:PRK07801 226 VEG-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVE 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503992696 315 ANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:PRK07801 305 INEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-391 |
1.17e-100 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 303.95 E-value: 1.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAG-TGQNPARQSAIRGGLPNTV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvlTDSRTGAQLGNSQlidslVHDGLWDAFNDYhmgV 159
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP---LGANAGPGRGLPR-----PDSWDIDMPNQF---E 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 160 TAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTS---ELNGTP----RLVDTDEQPRvDPSAEALASLL 232
Cdd:PRK07850 150 AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQApvlDEEGQPtgetRLVTRDQGLR-DTTMEGLAGLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 233 PTFDQqGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDL 312
Cdd:PRK07850 229 PVLEG-GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503992696 313 IEANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:PRK07850 308 VEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.10e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 295.00 E-value: 1.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVS 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDS--RTGAQLGNS----QLIDSLVH--------- 145
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKmvRWLAGWYAAksigQKLAALGKlrpsylapv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 146 ----DGLWDAFNDYHMGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRdEIVPVTSElNGTprLVDTDEQPRV 221
Cdd:PRK08170 162 igllRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDR-DGK--FYDHDDGVRP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 222 DPSAEALASLLPTFDQQ-GSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCL 300
Cdd:PRK08170 238 DSSMEKLAKLKPFFDRPyGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 301 ERAGWKLDEVDLIEANEAFAAQAISVGRVL-----------------EWDERRVNVNGGAIALGHPIGASGCRILVSLVH 363
Cdd:PRK08170 318 QRHGLTLEDLDLWEINEAFAAQVLACLAAWadeeycreqlgldgalgELDRERLNVDGGAIALGHPVGASGARIVLHLLH 397
|
410 420
....*....|....*....|....*....
gi 503992696 364 EMIKRDARKGLATLCIGGGQGVALAVERE 392
Cdd:PRK08170 398 ALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.45e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 287.78 E-value: 2.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAG-TGQNPARQSAIRGGLPNTV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDS---RTGAQLGNSQLIDSLVHDGLWDAFndyh 156
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTlpaKNGLGHYKSPGMEERYPGIQFSQF---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 157 MGvtAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSEL-NGTPRLVDTDEQPRVDPSAEALASLlPTF 235
Cdd:PRK06504 157 TG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRaDGSGEMHTVDEGIRFDATLEGIAGV-KLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 236 DQQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEA 315
Cdd:PRK06504 234 AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEV 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503992696 316 NEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:PRK06504 314 NEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-392 |
8.46e-91 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 279.95 E-value: 8.46e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 4 VVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVSAIT 83
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAP--------HVLTDSRTGAQLGnsQLIDSLVHDGLWD----- 150
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaRALVDLNKARTLG--QRLKLFSRLRLRDllpvp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 151 -AFNDY----HMGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTPrlVDTDEQPRVDPSA 225
Cdd:PRK08963 165 pAVAEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQP--LEEDNNIRGDSTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 226 EALASLLPTFDQQ-GSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDP---ALMGiaPVHATRRCLE 301
Cdd:PRK08963 243 EDYAKLRPAFDRKhGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwqdMLLG--PAYATPLALE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 302 RAGWKLDEVDLIEANEAFAAQAIS--------------VGR---VLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHE 364
Cdd:PRK08963 321 RAGLTLADLTLIDMHEAFAAQTLAnlqmfaserfarekLGRsqaIGEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHE 400
|
410 420
....*....|....*....|....*...
gi 503992696 365 MIKRDARKGLATLCIGGGQGVALAVERE 392
Cdd:PRK08963 401 LRRRGGGLGLTTACAAGGLGAAMVLEVE 428
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-386 |
2.86e-90 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 277.42 E-value: 2.86e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIG-CFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAG-TGQNPARQSAIRGGLPNT 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAP-----HVLTDsrtGAQLGNSQLIdslvhdgLWDafn 153
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQnemnrHMLRE---GWLVEHKPEI-------YWS--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 154 dyhMGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVT----------SELNGTPRLVDTDEQPRVDP 223
Cdd:PRK07108 148 ---MLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITvtagvadkatGRLFTKEVTVSADEGIRPDT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 224 SAEALASLLPTFdQQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGIAPVHATRRCLERA 303
Cdd:PRK07108 225 TLEGVSKIRSAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 304 GWKLDEVDLIEANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQ 383
Cdd:PRK07108 304 GLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQ 383
|
...
