|
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: 692.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVS 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLLDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 161 AENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEALIVDTDEQPRTDASAEGLAKLDPAFETLG 240
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 241 SVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNEAF 320
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550763766 321 AAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-392 |
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: 604.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVS 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLgNSQLLDSLVHDGLWDAFNDYHMGVT 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 161 AENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEAlIVDTDEQPRTDASAEGLAKLDPAFETLG 240
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEV-VVDRDEGPRPDTTLEKLAKLKPAFKKDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 241 SVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNEAF 320
Cdd:COG0183 239 TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550763766 321 AAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:COG0183 319 AAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-392 |
0e+00 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 594.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVS 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLLDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 161 AENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEALIVDTDEQPRTDASAEGLAKLDPAFETLG 240
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 241 SVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNEAF 320
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550763766 321 AAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-392 |
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: 592.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 5 VIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVSAITI 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 85 NDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLlDSLVHDGLWDAFNDYHMGVTAENL 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 165 AREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTqRQNGEALIVDTDEQPRTDASAEGLAKLDPAFETLGSVTA 244
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEV-PGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 245 GNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNEAFAAQA 324
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550763766 325 ISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-391 |
4.13e-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: 4.13e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 6 IVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVSAITIN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 86 DVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDS-RTGAQLGNSQLLDSLVHDgLWDAFNDYHMGVTAENL 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 165 AREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQrQNGEALIVDTDEQPRTDASAEGLAKLDPAFETLGSVTA 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVK-GRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 245 GNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNEAFAAQA 324
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550763766 325 ISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIE 391
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-391 |
9.10e-161 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 456.87 E-value: 9.10e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVS 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLLDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 161 AENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEALIVDTDEQPRTDASAEGLAKLDPAFETLG 240
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 241 SVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNEAF 320
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550763766 321 AAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIE 391
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-392 |
1.82e-157 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 448.64 E-value: 1.82e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVL-TAGAGQNPARQAALKGGLPNTV 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpTEPRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLLDSLVhDGLWDAFNDYHMGV 159
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMV-GALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 160 TAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEaLIVDTDEQPRTDASAEGLAKLDPAF-ET 238
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGE-VVFDTDEHVRADTTLEDLAKLKPVFkKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 239 LGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNE 318
Cdd:PRK09051 240 NGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550763766 319 AFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-392 |
8.48e-154 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 439.53 E-value: 8.48e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 2 KDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVSA 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 82 ITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLLDSLVHDGLWDAFNDYHMGVTA 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 162 ENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNG-EALIVDTDEQPrTDASAEGLAKLDPAF-ETL 239
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGrPSVIVDKDEGL-GKFDPAKLRKLRPSFkEDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 240 GSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNEA 319
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550763766 320 FAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.69e-145 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 418.62 E-value: 1.69e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQvlTAGAGQNPA--RQAALKGGLPNT 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLLDSLVHdGLWDAFNDYH-- 156
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRLAR-GRETAGGRRFpv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 157 ---MGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEALIVDTDEQPRTDASAEGLAKLD 233
Cdd:PRK06205 158 pggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLAKLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 234 PAFETL---GSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLND 310
Cdd:PRK06205 238 PIMGKQdpeATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 311 VDLIEVNEAFAAQAISVGKMLEW---DPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVA 387
Cdd:PRK06205 318 IDLIELNEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLA 397
|
....*
gi 550763766 388 LAIER 392
Cdd:PRK06205 398 AVFER 402
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-391 |
8.60e-144 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 414.04 E-value: 8.60e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVS 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVlTDSRTGAQLGNSQLLDSLVHDGLWDAFNDYHMGVT 160
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHG-SYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 161 AENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEALIvDTDEQPRTDASAEGLAKLDPAFETLG 240
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLF-DHDETVRPDTSLEILSKLRPAFDKNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 241 SVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNEAF 320
Cdd:PRK06633 240 VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550763766 321 AAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIE 391
Cdd:PRK06633 320 AAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-392 |
4.89e-137 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 397.02 E-value: 4.89e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVER-SGVAAHEIDEVILGQVLTAGA-GQNPARQAALKGGLPNT 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSrTGAQLGNSQLLDS-----LVHDGLWDAFN 153
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKA-DSAFSRQAEIFDTtigwrFVNPLMKAQYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 154 DYHMGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEALIVDTDEQPRTDASAEGLAKLD 233
Cdd:PRK09050 160 VDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALAKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 234 PAFETLGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDL 313
Cdd:PRK09050 240 PVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 314 IEVNEAFAAQAISVGKMLEW--DPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIE 391
Cdd:PRK09050 320 IELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIE 399
|
.
gi 550763766 392 R 392
Cdd:PRK09050 400 R 400
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-392 |
2.15e-125 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 366.98 E-value: 2.15e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHS-AVDLGSVVVRALVERS-GVAAHEIDEVILGQVL-TAGAGQNPARQAALKGGLPN 77
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAFRNVrAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQqTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 78 TVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSrapHVLTD---------SRTGAQLGNSqlldslvhdgl 148
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMG---HVPMNhgvdfhpglSKNVAKAAGM----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 149 wdafndyhMGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEALIVDTDEQPRTDASAEG 228
Cdd:PRK08947 147 --------MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 229 LAKLDPAFETL-GSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQ 307
Cdd:PRK08947 219 LAALRPAFDPVnGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 308 LNDVDLIEVNEAFAAQAISVGKMLEW-DPL--RVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQ 384
Cdd:PRK08947 299 ISDIDVFELNEAFAAQSLPCLKDLGLlDKMdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQ 378
|
....*...
gi 550763766 385 GVALAIER 392
Cdd:PRK08947 379 GIATVFER 386
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-392 |
1.41e-124 |
|
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.
