|
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: 677.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLG 239
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVtIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 240 SVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEAF 319
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588633 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIERD 392
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-391 |
0e+00 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 593.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDAdNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNA-KLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGS 240
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 241 VTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEAFA 320
Cdd:COG0183 240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446588633 321 AQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:COG0183 320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-392 |
0e+00 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 586.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLG 239
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIlIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 240 SVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEAF 319
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588633 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIERD 392
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIERD 393
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-391 |
0e+00 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 580.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 5 VIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAITI 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 85 NDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDAdNLVDSLVHDGLWDAFNDYHIGVTAENL 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGL-NTLDGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 165 AREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGSVTAG 244
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 245 NASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEAFAAQAL 324
Cdd:cd00751 240 NASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQAL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446588633 325 SVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:cd00751 320 ACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-390 |
1.62e-174 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 491.36 E-value: 1.62e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 6 IVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAITIN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 86 DVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGAL-PDADNLVDSLVHDgLWDAFNDYHIGVTAENL 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 165 AREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGSVTAG 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 245 NASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEAFAAQAL 324
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446588633 325 SVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-390 |
3.94e-151 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 432.60 E-value: 3.94e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLG 239
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVtIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 240 SVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEAF 319
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446588633 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-391 |
1.43e-148 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 425.91 E-value: 1.43e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVL-TAGAGQNPARQSAIKGGLPTTV 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpTEPRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVhDGLWDAFNDYHIGV 159
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMV-GALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 160 TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAF-DSL 238
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFkKEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 239 GSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEA 318
Cdd:PRK09051 241 GTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588633 319 FAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK09051 321 FAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-391 |
4.71e-145 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 417.19 E-value: 4.71e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 2 KEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSA 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 82 ITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVTA 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 162 ENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVP--IVTQRNGQTAIVDTDEQPrADASAEGLALLHPAFDS-L 238
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPveVPGGRGRPSVIVDKDEGL-GKFDPAKLRKLRPSFKEdG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 239 GSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEA 318
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588633 319 FAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.39e-141 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 408.61 E-value: 1.39e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQvlTAGAGQNPA--RQSAIKGGLPTT 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDadnlvDSLVHDGLWDA---FNDY 155
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGG-----GVQLHDRLARGretAGGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 156 HIGV------TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGL 228
Cdd:PRK06205 154 RFPVpggmieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVtVPQRKGDPTVVDRDEHPRADTTLESL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 229 ALLHP---AFDSLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGW 305
Cdd:PRK06205 234 AKLRPimgKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 306 QLAEVDLIEANEAFAAQALSVGKMLEW---DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGG 382
Cdd:PRK06205 314 TLDDIDLIELNEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGG 393
|
....*....
gi 446588633 383 QGVALTIER 391
Cdd:PRK06205 394 QGLAAVFER 402
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-390 |
1.51e-140 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 405.57 E-value: 1.51e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVlNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHG-SYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGS 240
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDKNGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 241 VTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEAFA 320
Cdd:PRK06633 241 VTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 321 AQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06633 321 AQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-391 |
3.49e-134 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 389.70 E-value: 3.49e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERT-GVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLPTT 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLND-----SRTGALPDAD---NLVDSLVHDglwd 150
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKadsafSRQAEIFDTTigwRFVNPLMKA---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 151 afndyHIGV-----TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADAS 224
Cdd:PRK09050 157 -----QYGVdsmpeTAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVtIPQKKGDPVVVDRDEHPRPETT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 225 AEGLALLHPAFDSLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAG 304
Cdd:PRK09050 232 LEALAKLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 305 WQLAEVDLIEANEAFAAQALSVGKMLEW--DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGG 382
Cdd:PRK09050 312 LTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVG 391
|
....*....
gi 446588633 383 QGVALTIER 391
Cdd:PRK09050 392 QGIALAIER 400
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-391 |
6.05e-123 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 360.43 E-value: 6.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHS-AVELGSMVVKALIERT-GVDANAIDEVILGQVL-TAGAGQNPARQSAIKGGLPT 77
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAFRNVrAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQqTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 78 TVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSrapHVlndsrtgalpDADNLVDSLVHDGLWDAFNDYHI 157
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMG---HV----------PMNHGVDFHPGLSKNVAKAAGMM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 158 GVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQ-RNGQTAIVDTDEQPRADASAEGLALLHPAFD 236
Cdd:PRK08947 148 GLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHdADGVLKLFDYDEVIRPETTVEALAALRPAFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 237 SL-GSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEA 315
Cdd:PRK08947 228 PVnGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446588633 316 NEAFAAQALSVGK---MLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK08947 308 NEAFAAQSLPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFER 386
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-391 |
2.22e-122 |
|
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.