gi 503992696 384 GVA 386
Cdd:PRK07108 384 GAA 386
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
5-390 |
1.72e-83 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 258.93 E-value: 1.72e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 5 VIVGALRTPIGCFQGALSRHSAVELGSVVVKALveRSGVDPQsIDEVILGQVLtaGTGQNPARQSAIRGGLPNTVSAITI 84
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGMERE-IDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 85 NDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHvltdsRTGAQLGNsqlidslvhdglwDAFNDYHMGVTAENL 164
Cdd:PRK06690 79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF-----QNRARFSP-------------ETIGDPDMGVAAEYV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 165 AREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPvtseLNGtprLVDTDEQPRVdPSAEALASLLPTFDQQGSVTAG 244
Cdd:PRK06690 141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILS----FNG---LLDESIKKEM-NYERIIKRTKPAFLHNGTVTAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 245 NASSINDGAAAVMMMSEAKAEELGL-PILARIRAfASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEAFAAQA 323
Cdd:PRK06690 213 NSCGVNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKV 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503992696 324 ISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVE 390
Cdd:PRK06690 292 VACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.81e-83 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 260.86 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIG---CFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGT-GQNPARQSAIRGGLP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 77 NTVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHvlTDSRTGAQLGNSQLIDSlVHDGLWDAFNDYH 156
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAA--MAAEDMAAGKPPLGMGS-GNLRLRALHPQSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 157 MGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSElNGTPRLvDTDEQPRVDPSAEALASLLPTF- 235
Cdd:PRK06025 158 QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRD-DGSVAL-DHEEFPRPQTTAEGLAALKPAFt 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 236 -------DQQGSV------------------TAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAFASVGVDPALMGI 290
Cdd:PRK06025 236 aiadyplDDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 291 APVHATRRCLERAGWKLDEVDLIEANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMIKRDA 370
Cdd:PRK06025 316 APVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGL 395
|
410 420
....*....|....*....|.
gi 503992696 371 RKGLATLCIGGGQGVALAVER 391
Cdd:PRK06025 396 KRGLVTMCAAGGMAPAIIIER 416
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-390 |
3.44e-83 |
|
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: 259.35 E-value: 3.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 7 VGALRTPIGCFQGALSRHS---AVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVSAIT 83
Cdd:cd00826 1 AGAAMTAFGKFGGENGADAndlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSraphvlTDSRTGAQlgnsqlidslvhdglwdafnDYHMGVtaen 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME------TSAENNAK--------------------EKHIDV---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 164 LAREYGiSRELQDAWALSSQHKARRAIDSGRFRDEIVPVTSELNGTPRLVDTDEQPRVDPSA--EALASLLPTFDQQGSV 241
Cdd:cd00826 131 LINKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGDEAslDEIAKLRPAFDKEDFL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 242 TAGNASSINDGAAAVMMMSEAKAEELGLPI-------LARIRAFASVGVDPA----LMGIAPVHATRRCLERAGWKLDEV 310
Cdd:cd00826 210 TAGNACGLNDGAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 311 DLIEANEAFAAQAISVGRVLEWDERR------------------VNVNGGAIALGHPIGASGCRILVSLVHEMIKRD--- 369
Cdd:cd00826 290 DLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAgkr 369
|
410 420
....*....|....*....|...