Pssm-ID: 131483 Cd Length: 400 Bit Score: 365.26 E-value: 1.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 2 KDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVER-SGVAAHEIDEVILGQVLTAGA-GQNPARQAALKGGLPNTV 79
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRT----GAQLGNSQLLDSLVHDGLWDAFNDY 155
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSafsrSAKIEDTTIGWRFINPLMKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 156 HMGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEALIVDTDEQPRTDASAEGLAKLDPA 235
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEGLAKLKPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 236 FETLGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIE 315
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550763766 316 VNEAFAAQAISVGKMLEW--DPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:TIGR02430 321 LNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-263 |
6.25e-123 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 355.84 E-value: 6.25e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 4 VVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVSAIT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVL-TDSRTGAQLGNSQLLDSLVHDGLWDAFNDYHMGVTAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 163 NLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEaLIVDTDEQPRTDASAEGLAKLDPAFETLGSV 242
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGK-PTVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
|
250 260
....*....|....*....|.
gi 550763766 243 TAGNASSINDGAAAVMMMSES 263
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
4-391 |
3.92e-121 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 356.51 E-value: 3.92e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 4 VVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVSAIT 83
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLLDSLVHDGLWDAFNDYH-MGVTAE 162
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 163 NLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEAlIVDTDEQPRTdASAEGLAKLDPAFETLGSV 242
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDT-VIDRDEQPFK-ANPEKIPTLKPAFSKTGTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 243 TAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNEAFAA 322
Cdd:PRK06954 247 TAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550763766 323 QAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIE 391
Cdd:PRK06954 327 VTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-392 |
3.20e-120 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 353.67 E-value: 3.20e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIG-CFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVL-TAGAGQNPARQAALKGGLPNT 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAP---HVLTDsrtgaqlgNSQLLDSLvhdglwdafNDY 155
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPmmgHVVRP--------NPRLVEAA---------PEY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 156 HMGV--TAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVS-TQRQNGE-------ALIVDTDEQPRTDAS 225
Cdd:PRK07661 144 YMGMghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDvTLRTVGEnnklqeeTITFSQDEGVRADTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 226 AEGLAKLDPAFETLGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAG 305
Cdd:PRK07661 224 LEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 306 WQLNDVDLIEVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQG 385
Cdd:PRK07661 304 LELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMG 383
|
....*..
gi 550763766 386 VALAIER 392
Cdd:PRK07661 384 AAGVFEL 390
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-392 |
5.19e-117 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 347.91 E-value: 5.19e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 3 DVVIVGALRTAIgCF--QGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQ-NPARQAALKGGLPNTV 79
Cdd:PLN02287 47 DVVIVAAYRTPI-CKakRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLGNSQLLDSLVHdglwdafndyhMGV 159
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP-----------MGI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 160 TAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQN-----GEALIVDTDEQPRTDASAEGLAKLDP 234
Cdd:PLN02287 195 TSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDpktgeEKPIVISVDDGIRPNTTLADLAKLKP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 235 AFETLGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLI 314
Cdd:PLN02287 275 VFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 315 EVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRN--ARKGIATLCIGGGQGVALAIER 392
Cdd:PLN02287 355 EINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-392 |
5.56e-116 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 343.24 E-value: 5.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCF------QGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLtaGAGQN---PARQAAL 71
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFrpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENwlyGGRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 72 KGGLPNTVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAP-----HV------LTDSRtgaqlgnsqll 140
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPmgdnpHIepnpklLTDPK----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 141 dsLVHdglWDAFNDYHMGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRqNGEALIVDTDEQP 220
Cdd:PRK06445 148 --YIE---YDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEV-EGKKKVVDVDQSV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 221 RTDASAEGLAKLDPAFETLGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRC 300
Cdd:PRK06445 222 RPDTSLEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 301 LERAGWQLNDVDLIEVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCI 380
Cdd:PRK06445 302 LEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCV 381
|
410
....*....|..
gi 550763766 381 GGGQGVALAIER 392
Cdd:PRK06445 382 GGGQGGAVVLER 393
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-391 |
7.20e-115 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 340.06 E-value: 7.20e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVS 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVL-TDSRTGAQ---LGNSQLLDSLVHDGLWDAFNDYH 156
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPKhllHKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 157 MGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTqrqngealiVDTDEQPRTdASAEGLAKLDPAF 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND---------LDRDEGIRK-TTMEDLAKLPPAF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 237 ETLGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEV 316
Cdd:PRK06366 231 DKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEH 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550763766 317 NEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIE 391
Cdd:PRK06366 311 NEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-392 |
6.74e-114 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 338.13 E-value: 6.74e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVD--LGSVVVRALVERSGVAAHEIDEVILGQVL-TAGAGQNPARQAALKGGLPN 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGKAPRGMFKNTRPDdlLAHVLRSAVAQVPGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 78 TVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltdsrtgaQLGNSQLLDSLVHDGLWDAFNDYHM 157
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP----------MMGNKPSMSPAIFARDENVGIAYGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 158 GVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVS-TQRQNGEA--------LIVDTDEQPRTDASAEG 228
Cdd:PRK09052 155 GLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEiTERFPDLAtgevdvktRTVDLDEGPRADTSLEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 229 LAKLDPAFETLGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQL 308
Cdd:PRK09052 235 LAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 309 NDVDLIEVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVAL 388
Cdd:PRK09052 315 DDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAG 394
|
....