Pssm-ID: 131483 Cd Length: 400 Bit Score: 359.87 E-value: 2.22e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 2 KEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERT-GVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLPTTV 79
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTgALPDADNLVDS-----LVHDGLWDAFND 154
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADS-AFSRSAKIEDTtigwrFINPLMKALYGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 155 YHIGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHP 233
Cdd:TIGR02430 160 DSMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVvIPQKKGEPTVVDQDEHPRPETTLEGLAKLKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 234 AFDSLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLI 313
Cdd:TIGR02430 240 VVRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 314 EANEAFAAQALSVGKMLEW--DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:TIGR02430 320 ELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-262 |
3.78e-119 |
|
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: 346.21 E-value: 3.78e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 4 VVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAIT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLN-DSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVTAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 163 NLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTaIVDTDEQPRADASAEGLALLHPAFDSLGSV 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVtVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
|
250 260
....*....|....*....|.
gi 446588633 242 TAGNASSINDGAAAVMMMSEA 262
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-391 |
4.76e-118 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 348.28 E-value: 4.76e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIG-CFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVL-TAGAGQNPARQSAIKGGLPTT 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP---HVLNDSRTgalpdadnlvdslvhdgLWDAFNDY 155
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPmmgHVVRPNPR-----------------LVEAAPEY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 156 HIGV--TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQR----NGQ----TAIVDTDEQPRADAS 224
Cdd:PRK07661 144 YMGMghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVdVTLRtvgeNNKlqeeTITFSQDEGVRADTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 225 AEGLALLHPAFDSLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAG 304
Cdd:PRK07661 224 LEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 305 WQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQG 384
Cdd:PRK07661 304 LELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMG 383
|
....*..
gi 446588633 385 VALTIER 391
Cdd:PRK07661 384 AAGVFEL 390
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-391 |
3.85e-115 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 340.93 E-value: 3.85e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCF------QGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLtaGAGQN---PARQSAI 71
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFrpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENwlyGGRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 72 KGGLPTTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLN---DSRTGALPDADnlvdsLVHdgl 148
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphiEPNPKLLTDPK-----YIE--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 149 WDAFNDYHIGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGL 228
Cdd:PRK06445 151 YDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 229 ALLHPAFDSLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLA 308
Cdd:PRK06445 231 AKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 309 EVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALT 388
Cdd:PRK06445 311 DIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVV 390
|
...
gi 446588633 389 IER 391
Cdd:PRK06445 391 LER 393
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-390 |
6.71e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 333.01 E-value: 6.71e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK06954 6 QDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYH-IGV 159
Cdd:PRK06954 86 CTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 160 TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRAdASAEGLALLHPAFDSLG 239
Cdd:PRK06954 166 FAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAFSKTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 240 SVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEAF 319
Cdd:PRK06954 245 TVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAF 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446588633 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06954 325 AVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-390 |
2.19e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 331.20 E-value: 2.19e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVL-NDSRTGA---LPDADNLVDSLVHDGLWDAFNDYH 156
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPkhlLHKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 157 IGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTqrngqtaiVDTDEQPRaDASAEGLALLHPAFD 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND--------LDRDEGIR-KTTMEDLAKLPPAFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 237 SLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEAN 316
Cdd:PRK06366 232 KNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446588633 317 EAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06366 312 EAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-391 |
5.16e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 330.69 E-value: 5.16e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQ--GTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAG-AGQNPARQSAIKGGLPT 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 78 TVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvlnDSRTGALPdadnlVDSLVhdglwdAFNDYHI 157
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPM---GSDGGAWA-----MDPST------NFPTYFV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 158 --GVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPiVTQRNGQTaIVDTDEQPRADASAEGLALLHPAF 235
Cdd:PRK08242 147 pqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVP-VKDQNGLT-ILDHDEHMRPGTTMESLAKLKPSF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 236 DSLGSV---------------------TAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVY 294
Cdd:PRK08242 225 AMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 295 ATRRCLERAGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGL 374
Cdd:PRK08242 305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTAL 384
|
410
....*....|....*..