gi 503992696 370 --ARKGLATLCIGGGQGVALAVE 390
Cdd:cd00826 370 qgAGAGLALLCIGGGGGAAMCIE 392
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
269-391 |
1.14e-65 |
|
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: 204.80 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 269 LPILARIRAFASVGVDPALMGIAPVHATRRCLERAGWKLDEVDLIEANEAFAAQAISVGRVLEWDERRVNVNGGAIALGH 348
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 503992696 349 PIGASGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-391 |
3.95e-60 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 200.51 E-value: 3.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVS 80
Cdd:PRK09268 6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDS------------------RTGAQLGNSQLIDS 142
Cdd:PRK09268 86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGlrkillelnrakttgdrlKALGKLRPKHLAPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 143 LVHD-----GLwdafndyHMGVTAENLAREYGISRELQDAWALSSQHKARRAIDSGRFRDEIVPVtselngtpRLVDTDE 217
Cdd:PRK09268 166 IPRNgeprtGL-------SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF--------LGLTRDN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 218 QPRVDPSAEALASLLPTFD--QQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRAF--ASV----GVDPALMg 289
Cdd:PRK09268 231 NLRPDSSLEKLAKLKPVFGkgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetAAVdfvhGKEGLLM- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 290 iAPVHATRRCLERAGWKLDEVDLIEANEAFAAQAISVGRVLEWDE-----------------RRVNVNGGAIALGHPIGA 352
Cdd:PRK09268 310 -APAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEycrerlgldaplgsidrSKLNVNGSSLAAGHPFAA 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 503992696 353 SGCRILVSLVHEMIKRDARKGLATLCIGGGQGVALAVER 391
Cdd:PRK09268 389 TGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
26-389 |
3.19e-24 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 100.21 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 26 AVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNtVSAITINDVCGSGLKALHLATQAIQCG 105
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISG-GPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 106 EADVVIAGGqenmsraphvltdsrtgaqlgnsqlidslvhdglwdafndyhmgvtaenlareygisrelqdawalssqhk 185
Cdd:cd00327 86 KADIVLAGG----------------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 186 arraidsgrfrdeivpvtselngtprlvdtdeqprvdpsaealasllptfdqqgsvtaGNASSINDGAAAVMMMSEAKAE 265
Cdd:cd00327 95 ----------------------------------------------------------SEEFVFGDGAAAAVVESEEHAL 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 266 ELGLPILARIRAFASVGVD----PALMGIAPVHATRRCLERAGWKLDEVDLIEANEAFAAQAISVGRVLEWDE---RRVN 338
Cdd:cd00327 117 RRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPdgvRSPA 196
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 503992696 339 VNGGAIALGHPIGASGCRILVSLV----HEMIK---RDARKGLATLCIGGGQGVALAV 389
Cdd:cd00327 197 VSATLIMTGHPLGAAGLAILDELLlmleHEFIPptpREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-373 |
5.41e-22 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 96.50 E-value: 5.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGCFQGALSRHSAVELGsvvVKALvERSGVDPQSIDEVILGQVLtAGT--GQ-NPARQSAIRGGLPN 77
Cdd:PRK06064 1 MRDVAIIGVGQTKFGELWDVSLRDLAVEAG---LEAL-EDAGIDGKDIDAMYVGNMS-AGLfvSQeHIAALIADYAGLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 78 tVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLgnsqlidslvhDGLWDAFndyhM 157
Cdd:PRK06064 76 -IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAG-----------DYEWEEF----F 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 158 GVTAENL----AR----EYGISRELQDAWALSSQHKARRAIDSgRFRDEIVpVTSELNGTPrlvdtdeqprvdpsaeaLA 229
Cdd:PRK06064 140 GATFPGLyaliARrymhKYGTTEEDLALVAVKNHYNGSKNPYA-QFQKEIT-VEQVLNSPP-----------------VA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 230 SLLPTFDqqgsvtagnASSINDGAAAVMMMSEAKAEELGL-PIlaRIRAFASVGVDPAL------MGI-APVHATRRCLE 301
Cdd:PRK06064 201 DPLKLLD---------CSPITDGAAAVILASEEKAKEYTDtPV--WIKASGQASDTIALhdrkdfTTLdAAVVAAEKAYK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 302 RAGWKLDEVDLIEANEAFA-AQAISV-----------GRVLEWDERR------VNVNGGAIALGHPIGASGCRILVSLVH 363
Cdd:PRK06064 270 MAGIEPKDIDVAEVHDCFTiAEILAYedlgfakkgegGKLAREGQTYiggdipVNPSGGLKAKGHPVGATGVSQAVEIVW 349
|
410
....*....|