gi 550763766 389 AIER 392
Cdd:PRK09052 395 IFER 398
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-392 |
1.45e-110 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 329.43 E-value: 1.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGA-GQNPARQAALKGGLPNTV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLT-------------DSRTGAQLGNSQLLDSlvhd 146
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGkaesafsrdakvfDTTIGARFPNPKIVAQ---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 147 glwdaFNDYHMGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVST-QRQNGEALIVDTDEQPRTDAS 225
Cdd:PRK08131 157 -----YGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVpQGRKLPPKLVAEDEHPRPSST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 226 AEGLAKLDPAFETlGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAG 305
Cdd:PRK08131 232 VEALTKLKPLFEG-GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 306 WQLNDVDLIEVNEAFAAQAISVGKML--EWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGG 383
Cdd:PRK08131 311 LTLDDMDIIEINEAFASQVLGCLKGLgvDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVG 390
|
....*....
gi 550763766 384 QGVALAIER 392
Cdd:PRK08131 391 QGLAMVIER 399
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.31e-107 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 321.83 E-value: 1.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQ--GALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAG-AGQNPARQAALKGGLPN 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 78 TVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltdsrTGAQlGNSQLLDSLVhdglwdAFNDYHM 157
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP-------MGSD-GGAWAMDPST------NFPTYFV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 158 --GVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQrqNGeALIVDTDEQPRTDASAEGLAKLDPA 235
Cdd:PRK08242 147 pqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQ--NG-LTILDHDEHMRPGTTMESLAKLKPS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 236 FETLGSV---------------------TAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPV 294
Cdd:PRK08242 224 FAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 295 YATRRCLERAGWQLNDVDLIEVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKG 374
Cdd:PRK08242 304 PATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTA 383
|
410
....*....|....*...
gi 550763766 375 IATLCIGGGQGVALAIER 392
Cdd:PRK08242 384 LITLCVGGGMGIATIIER 401
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-392 |
1.53e-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: 318.81 E-value: 1.53e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 3 DVVIVGALRTAIGCFQGALARHS-AVDLGSVVVRALVER-SGVAAHEIDEVILGQV-LTAGAGQNPARQAALKGGLPNTV 79
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTrAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVqQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHvltdsrtgaqlgnSQLLDSLVHDGLWDAFNDYHMGV 159
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPM-------------MHGVDFHPGMSLHVAKAAGMMGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 160 TAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEALIVDTDEQPRTDASAEGLAKLDPAFETL 239
Cdd:TIGR02445 148 TAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPAFDPK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 240 -GSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNE 318
Cdd:TIGR02445 228 nGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550763766 319 AFAAQAISVGK---MLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:TIGR02445 308 AFAAQALPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-392 |
3.85e-106 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 318.49 E-value: 3.85e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIG-CFQGALARHSAVDLGSVVVRALVER-SGVAAHEIDEVILGQVLTAG-AGQNPARQAALKGGLPn 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKvPALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 78 TVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDS--------------RTG--AQLGNSQLLD 141
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSlpdtknplfaeaqaRTAarAEGGAEAWHD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 142 SLVHDGLWDAFndYHMGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQrqngEALIVDTDEQPR 221
Cdd:PRK07851 160 PREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP----DGTVVSTDDGPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 222 TDASAEGLAKLDPAFETLGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCL 301
Cdd:PRK07851 234 AGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 302 ERAGWQLNDVDLIEVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIG 381
Cdd:PRK07851 314 ARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVG 393
|
410
....*....|.
gi 550763766 382 GGQGVALAIER 392
Cdd:PRK07851 394 GGQGMAMVLER 404
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-392 |
4.51e-103 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 309.71 E-value: 4.51e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAG--AGqNPARQAALKGGLPNT 78
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpqAG-NIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvLTDSRT-GAQLGnsqLLDSLVHDGLWDA-FNDYH 156
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTaGEQLG---FTSPFAESKGWLHrYGDQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 157 MG--VTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTqrqngealiVDTDEQPRtDASAEGLAKLDP 234
Cdd:PRK07801 155 VSqfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPR-ETSLEKMAGLKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 235 AFETlGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLI 314
Cdd:PRK07801 225 LVEG-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVV 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550763766 315 EVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:PRK07801 304 EINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-392 |
5.02e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 308.48 E-value: 5.02e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVS 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDS--RTGAQLGNS----QLLDSLVH--------- 145
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKmvRWLAGWYAAksigQKLAALGKlrpsylapv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 146 ----DGLWDAFNDYHMGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRdEIVPVSTQRQNgealIVDTDEQPR 221
Cdd:PRK08170 162 igllRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDRDGK----FYDHDDGVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 222 TDASAEGLAKLDPAFET-LGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRC 300
Cdd:PRK08170 237 PDSSMEKLAKLKPFFDRpYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 301 LERAGWQLNDVDLIEVNEAFAAQAISV-----------------GKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLV 363
Cdd:PRK08170 317 LQRHGLTLEDLDLWEINEAFAAQVLAClaawadeeycreqlgldGALGELDRERLNVDGGAIALGHPVGASGARIVLHLL 396
|
410 420
....*....|....*....|....*....