gi 446588633 375 ATLCIGGGQGVALTIER 391
Cdd:PRK08242 385 ITLCVGGGMGIATIIER 401
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-392 |
8.11e-111 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 332.11 E-value: 8.11e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 3 EVVIVGALRTPI-----GCFQGTLArhsaVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQ-NPARQSAIKGGLP 76
Cdd:PLN02287 47 DVVIVAAYRTPIckakrGGFKDTYP----DDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 77 TTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHdglwdafndyh 156
Cdd:PLN02287 123 ETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP----------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 157 IGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQR------NGQTAIVDTDEQPRADASAEGLAL 230
Cdd:PLN02287 192 MGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIvdpktgEEKPIVISVDDGIRPNTTLADLAK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 231 LHPAFDSLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEV 310
Cdd:PLN02287 272 LKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 311 DLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKR--DARKGLATLCIGGGQGVALT 388
Cdd:PLN02287 352 DLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRgkDCRFGVVSMCIGTGMGAAAV 431
|
....
gi 446588633 389 IERD 392
Cdd:PLN02287 432 FERG 435
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-391 |
1.09e-107 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 321.95 E-value: 1.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAV-ELGSMVVKALIERT-GVDANAIDEVILGQVL-TAGAGQNPARQSAIKGGLPT 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGKAPRGMFKNTRPdDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 78 TVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLND-SRTGALPDADNLVDSLvhdglwdafndYH 156
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKpSMSPAIFARDENVGIA-----------YG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 157 IGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQR-----NGQTAI----VDTDEQPRADASAE 226
Cdd:PRK09052 154 MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYeITERfpdlaTGEVDVktrtVDLDEGPRADTSLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 227 GLALLHPAFDSLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQ 306
Cdd:PRK09052 234 GLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 307 LAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVA 386
Cdd:PRK09052 314 QDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAA 393
|
....*
gi 446588633 387 LTIER 391
Cdd:PRK09052 394 GIFER 398
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.93e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 316.17 E-value: 2.93e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIG-CFQGTLARHSAVELGSMVVKALIERT-GVDANAIDEVILGQVLTAG-AGQNPARQSAIKGGLPT 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 78 tVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSrtgaLPDADNLV---------------DS 142
Cdd:PRK07851 81 -LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDS----LPDTKNPLfaeaqartaaraeggAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 143 LVHDGLWD-AFNDYHI--GVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPiVTQRNGqtAIVDTDEQP 219
Cdd:PRK07851 156 AWHDPREDgLLPDVYIamGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITP-VTLPDG--TVVSTDDGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 220 RADASAEGLALLHPAFDSLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRC 299
Cdd:PRK07851 233 RAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 300 LERAGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCI 379
Cdd:PRK07851 313 LARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCV 392
|
410
....*....|..
gi 446588633 380 GGGQGVALTIER 391
Cdd:PRK07851 393 GGGQGMAMVLER 404
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-391 |
9.26e-105 |
|
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: 314.19 E-value: 9.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 3 EVVIVGALRTPIGCFQGTLARHSAVE-LGSMVVKALIER-TGVDANAIDEVILGQV-LTAGAGQNPARQSAIKGGLPTTV 79
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTRAEdLSAHLMSKLLARnPKVDPAEVEDIYWGCVqQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvlndsrtgalpdADNLVDSLVHDGLWDAFNDYHIGV 159
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP-------------MMHGVDFHPGMSLHVAKAAGMMGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 160 TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQ-RNGQTAIVDTDEQPRADASAEGLALLHPAFDSL 238
Cdd:TIGR02445 148 TAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHdADGFLKQFDYDEVIRPETTVESLAALRPAFDPK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 239 -GSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANE 317
Cdd:TIGR02445 228 nGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446588633 318 AFAAQALSVGK---MLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:TIGR02445 308 AFAAQALPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-391 |
3.06e-104 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 313.25 E-value: 3.06e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLPTTV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDAdNLVDSLV-----HDGLWDAFND 154
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDA-KVFDTTIgarfpNPKIVAQYGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 155 YHIGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIV--TQRNGQTAIVDTDEQPRADASAEGLALLH 232
Cdd:PRK08131 160 DSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEvpQGRKLPPKLVAEDEHPRPSSTVEALTKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 233 PAFDSlGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDL 312
Cdd:PRK08131 240 PLFEG-GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 313 IEANEAFAAQALSVGKML--EWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK08131 319 IEINEAFASQVLGCLKGLgvDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
.