gi 503992696 364 EmIKRDARKG 373
Cdd:PRK06064 350 Q-LRGEAEKG 358
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
25-389 |
5.27e-20 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 90.40 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 25 SAVELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIRGGLPNTVsAITINDVCGSGLKALHLATQAIQC 104
Cdd:cd00829 15 SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKP-ATRVEAAGASGSAAVRAAAAAIAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 105 GEADVVIAGGQENMSRAPhvlTDSRTGAQLGNSQLIDSLVHDGLwdAFNDYHMGVTAENLAReYGISRELQDAWALssqh 184
Cdd:cd00829 94 GLADVVLVVGAEKMSDVP---TGDEAGGRASDLEWEGPEPPGGL--TPPALYALAARRYMHR-YGTTREDLAKVAV---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 185 KARR-AIDSGR--FRDEIvPVTSELNGtpRLVdtdeqprVDPsaealasllptfdqqgsVTAGNASSINDGAAAVMMMSE 261
Cdd:cd00829 164 KNHRnAARNPYaqFRKPI-TVEDVLNS--RMI-------ADP-----------------LRLLDCCPVSDGAAAVVLASE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 262 AKAEELGLPiLARIRAFAsVGVDPALMG--------IAPVHATRRCLERAGWKLDEVDLIEANEAF-------------- 319
Cdd:cd00829 217 ERARELTDR-PVWILGVG-AASDTPSLSerddflslDAARLAARRAYKMAGITPDDIDVAELYDCFtiaellaledlgfc 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 320 ----AAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGcrilVSLVHEMIK-----------RDARKGLATLciGGGQG 384
Cdd:cd00829 295 ekgeGGKLVREGDTAIGGDLPVNTSGGLLSKGHPLGATG----LAQAVEAVRqlrgeagarqvPGARVGLAHN--IGGTG 368
|
....*
gi 503992696 385 VALAV 389
Cdd:cd00829 369 SAAVV 373
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
28-368 |
8.05e-13 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 69.10 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 28 ELGSVVVKALVERSGVDPQSIDEVILGQVLTAGTGQNPA----RQSAIRGGLPNTVSAitindVCGSGLKALHLATQAIQ 103
Cdd:PRK12578 23 ELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPApivaEYSGLTGKVPLRVEA-----MCATGLAASLTAYTAVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 104 CGEADVVIAGGQENMSRaphvlTDSRT----GAQLGNSQlidslvhdglWD------AFNDYHMGVTAENLAReYGISRE 173
Cdd:PRK12578 98 SGLVDMAIAVGVDKMTE-----VDTSTslaiGGRGGNYQ----------WEyhfygtTFPTYYALYATRHMAV-YGTTEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 174 lQDAWALSSQHKARRAIDSGRFRDeivPVTSElngtprlvdtdeqprvdpsaEALASLLPTFdqqgSVTAGNASSINDGA 253
Cdd:PRK12578 162 -QMALVSVKAHKYGAMNPKAHFQK---PVTVE--------------------EVLKSRAISW----PIKLLDSCPISDGS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 254 AAVMMMSEAKAEELGL--PI---------------------------LARIRAFASVGVDPALMGIAPVHATRRCLERAG 304
Cdd:PRK12578 214 ATAIFASEEKVKELKIdsPVwitgigyandyayvarrgewvgfkatqLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMG 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503992696 305 WKldevDLIEANEAFAAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGcrilVSLVHEMIKR 368
Cdd:PRK12578 294 YE----DLGFTEKGKGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATG----LSMIYEITKQ 349
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-386 |
1.00e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 62.66 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPIGcfqgalsRHSAVELGSVVVKAL---VERSGVDPQSIDEVILGQvLTAGTGQNPARQSAIRGGLPN 77
Cdd:PRK07516 1 MMTASIVGWAHTPFG-------KLDAETLESLIVRVAreaLAHAGIAAGDVDGIFLGH-FNAGFSPQDFPASLVLQADPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 78 T--VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltdsrtGAQLGNSQLIDSLVHD------GLW 149
Cdd:PRK07516 73 LrfKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP--------TAEVGDILLGASYLKEegdtpgGFA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 150 DAFndyhmGVTAENLAREYG-ISRELqdAWALSSQHK---------ARRAIDSGRFRDEivpvtSELNgtprlvdtdeqP 219
Cdd:PRK07516 145 GVF-----GRIAQAYFQRYGdQSDAL--AMIAAKNHAngvanpyaqMRKDLGFEFCRTV-----SEKN-----------P 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 220 RVdpsaealASLLPTFDqqgsvtagnASSINDGAAAVMMMSEAKAEELGLPIlaRIRAFASVG-------VDPALMGiAP 292
Cdd:PRK07516 202 LV-------AGPLRRTD---------CSLVSDGAAALVLADAETARALQRAV--RFRARAHVNdflplsrRDPLAFE-GP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 293 VHATRRCLERAGWKLDEVDLIEANEAF------------------AAQAISVGRVLEWDERRVNVNGGAIALGHPIGASG 354
Cdd:PRK07516 263 RRAWQRALAQAGVTLDDLSFVETHDCFtiaelieyeamglappgqGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATG 342
|
410 420 430
....*....|....*....|....*....|....*....