gi 550763766 364 HEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:PRK08170 397 HALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-392 |
2.91e-100 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 302.80 E-value: 2.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAG-AGQNPARQAALKGGLPNTV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTdsrtgAQLGNSQLLDSLVHDGLWDAFND--YHM 157
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP-----STLPAKNGLGHYKSPGMEERYPGiqFSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 158 GVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEALIVDTDEQPRTDASAEGLAKLDPAFE 237
Cdd:PRK06504 156 FTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKLIAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 238 TlGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVN 317
Cdd:PRK06504 236 G-GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVN 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550763766 318 EAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:PRK06504 315 EAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-392 |
2.22e-98 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 297.79 E-value: 2.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGA-GQNPARQAALKGGLPNTV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvlTDSRTGAQLGNSQlldslVHDGLWDAFNDYhmgV 159
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP---LGANAGPGRGLPR-----PDSWDIDMPNQF---E 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 160 TAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVST------QRQNGEALIVDTDEQPRtDASAEGLAKLD 233
Cdd:PRK07850 150 AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQApvldeeGQPTGETRLVTRDQGLR-DTTMEGLAGLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 234 PAFETlGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDL 313
Cdd:PRK07850 229 PVLEG-GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550763766 314 IEVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:PRK07850 308 VEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-387 |
5.51e-95 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 289.36 E-value: 5.51e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIG-CFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGA-GQNPARQAALKGGLPNT 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSraphvLTDSRTGAQLGNSQLLDSLVHDGLWDafndyhMG 158
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIS-----CVQNEMNRHMLREGWLVEHKPEIYWS------ML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 159 VTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVS---------TQRQNGEALIVDTDEQPRTDASAEGL 229
Cdd:PRK07108 150 QTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITvtagvadkaTGRLFTKEVTVSADEGIRPDTTLEGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 230 AKLDPAFETlGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLN 309
Cdd:PRK07108 230 SKIRSALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550763766 310 DVDLIEVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVA 387
Cdd:PRK07108 309 DIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-392 |
3.20e-89 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 275.71 E-value: 3.20e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 4 VVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVSAIT 83
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAP--------HVLTDSRTGAQLGnsQLLDSLVHDGLWD----- 150
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaRALVDLNKARTLG--QRLKLFSRLRLRDllpvp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 151 -AFNDY----HMGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEI--VPVSTQRQngealIVDTDEQPRTD 223
Cdd:PRK08963 165 pAVAEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVmtAHVPPYKQ-----PLEEDNNIRGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 224 ASAEGLAKLDPAFE-TLGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDP---ALMGiaPVYATRR 299
Cdd:PRK08963 240 STLEDYAKLRPAFDrKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwqdMLLG--PAYATPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 300 CLERAGWQLNDVDLIEVNEAFAAQAISVGKML-----------------EWDPLRVNVNGGAIALGHPIGASGCRILVSL 362
Cdd:PRK08963 318 ALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQT 397
|
410 420 430
....*....|....*....|....*....|
gi 550763766 363 VHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:PRK08963 398 LHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-391 |
1.88e-87 |
|
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: 270.13 E-value: 1.88e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 7 VGALRTAIGCFQGALARHS---AVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVSAIT 83
Cdd:cd00826 1 AGAAMTAFGKFGGENGADAndlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSraphvlTDSRTGAQlgnsqlldslvhdglwdafnDYHMGVtaen 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME------TSAENNAK--------------------EKHIDV---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 164 LAREYGiSRELQDAYALSSQQKARAAIDSGRFRDEIVPVSTQRQNGEaLIVDTDE--QPRTDASAEGLAKLDPAFETLGS 241
Cdd:cd00826 131 LINKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGD-IHSDADEyiQFGDEASLDEIAKLRPAFDKEDF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 242 VTAGNASSINDGAAAVMMMSESKAQELALPV-------LARIKAFASVGVDPA----LMGIAPVYATRRCLERAGWQLND 310
Cdd:cd00826 209 LTAGNACGLNDGAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 311 VDLIEVNEAFAAQAISVGKMLEWDPLR------------------VNVNGGAIALGHPIGASGCRILVSLVHEMKKRN-- 370
Cdd:cd00826 289 LDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAgk 368
|
410 420
....*....|....*....|....