gi 446588633 391 R 391
Cdd:PRK08131 399 R 399
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-391 |
9.50e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 306.25 E-value: 9.50e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAG--AGqNPARQSAIKGGLPTT 78
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpqAG-NIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvLNDSRTGALPDAdnLVDSLVHDGLWDA-FNDYHI 157
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTAGEQLG--FTSPFAESKGWLHrYGDQEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 158 G--VTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIvtqrngqtAIVDTDEQPRaDASAEGLALLHPAF 235
Cdd:PRK07801 156 SqfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV--------GGVTVDEGPR-ETSLEKMAGLKPLV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 236 DSlGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEA 315
Cdd:PRK07801 227 EG-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEI 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446588633 316 NEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK07801 306 NEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-391 |
1.91e-100 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 303.18 E-value: 1.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLPTTV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADnlvdslvhDGLWDAFNDYhigV 159
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPRPD--------SWDIDMPNQF---E 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 160 TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVT-------QRNGQTAIVDTDEQPRaDASAEGLALLH 232
Cdd:PRK07850 150 AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQApvldeegQPTGETRLVTRDQGLR-DTTMEGLAGLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 233 PAFDSlGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDL 312
Cdd:PRK07850 229 PVLEG-GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446588633 313 IEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK07850 308 VEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-391 |
5.76e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 298.08 E-value: 5.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPD---ADNLVDSLVH------------ 145
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWLAGwyaAKSIGQKLAAlgklrpsylapv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 146 ----DGLWDAFNDYHIGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKdEIVPIVTqRNGQtaIVDTDEQPRA 221
Cdd:PRK08170 162 igllRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFD-RDGK--FYDHDDGVRP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 222 DASAEGLALLHPAFDS-LGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCL 300
Cdd:PRK08170 238 DSSMEKLAKLKPFFDRpYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 301 ERAGWQLAEVDLIEANEAFAAQALSV-----------------GKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVH 363
Cdd:PRK08170 318 QRHGLTLEDLDLWEINEAFAAQVLAClaawadeeycreqlgldGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLH 397
|
410 420
....*....|....*....|....*...
gi 446588633 364 EMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK08170 398 ALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-391 |
4.97e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 294.71 E-value: 4.97e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAG-AGQNPARQSAIKGGLPTTV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNdsrtGALPdADNLVDSLVHDGLWDAFNDYHIG- 158
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP----STLP-AKNGLGHYKSPGMEERYPGIQFSq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 159 -VTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHPAFD 236
Cdd:PRK06504 156 fTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLeITRADGSGEMHTVDEGIRFDATLEGIAGVKLIAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 237 SlGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEAN 316
Cdd:PRK06504 236 G-GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVN 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446588633 317 EAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK06504 315 EAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-392 |
1.14e-91 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 282.26 E-value: 1.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 4 VVIVGALRTPigcF--QGTLARH-SAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK08963 7 IAIVSGLRTP---FakQATAFHGiPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP--------HVLND-SRTGALPDADNLVDSLvhdGLWD- 150
Cdd:PRK08963 84 AYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaRALVDlNKARTLGQRLKLFSRL---RLRDl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 151 -----AFNDYHIGV----TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTaiVDTDEQPRA 221
Cdd:PRK08963 161 lpvppAVAEYSTGLrmgdTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQP--LEEDNNIRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 222 DASAEGLALLHPAFD-SLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDP---ALMGiaPVYATR 297
Cdd:PRK08963 239 DSTLEDYAKLRPAFDrKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwqdMLLG--PAYATP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 298 RCLERAGWQLAEVDLIEANEAFAAQALSVGKML-----------------EWDERRVNVNGGAIALGHPIGASGCRILVS 360
Cdd:PRK08963 317 LALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQ 396
|
410 420 430
....*....|....*....|....*....|..