gi 503992696 355 -------CRILVSLVHEMIKRDARkgLATLCIGGGQGVA 386
Cdd:PRK07516 343 vsmhvlaAMQLTGEAGGMQIPGAK--LAGVFNMGGAAVA 379
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
32-114 |
4.31e-07 |
|
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: 50.71 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 32 VVVKALvERSGVDPQSIDEVILGQVLTAGTGQNPARQSAIR------------GGLPNTVS------------AITINDV 87
Cdd:pfam00109 94 AAWEAL-EDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEdggprrgspfavGTMPSVIAgrisyflglrgpSVTVDTA 172
|
90 100
....*....|....*....|....*..
gi 503992696 88 CGSGLKALHLATQAIQCGEADVVIAGG 114
Cdd:pfam00109 173 CSSSLVAIHAAVQSIRSGEADVALAGG 199
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
82-354 |
4.97e-07 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 51.44 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 82 ITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSraPHVLT---DSRTGAqLGNsqlidslvHDGLWDAFNDYHM- 157
Cdd:PRK08256 74 VNVNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQ--PGALGsvwDDRPSP-LER--------FDKALAELQGFDPa 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 158 -------GVTAENLAREYGISRElQDAW--ALSSQHKAR--RAIdsgrFRDeivPVTSElngtprlvdtdeqprvdpsaE 226
Cdd:PRK08256 143 ppalrmfGGAGREHMEKYGTTAE-TFAKigVKARRHAANnpYAQ----FRD---EYTLE--------------------D 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 227 ALASllPTFdqQGSVTAGNASSINDGAAAVMMMSEAKAEELGLPILARIRA------FASVGVDPALMGIAPVHATR--- 297
Cdd:PRK08256 195 VLAS--PMI--WGPLTRLQCCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAqamttdTPSTFDGRSMIDLVGYDMTRaaa 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 298 -RCLERAGWKLDEVDLIEANEAFAAQAISV------------------------GRVLewderrVNVNGGAIALGHPIGA 352
Cdd:PRK08256 271 qQVYEQAGIGPEDIDVVELHDCFSANELLTyealglcpegeaekfiddgdntygGRWV------VNPSGGLLSKGHPLGA 344
|
..
gi 503992696 353 SG 354
Cdd:PRK08256 345 TG 346
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
32-114 |
6.31e-06 |
|
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: 47.94 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 32 VVVKALvERSGVDPQSIDE----VILGQ------VLTAGTGQNPARQSAI---RGGLPNTVS--------AITINDVCGS 90
Cdd:cd00833 94 VAWEAL-EDAGYSPESLAGsrtgVFVGAsssdylELLARDPDEIDAYAATgtsRAFLANRISyffdlrgpSLTVDTACSS 172
|
90 100
....*....|....*....|....