gi 550763766 371 ---ARKGIATLCIGGGQGVALAIE 391
Cdd:cd00826 369 rqgAGAGLALLCIGGGGGAAMCIE 392
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
5-391 |
3.83e-83 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 258.16 E-value: 3.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 5 VIVGALRTAIGCFQGALARHSAVDLGSVVVRALverSGVAAHEIDEVILGQVLtaGAGQNPARQAALKGGLPNTVSAITI 84
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL---SKGMEREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 85 NDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHvltdsRTGAQLGNsqlldslvhdglwDAFNDYHMGVTAENL 164
Cdd:PRK06690 79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF-----QNRARFSP-------------ETIGDPDMGVAAEYV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 165 AREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVS-------TQRQNGEALIvdtdeqPRTDasaeglakldPAFE 237
Cdd:PRK06690 141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNglldesiKKEMNYERII------KRTK----------PAFL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 238 TLGSVTAGNASSINDGAAAVMMMSESKAQELAL-PVLARIKAfASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEV 316
Cdd:PRK06690 205 HNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEI 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550763766 317 NEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIE 391
Cdd:PRK06690 284 NEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-392 |
2.71e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 252.39 E-value: 2.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIG---CFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGA-GQNPARQAALKGGLP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 77 NTVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHvlTDSRTGAQLGNSQLLDSlVHDGLWDAFNDYH 156
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAA--MAAEDMAAGKPPLGMGS-GNLRLRALHPQSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 157 MGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVstQRQNGeALIVDTDEQPRTDASAEGLAKLDPAF 236
Cdd:PRK06025 158 QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV--YRDDG-SVALDHEEFPRPQTTAEGLAALKPAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 237 ETLGSVT--------------------------AGNASSINDGAAAVMMMSESKAQELALPVLARIKAFASVGVDPALMG 290
Cdd:PRK06025 235 TAIADYPlddkgttyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLML 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 291 IAPVYATRRCLERAGWQLNDVDLIEVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKRN 370
Cdd:PRK06025 315 NAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRG 394
|
410 420
....*....|....*....|..
gi 550763766 371 ARKGIATLCIGGGQGVALAIER 392
Cdd:PRK06025 395 LKRGLVTMCAAGGMAPAIIIER 416
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
270-392 |
1.11e-66 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 207.11 E-value: 1.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 270 LPVLARIKAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEVNEAFAAQAISVGKMLEWDPLRVNVNGGAIALGH 349
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 550763766 350 PIGASGCRILVSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.69e-62 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 206.67 E-value: 1.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGCFQGALARHSAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVS 80
Cdd:PRK09268 6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTD--SRTGAQLGNS-------QLLDSLVHDGLWDA 151
Cdd:PRK09268 86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEglRKILLELNRAkttgdrlKALGKLRPKHLAPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 152 F--ND-----YHMGVTAENLAREYGISRELQDAYALSSQQKARAAIDSGRFRDEIVPVstqrqngeaLIVDTDEQPRTDA 224
Cdd:PRK09268 166 IprNGeprtgLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF---------LGLTRDNNLRPDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 225 SAEGLAKLDPAFET--LGSVTAGNASSINDGAAAVMMMSESKAQELALPVLARIKAF--ASV----GVDPALMgiAPVYA 296
Cdd:PRK09268 237 SLEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetAAVdfvhGKEGLLM--APAYA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 297 TRRCLERAGWQLNDVDLIEVNEAFAAQAISVGKMLE-----------------WDPLRVNVNGGAIALGHPIGASGCRIL 359
Cdd:PRK09268 315 VPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEdeeycrerlgldaplgsIDRSKLNVNGSSLAAGHPFAATGGRIV 394
|
410 420 430
....*....|....*....|....*....|...
gi 550763766 360 VSLVHEMKKRNARKGIATLCIGGGQGVALAIER 392
Cdd:PRK09268 395 ATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
29-390 |
1.51e-20 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 89.81 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 29 LGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNtVSAITINDVCGSGLKALHLATQAIQCGEAD 108
Cdd:cd00327 10 LGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISG-GPAYSVNQACATGLTALALAVQQVQNGKAD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 109 VVIAGGqenmsraphvltdsrtgaqlgnsqlldslvhdglwdafndyhmgvtaenlareygisrelqdayalssqqkara 188
Cdd:cd00327 89 IVLAGG-------------------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 189 aidsgrfrdeivpvstqrqngealivdtdeqprtdasaeglakldpafetlgsvtaGNASSINDGAAAVMMMSESKAQEL 268
Cdd:cd00327 95 --------------------------------------------------------SEEFVFGDGAAAAVVESEEHALRR 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 269 ALPVLARIKAFASVGVD----PALMGIAPVYATRRCLERAGWQLNDVDLIEVNEAFAAQAISVGKMLEWDPLRVN---VN 341
Cdd:cd00327 119 GAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRspaVS 198
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 550763766 342 GGAIALGHPIGASGCRILVSLVHEMK-------KRNARKGIATLCIGGGQGVALAI 390
Cdd:cd00327 199 ATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
25-390 |
1.42e-18 |
|
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: 86.16 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 25 SAVDLGSVVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVsAITINDVCGSGLKALHLATQAIQC 104
Cdd:cd00829 15 SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKP-ATRVEAAGASGSAAVRAAAAAIAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 105 GEADVVIAGGQENMSRAPhvlTDSRTGAQLGNSQLLDSLVHDGLwdAFNDYHMGVTAENLAReYGISRElqdAYALSSQQ 184
Cdd:cd00829 94 GLADVVLVVGAEKMSDVP---TGDEAGGRASDLEWEGPEPPGGL--TPPALYALAARRYMHR-YGTTRE---DLAKVAVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 185 KARAAIDSGR--FRDEIvpvstqrqngealivDTDEQPRTDASAEGLAKLDpafetlgsvtagnASSINDGAAAVMMMSE 262
Cdd:cd00829 165 NHRNAARNPYaqFRKPI---------------TVEDVLNSRMIADPLRLLD-------------CCPVSDGAAAVVLASE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 263 SKAQELALPvLARIKAFAsVGVDPALMG--------IAPVYATRRCLERAGWQLNDVDLIEVNEAF-------------- 320
Cdd:cd00829 217 ERARELTDR-PVWILGVG-AASDTPSLSerddflslDAARLAARRAYKMAGITPDDIDVAELYDCFtiaellaledlgfc 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 321 ----AAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMKKR-------NARKGIATLCIGGGQGVALA 389
Cdd:cd00829 295 ekgeGGKLVREGDTAIGGDLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEagarqvpGARVGLAHNIGGTGSAAVVT 374
|
.