gi 446588633 361 LVHEMVKRDARKGLATLCIGGGQGVALTIERD 392
Cdd:PRK08963 397 TLHELRRRGGGLGLTTACAAGGLGAAMVLEVE 428
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-386 |
3.55e-91 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 279.73 E-value: 3.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIG-CFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLPTT 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTgalpdADNLVDSLVHDGLWDAFNdyhig 158
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHML-----REGWLVEHKPEIYWSMLQ----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 159 vTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIvTQRNG-----------QTAIVDTDEQPRADASAEG 227
Cdd:PRK07108 151 -TAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPI-TVTAGvadkatgrlftKEVTVSADEGIRPDTTLEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 228 LALLHPAFDSlGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQL 307
Cdd:PRK07108 229 VSKIRSALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKV 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446588633 308 AEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVA 386
Cdd:PRK07108 308 DDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-390 |
1.44e-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: 270.52 E-value: 1.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 7 VGALRTPIGCFQGTLARHS---AVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAIT 83
Cdd:cd00826 1 AGAAMTAFGKFGGENGADAndlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAphvlndSRTGALpdadnlvdslvhdglwdafnDYHIGVtaen 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETS------AENNAK--------------------EKHIDV---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 164 LAREYGiSRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDE--QPRADASAEGLALLHPAFDSLGSV 241
Cdd:cd00826 131 LINKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEyiQFGDEASLDEIAKLRPAFDKEDFL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 242 TAGNASSINDGAAAVMMMSEAKAQ-------ALGLPVLARIRAFASVGVDPA----LMGIAPVYATRRCLERAGWQLAEV 310
Cdd:cd00826 210 TAGNACGLNDGAAAAILMSEAEAQkhglqskAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 311 DLIEANEAFAAQALSVGKMLEWDERR------------------VNVNGGAIALGHPIGASGCRILVSLVHEMVKRD--- 369
Cdd:cd00826 290 DLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAgkr 369
|
410 420
....*....|....*....|...
gi 446588633 370 --ARKGLATLCIGGGQGVALTIE 390
Cdd:cd00826 370 qgAGAGLALLCIGGGGGAAMCIE 392
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-390 |
5.27e-82 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 255.08 E-value: 5.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 3 EVVIVGALRTPIGCFQGTLARHSAVELGSMVVKAL---IERtgvdanAIDEVILGQVLtaGAGQNPARQSAIKGGLPTTV 79
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFLskgMER------EIDDVILGNVV--GPGGNVARLSALEAGLGLHI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvlnDSRTGALPDAdnlvdslvhdglwdaFNDYHIGV 159
Cdd:PRK06690 74 PGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF---QNRARFSPET---------------IGDPDMGV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 160 TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVP--------IVTQRNGQTAIvdtdeqPRADasaeglall 231
Cdd:PRK06690 136 AAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSfnglldesIKKEMNYERII------KRTK--------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 232 hPAFDSLGSVTAGNASSINDGAAAVMMMSEAKAQALGL-PVLARIRAfASVGVDPALMGIAPVYATRRCLERAGWQLAEV 310
Cdd:PRK06690 201 -PAFLHNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 311 DLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06690 279 DYFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-391 |
5.65e-82 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 257.01 E-value: 5.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIG---CFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 77 TTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMS-RAPHVLNDSRTGALP---DADNLVDSLVHDglwdaf 152
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGKPPlgmGSGNLRLRALHP------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 153 nDYHIGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVtqRNGQTAIVDTDEQPRADASAEGLALLH 232
Cdd:PRK06025 155 -QSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY--RDDGSVALDHEEFPRPQTTAEGLAALK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 233 PAFDSLGSVT--------------------------AGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAFASVGVDPA 286
Cdd:PRK06025 232 PAFTAIADYPlddkgttyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 287 LMGIAPVYATRRCLERAGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMV 366
Cdd:PRK06025 312 LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELE 391
|
410 420
....*....|....*....|....*
gi 446588633 367 KRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK06025 392 RRGLKRGLVTMCAAGGMAPAIIIER 416