gi 503992696 91 GLKALHLATQAIQCGEADVVIAGG 114
Cdd:cd00833 173 SLVALHLACQSLRSGECDLALVGG 196
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
1-381 |
9.09e-06 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 47.38 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 1 MKDVVIVGALRTPigcFQGALSRHSA--VELGSVVVKALVERSGVDPQSIDEVILGQV---LTAGTGQnparqsaiRGGL 75
Cdd:PRK06289 2 SDDVWVLGGYQSD---FARNWTKEGRdfADLTREVVDGTLAAAGVDADDIEVVHVGNFfgeLFAGQGH--------LGAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 76 PNTVS-------AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltDSRTGAQLGNSQLIDslvHDG- 147
Cdd:PRK06289 71 PATVHpalwgvpASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVP----GDVAAEHLGAAAWTG---HEGq 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 148 ----LW-DAFNDyhmgvTAENLAREYGISRELQDAWALSSQHKARRAIDSgRFRDEIVPvtselngTPRLVDTDEQprvD 222
Cdd:PRK06289 144 darfPWpSMFAR-----VADEYDRRYGLDEEHLRAIAEINFANARRNPNA-QTRGWAFP-------DEATNDDDAT---N 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 223 PSAEalasllptfdqqGSVTAGNASSINDGAAAVMMMSEAKAEEL-GLPILARIRAFasvGVDPALMGIAP--------- 292
Cdd:PRK06289 208 PVVE------------GRLRRQDCSQVTDGGAGVVLASDAYLRDYaDARPIPRIKGW---GHRTAPLGLEQkldrsagdp 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 293 -----VH-ATRRCLERAGWKLDEVDLIEANEAFAA------------------QAISVGRVLEWDERRVNVNGGAIALGH 348
Cdd:PRK06289 273 yvlphVRqAVLDAYRRAGVGLDDLDGFEVHDCFTPseylaidhigltgpgeswKAIENGEIAIGGRLPINPSGGLIGGGH 352
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 503992696 349 PIGASGCRILVSLVHEMIKR-------DARKGLaTLCIGG 381
Cdd:PRK06289 353 PVGASGVRMLLDAAKQVTGTagdyqveGAKTFG-TLNIGG 391
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
29-354 |
2.33e-05 |
|
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: 45.99 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 29 LGSVVVKALVERSGVDPQSIDE----VILG----------QVLTAGTGQNPARQSA--IRGGLPNTVSA----------- 81
Cdd:cd00834 74 FALAAAEEALADAGLDPEELDPerigVVIGsgigglatieEAYRALLEKGPRRVSPffVPMALPNMAAGqvairlglrgp 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 82 -ITINDVCGSGLKALHLATQAIQCGEADVVIAGGqenmsraphvltdsrtgaqlgnsqlIDSLVHDGLWDAFNDyhMGvt 160
Cdd:cd00834 154 nYTVSTACASGAHAIGDAARLIRLGRADVVIAGG-------------------------AEALITPLTLAGFAA--LR-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 161 aenlareygisrelqdawALSSQH----KARRAIDSGRfrDEIVpvtselngtprlvdtdeqprvdpsaealasllptfd 236
Cdd:cd00834 205 ------------------ALSTRNddpeKASRPFDKDR--DGFV------------------------------------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 237 qqgsvtagnassINDGAAAVMMMSEAKAEELGLPILARIRAFASVG-----VDPALMGIAPVHATRRCLERAGWKLDEVD 311
Cdd:cd00834 229 ------------LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDID 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 503992696 312 LI-------EANEAFAAQAISvgRVLEWDERRVNVNG--GAIalGHPIGASG 354
Cdd:cd00834 297 YInahgtstPLNDAAESKAIK--RVFGEHAKKVPVSStkSMT--GHLLGAAG 344
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
235-354 |
1.43e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 43.50 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 235 FDQQ--GSVTAgnassinDGAAAVMMMSEAKAEELGLPILARIRAF-----ASVGVDPALMGIAPVHATRRCLERAGWKL 307
Cdd:PRK05952 199 FDRQreGLVLG-------EGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTP 271
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 503992696 308 DEVDLIEA-------NEAFAAQAISvgrvlEWDERRVNVNGGAIALGHPIGASG 354
Cdd:PRK05952 272 EDIDYIHAhgtatrlNDQREANLIQ-----ALFPHRVAVSSTKGATGHTLGASG 320
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
252-354 |
1.68e-04 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 43.55 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 252 GAAAVMMMSEAKAEELGLPILARIRAFASVG-----VDPALMGIAPVHATRRCLERAGWKLDEVDLI-------EANEAF 319
Cdd:COG0304 232 GAGVLVLEELEHAKARGAKIYAEVVGYGASSdayhiTAPAPDGEGAARAMRAALKDAGLSPEDIDYInahgtstPLGDAA 311
|
90 100 110
....*....|....*....|....*....|....*..
gi 503992696 320 AAQAISvgRVLEWDERRVNVNggAI--ALGHPIGASG 354
Cdd:COG0304 312 ETKAIK--RVFGDHAYKVPVS--STksMTGHLLGAAG 344
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
81-114 |
2.77e-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: 2.77e-04
10 20 30
....*....|....*....|....*....|....