gi 550763766 390 I 390
Cdd:cd00829 375 I 375
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-374 |
3.64e-18 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 85.33 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGcfqgalaRHSAVDLGSVVVRALV---ERSGVAAHEIDEVILGQVLTAG-AGQ-NPARQAALKGGL 75
Cdd:PRK06064 1 MRDVAIIGVGQTKFG-------ELWDVSLRDLAVEAGLealEDAGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYAGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 76 PNtVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTDSRTGAQLgnsqlldslvhDGLWDAFndy 155
Cdd:PRK06064 74 AP-IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAG-----------DYEWEEF--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 156 hMGVTAENL----AR----EYGISRElqDAYALSSQQKARAAIDS-GRFRDEIvpvstqrqngealivDTDEQPRTDASA 226
Cdd:PRK06064 139 -FGATFPGLyaliARrymhKYGTTEE--DLALVAVKNHYNGSKNPyAQFQKEI---------------TVEQVLNSPPVA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 227 EGLAKLDpafetlgsvtagnASSINDGAAAVMMMSESKAQELAL-PVlaRIKAFASVGVDPAL------MGI-APVYATR 298
Cdd:PRK06064 201 DPLKLLD-------------CSPITDGAAAVILASEEKAKEYTDtPV--WIKASGQASDTIALhdrkdfTTLdAAVVAAE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 299 RCLERAGWQLNDVDLIEVNEAFA-AQAISV-----------GKMLEWDPLR------VNVNGGAIALGHPIGASGCRILV 360
Cdd:PRK06064 266 KAYKMAGIEPKDIDVAEVHDCFTiAEILAYedlgfakkgegGKLAREGQTYiggdipVNPSGGLKAKGHPVGATGVSQAV 345
|
410
....*....|....
gi 550763766 361 SLVHEMKKRnARKG 374
Cdd:PRK06064 346 EIVWQLRGE-AEKG 358
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-355 |
1.60e-12 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 68.44 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAIGcfqgalaRHSAVDLGSVVVRAL---VERSGVAAHEIDEVILGQVltaGAGQNP-ARQAALKG--- 73
Cdd:PRK07516 1 MMTASIVGWAHTPFG-------KLDAETLESLIVRVAreaLAHAGIAAGDVDGIFLGHF---NAGFSPqDFPASLVLqad 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 74 -GLPNtVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltdsrtGAQLGNSQLLDSLVHDGlwdaf 152
Cdd:PRK07516 71 pALRF-KPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP--------TAEVGDILLGASYLKEE----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 153 ndyhmGVTAENLAREYG-ISRELQDAYAlsSQQKARAAIdsgrfrdeivpVSTQRQNGealivdtdeqprtdaSAEGLAK 231
Cdd:PRK07516 137 -----GDTPGGFAGVFGrIAQAYFQRYG--DQSDALAMI-----------AAKNHANG---------------VANPYAQ 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 232 L--DPAFETLGSVTAGN-----------ASSINDGAAAVMMMSESKAQELALPVlaRIKAFASVG-------VDPALMGi 291
Cdd:PRK07516 184 MrkDLGFEFCRTVSEKNplvagplrrtdCSLVSDGAAALVLADAETARALQRAV--RFRARAHVNdflplsrRDPLAFE- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 292 APVYATRRCLERAGWQLNDVDLIEVNEAF------------------AAQAISVGKMLEWDPLRVNVNGGAIALGHPIGA 353
Cdd:PRK07516 261 GPRRAWQRALAQAGVTLDDLSFVETHDCFtiaelieyeamglappgqGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGA 340
|
..