gi 503992696 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGG 114
Cdd:smart00825 90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
247-365 |
3.04e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 42.57 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 247 SSINDGAAAVMMMSEAKAEELGLP--------ILARIRAFASVGVDP--ALMGIAPVHATRRCLERAGWKLDEVDLIEAN 316
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSpndsrlveIKSLACASGNLYEDPpdATRMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503992696 317 EAF------------------AAQAISVGRVLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEM 365
Cdd:PTZ00455 336 DCFtiaellmyealgiaeyghAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQM 402
|
|
| PRK08257 |
PRK08257 |
acetyl-CoA acetyltransferase; Validated |
251-314 |
3.61e-04 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 236204 [Multi-domain] Cd Length: 498 Bit Score: 42.59 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 251 DGAAAVMMMSEAKAEELGLP------------------ILARIRAFASVGVDpalmgiapvHATRRCLERAGWKLDEVDL 312
Cdd:PRK08257 244 DQGAAVLLTSVAKARRLGVPedrwvylhggadahdpydILERPDLHRSPAIR---------AAGRRALALAGLGIDDIDA 314
|
..
gi 503992696 313 IE 314
Cdd:PRK08257 315 FD 316
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
32-114 |
6.70e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 42.17 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 32 VVVKALvERSGVDPQSIDE----VILG------QVLTAGTGQNPARQSAIrGGLPNTVS------------AITINDVCG 89
Cdd:COG3321 98 VAWEAL-EDAGYDPESLAGsrtgVFVGassndyALLLLADPEAIDAYALT-GNAKSVLAgrisykldlrgpSVTVDTACS 175
|
90 100
....*....|....*....|....*
gi 503992696 90 SGLKALHLATQAIQCGEADVVIAGG 114
Cdd:COG3321 176 SSLVAVHLACQSLRSGECDLALAGG 200
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
82-119 |
7.38e-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: 41.27 E-value: 7.38e-04
10 20 30
....*....|....*....|....*....|....*...
gi 503992696 82 ITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMS 119
Cdd:cd00828 156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
71-116 |
3.42e-03 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 39.31 E-value: 3.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503992696 71 IRGGLPNTVSAitindvCGSGLKALHLATQAIQCGEADVVIAGGQE 116
Cdd:COG0304 150 LKGPNYTVSTA------CASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
20-120 |
4.43e-03 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 38.68 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 20 ALSRHSAVELGSVVVKALVERSGVDPQSIDEVIlgqvLTAGTGQN--PARQSAIRG--GLPNTVsAITINDVCGSGLKAL 95
Cdd:cd00830 44 ADPGETTSDLAVEAAKKALEDAGIDADDIDLII----VATSTPDYlfPATACLVQArlGAKNAA-AFDINAACSGFLYGL 118
|
90 100
....*....|....*....|....*
gi 503992696 96 HLATQAIQCGEADVVIAGGQENMSR 120
Cdd:cd00830 119 STAAGLIRSGGAKNVLVVGAETLSR 143
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
251-354 |
4.49e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 39.00 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 251 DGAAAVMMMSEAKAEELGLPILARIRAFASVG-----VDPALMGIAPVHATRRCLERAGWKLDEVDLIEA-------NEA 318
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDYINAhgtstpaGDK 311
|
90 100 110
....*....|....*....|....*....|....*.
gi 503992696 319 FAAQAISvgRVLEWDERRVNVNGGAIALGHPIGASG 354
Cdd:PRK07314 312 AETQAIK--RVFGEHAYKVAVSSTKSMTGHLLGAAG 345
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
25-120 |
5.55e-03 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 38.55 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992696 25 SAVELGSVVVKALVERSGVDPQSIDEVILG----QVLTAGTGqnpAR-QSAIrgGLPNTVsAITINDVCGSGLKALHLAT 99
Cdd:COG0332 50 TTSDLAVEAARKALEAAGIDPEDIDLIIVAtvtpDYLFPSTA---CLvQHKL--GAKNAA-AFDINAACSGFVYALSVAA 123
|
90 100
....*....|....*....|..
gi 503992696 100 QAIQCGEAD-VVIAGGqENMSR 120
Cdd:COG0332 124 ALIRSGQAKnVLVVGA-ETLSR 144
|
|
| |