gi 550763766 354 SG 355
Cdd:PRK07516 341 TG 342
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
34-369 |
1.73e-11 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 65.25 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 34 VRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALKGGLPNTVSaITINDVCGSGLKALHLATQAIQCGEADVVIAG 113
Cdd:PRK12578 29 IKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVP-LRVEAMCATGLAASLTAYTAVASGLVDMAIAV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 114 GQENMSRaphvlTDSRT----GAQLGNSQlldslvhdglWD------AFNDYHMGVTAENLAReYGISRElQDAYALSSQ 183
Cdd:PRK12578 108 GVDKMTE-----VDTSTslaiGGRGGNYQ----------WEyhfygtTFPTYYALYATRHMAV-YGTTEE-QMALVSVKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 184 QKARAAIDSGRFRDEIVpvstqrqngealivdTDEQPRTDASAEGLAKLDpafetlgsvtagnASSINDGAAAVMMMSES 263
Cdd:PRK12578 171 HKYGAMNPKAHFQKPVT---------------VEEVLKSRAISWPIKLLD-------------SCPISDGSATAIFASEE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 264 KAQELAL--PVLARIKAFASvgvDPALMGI--------APVYATRRCLERAGWQLNDVDLIEVNEAFAAQAISV------ 327
Cdd:PRK12578 223 KVKELKIdsPVWITGIGYAN---DYAYVARrgewvgfkATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGyedlgf 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 550763766 328 ------GKMLE------WDPLRVNVNGGAIALGHPIGASGcrilVSLVHEMKKR 369
Cdd:PRK12578 300 tekgkgGKFIEegqsekGGKVGVNLFGGLKAKGHPLGATG----LSMIYEITKQ 349
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
1-382 |
2.90e-08 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 55.08 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 1 MKDVVIVGALRTAigcFQGALARHSA--VDLGSVVVRALVERSGVAAHEIDEVILGQVltagAGQNPARQAALkGGLPNT 78
Cdd:PRK06289 2 SDDVWVLGGYQSD---FARNWTKEGRdfADLTREVVDGTLAAAGVDADDIEVVHVGNF----FGELFAGQGHL-GAMPAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 79 VS-------AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltDSRTGAQLGNSQLLDslvHDG---- 147
Cdd:PRK06289 74 VHpalwgvpASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVP----GDVAAEHLGAAAWTG---HEGqdar 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 148 -LW-DAFNDyhmgvTAENLAREYGISRElqDAYALSSQQKARAaidsgrfrdeivpvstqRQNGEAlivdtdeQPRT--- 222
Cdd:PRK06289 147 fPWpSMFAR-----VADEYDRRYGLDEE--HLRAIAEINFANA-----------------RRNPNA-------QTRGwaf 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 223 -DASAEGLAKLDPAFEtlGSVTAGNASSINDGAAAVMMMSESKAQELA-LPVLARIKAFasvGVDPALMGIAPVYA---- 296
Cdd:PRK06289 196 pDEATNDDDATNPVVE--GRLRRQDCSQVTDGGAGVVLASDAYLRDYAdARPIPRIKGW---GHRTAPLGLEQKLDrsag 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 297 -------TRRCLE----RAGWQLNDVDLIEVNEAFAA------------------QAISVGKMLEWDPLRVNVNGGAIAL 347
Cdd:PRK06289 271 dpyvlphVRQAVLdayrRAGVGLDDLDGFEVHDCFTPseylaidhigltgpgeswKAIENGEIAIGGRLPINPSGGLIGG 350
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 550763766 348 GHPIGASGCRILVSLVHEMKKR-------NARKGiATLCIGG 382
Cdd:PRK06289 351 GHPVGASGVRMLLDAAKQVTGTagdyqveGAKTF-GTLNIGG 391
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
32-114 |
2.85e-06 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 48.02 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 32 VVVRALVERSGVAAHEIDEVILGQVLTAGAGQNPARQAALK------------GGLPNTVS------------AITINDV 87
Cdd:pfam00109 93 EAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEdggprrgspfavGTMPSVIAgrisyflglrgpSVTVDTA 172
|
90 100
....*....|....*....|....*..
gi 550763766 88 CGSGLKALHLATQAIQCGEADVVIAGG 114
Cdd:pfam00109 173 CSSSLVAIHAAVQSIRSGEADVALAGG 199
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
28-355 |
2.20e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 46.04 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 28 DLGSVVVRALVERSGVAAHEIDEVILGQVltagAGQNPARQAALKG----GLPntvsAITINDVCGSGLKALHLATQAIQ 103
Cdd:PRK08256 24 DMAAEAGRAALADAGIDYDAVQQAYVGYV----YGDSTSGQRALYEvgmtGIP----IVNVNNNCSTGSTALFLARQAVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 104 CGEADVVIAGGQENMSraPHVLT---DSRTgaqlgnSQLLDslvHDGLWDAFNDYHMGVTAenlAREYGIS-RELQDAYA 179
Cdd:PRK08256 96 SGAADCALALGFEQMQ--PGALGsvwDDRP------SPLER---FDKALAELQGFDPAPPA---LRMFGGAgREHMEKYG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 180 LSSQQKARAAIDSGR---------FRDeivPVSTQRQNGEALIVDtdeqprtdasaeGLAKLdpafetlgsvtagNASSI 250
Cdd:PRK08256 162 TTAETFAKIGVKARRhaannpyaqFRD---EYTLEDVLASPMIWG------------PLTRL-------------QCCPP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 251 NDGAAAVMMMSESKAQELALPVLARIKA------FAS----------VGVDPALMGIAPVYatrrclERAGWQLNDVDLI 314
Cdd:PRK08256 214 TCGAAAAIVCSEEFARKHGLDRAVEIVAqamttdTPStfdgrsmidlVGYDMTRAAAQQVY------EQAGIGPEDIDVV 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550763766 315 EVNEAFAAQAI------------SVGKMLE---------WdplRVNVNGGAIALGHPIGASG 355
Cdd:PRK08256 288 ELHDCFSANELltyealglcpegEAEKFIDdgdntyggrW---VVNPSGGLLSKGHPLGATG 346
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
248-367 |
3.66e-05 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 45.65 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 248 SSINDGAAAVMMMSESKAQELALP----VLARIKAFASVG----VDP--ALMGIAPVYATRRCLERAGWQLNDVDLIEVN 317
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSpndsRLVEIKSLACASgnlyEDPpdATRMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550763766 318 EAF------------------AAQAISVGKMLEWDPLRVNVNGGAIALGHPIGASGCRILVSLVHEMK 367
Cdd:PTZ00455 336 DCFtiaellmyealgiaeyghAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
81-114 |
3.81e-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: 45.63 E-value: 3.81e-05
10 20 30
....*....|....*....|....*....|....
gi 550763766 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGG 114
Cdd:cd00833 163 SLTVDTACSSSLVALHLACQSLRSGECDLALVGG 196
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
242-390 |
1.14e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 44.13 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 242 VTAGNASSINDGAAAVMMMSESKAQELA-LPVlaRIKAFASvGVD----------------------------PALMGI- 291
Cdd:PRK06365 217 LTRLDVCAMSDGAACAILASEDKAFEITdKPV--LIKAIGT-GSDtlrladrpfgevpllpnespddykdlryPGVHSFr 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 292 APVYATRRCLERAGWQ--LNDVDLIEVNEAFAA------------------QAISVGKMLEWDPLRVNVNGGAIALGHPI 351
Cdd:PRK06365 294 AGRMAAKEAYEMAGITdpLNDLDLIELHDAYTSseiqtyedlglckygeggQFIESGKPELPGKLPVNPSGGLLAAGHAV 373
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 550763766 352 GASGCR----ILVSLVHEMKK---------RNARKGIATLCIGGGQGVALAI 390
Cdd:PRK06365 374 GATGIMqavfMFWQLQGRIKKhfhddylqvKNAKRGLIHSHAGTGTYVTVTI 425
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
61-114 |
2.47e-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: 2.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550763766 61 AGQNPARqaaLKG-------GLPNTVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGG 114
Cdd:smart00825 66 AGIDPES---LRGsrtgvfvGVSSSDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
25-120 |
6.21e-04 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 41.25 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 25 SAVDLGSVVVRALVERSGVAAHEIDEVILG-----QVLTAGAgqnpAR-QAALkgGLPNTVsAITINDVCGSGLKALHLA 98
Cdd:COG0332 50 TTSDLAVEAARKALEAAGIDPEDIDLIIVAtvtpdYLFPSTA----CLvQHKL--GAKNAA-AFDINAACSGFVYALSVA 122
|
90 100
....*....|....*....|...
gi 550763766 99 TQAIQCGEAD-VVIAGGqENMSR 120
Cdd:COG0332 123 AALIRSGQAKnVLVVGA-ETLSR 144
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
176-355 |
8.68e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 41.21 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 176 DAYALSSQQkARAAIDSGRFR----DEIVPVST---QRQNGEALIVDTDEQPRTDASAEGLAKLDPAfetlgsvtagnas 248
Cdd:PRK07937 137 DSVSMAGLQ-ARAGLDAGKWTeeqmAEVAARSRadaRRNPSAEPSISVDELLARPYFADPLRRHDIA------------- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 249 SINDGAAAVMMMSESKAQELAlPVLARIKAFASvGVDPALMG---IAPVYATRRCLERA-GWQLNDVDLIEVNEAFAAQA 324
Cdd:PRK07937 203 PITDGAAAVVLAAGDRARELR-ERPAWITGIEH-RIESPSLGardLTRSPSTALAAEAAtGGDAGGVDVAELHAPFTHQE 280
|
170 180 190
....*....|....*....|....*....|..
gi 550763766 325 ISVGKMLEW-DPLRVNVNGGAIAlGHPIGASG 355
Cdd:PRK07937 281 LILREALGLgDKTKVNPSGGALA-ANPMFAAG 311
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
82-119 |
1.03e-03 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 40.89 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|....*...
gi 550763766 82 ITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMS 119
Cdd:cd00828 156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
20-120 |
1.14e-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: 40.60 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 20 ALARHSAVDLGSVVVRALVERSGVAAHEIDEVILgqvltagAGQNPAR---------QAALkgGLPNTVsAITINDVCGS 90
Cdd:cd00830 44 ADPGETTSDLAVEAAKKALEDAGIDADDIDLIIV-------ATSTPDYlfpataclvQARL--GAKNAA-AFDINAACSG 113
|
90 100 110
....*....|....*....|....*....|
gi 550763766 91 GLKALHLATQAIQCGEADVVIAGGQENMSR 120
Cdd:cd00830 114 FLYGLSTAAGLIRSGGAKNVLVVGAETLSR 143
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
81-114 |
1.27e-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: 1.27e-03
10 20 30
....*....|....*....|....*....|....
gi 550763766 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGG 114
Cdd:COG3321 167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGG 200
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
252-355 |
1.64e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 40.42 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550763766 252 DGAAAVMMMSESKAQELALPVLARIKAF-----ASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLI-------EVNEA 319
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQ 289
|
90 100 110
....*....|....*....|....*....|....*.
gi 550763766 320 FAAQAISvgkmlEWDPLRVNVNGGAIALGHPIGASG 355
Cdd:PRK05952 290 REANLIQ-----ALFPHRVAVSSTKGATGHTLGASG 320
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
65-116 |
3.63e-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: 39.06 E-value: 3.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 550763766 65 PARQAALKGGLPNTVsaITINDVCGSGLKALHLATQAIQCGEADVVIAGGQE 116
Cdd:cd00834 140 AAGQVAIRLGLRGPN--YTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
71-116 |
4.26e-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: 38.92 E-value: 4.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 550763766 71 LKGGLPNTVSAitindvCGSGLKALHLATQAIQCGEADVVIAGGQE 116
Cdd:COG0304 150 LKGPNYTVSTA------CASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| |