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
269-391 |
9.11e-67 |
|
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: 207.49 E-value: 9.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 269 LPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGH 348
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446588633 349 PIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-391 |
3.55e-60 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 200.51 E-value: 3.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK09268 6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPD---ADNLVDSLvhdGLWDAFNDYHI 157
Cdd:PRK09268 86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLElnrAKTTGDRL---KALGKLRPKHL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 158 GVT----------------AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIvtqrNGqtaiVDTDEQPRA 221
Cdd:PRK09268 163 APEiprngeprtglsmgehAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF----LG----LTRDNNLRP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 222 DASAEGLALLHPAFD--SLGSVTAGNASSINDGAAAVMMMSEAKAQALGLPVLARIRAF--ASV----GVDPALMgiAPV 293
Cdd:PRK09268 235 DSSLEKLAKLKPVFGkgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetAAVdfvhGKEGLLM--APA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 294 YATRRCLERAGWQLAEVDLIEANEAFAAQALSVGKMLEWDE-----------------RRVNVNGGAIALGHPIGASGCR 356
Cdd:PRK09268 313 YAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEycrerlgldaplgsidrSKLNVNGSSLAAGHPFAATGGR 392
|
410 420 430
....*....|....*....|....*....|....*
gi 446588633 357 ILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK09268 393 IVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
26-389 |
1.57e-23 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 98.29 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 26 AVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTtVSAITINDVCGSGLKALHLATQAIQCG 105
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISG-GPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 106 EADIVIAGGqenmsraphvlndsrtgalpdadnlvdslvhdglwdafndyhigvtaenlareygisrelqdayalssqqk 185
Cdd:cd00327 86 KADIVLAGG----------------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 186 araaidtgrfkdeivpivtqrngqtaivdtdeqpradasaeglallhpafdslgsvtaGNASSINDGAAAVMMMSEAKAQ 265
Cdd:cd00327 95 ----------------------------------------------------------SEEFVFGDGAAAAVVESEEHAL 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 266 ALGLPVLARIRAFASVGVD----PALMGIAPVYATRRCLERAGWQLAEVDLIEANEAFAAQALSVGKMLEWDE---RRVN 338
Cdd:cd00327 117 RRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPdgvRSPA 196
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446588633 339 VNGGAIALGHPIGASGCRILVSLVHEM-------VKRDARKGLATLCIGGGQGVALTI 389
Cdd:cd00327 197 VSATLIMTGHPLGAAGLAILDELLLMLehefippTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-373 |
5.02e-17 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 81.87 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGCFQGTLARHSAVELGsmvVKAlIERTGVDANAIDEVILGQVLTAG-AGQ-NPARQSAIKGGLpTT 78
Cdd:PRK06064 1 MRDVAIIGVGQTKFGELWDVSLRDLAVEAG---LEA-LEDAGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYAGL-AP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvlndsrtgalPDADNLVDSLVhDGLWDAFNdyhiG 158
Cdd:PRK06064 76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPT----------PDATEAIARAG-DYEWEEFF----G 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 159 VTAENL----AR----EYGISRE------LQDAYALSSQQKARaaidtgrFKDEIvpivtqrngqtaivDTDEQPRADAS 224
Cdd:PRK06064 141 ATFPGLyaliARrymhKYGTTEEdlalvaVKNHYNGSKNPYAQ-------FQKEI--------------TVEQVLNSPPV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 225 AEGLALLHpafdslgsvtagnASSINDGAAAVMMMSEAKA--------------QALGLPVLARIRAFASVGvdpalmgi 290
Cdd:PRK06064 200 ADPLKLLD-------------CSPITDGAAAVILASEEKAkeytdtpvwikasgQASDTIALHDRKDFTTLD-------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 291 APVYATRRCLERAGWQLAEVDLIEANEAFA-AQALSV-----------GKMLEWDERR------VNVNGGAIALGHPIGA 352
Cdd:PRK06064 259 AAVVAAEKAYKMAGIEPKDIDVAEVHDCFTiAEILAYedlgfakkgegGKLAREGQTYiggdipVNPSGGLKAKGHPVGA 338
|
410 420
....*....|....*....|.
gi 446588633 353 SGCRILVSLVHEMvKRDARKG 373
Cdd:PRK06064 339 TGVSQAVEIVWQL-RGEAEKG 358
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
25-389 |
8.02e-15 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 74.99 E-value: 8.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 25 SAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLpTTVSAITINDVCGSGLKALHLATQAIQC 104
Cdd:cd00829 15 SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGL-LGKPATRVEAAGASGSAAVRAAAAAIAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 105 GEADIVIAGGQENMSRAPhvlndSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVTAENLAReYGISRElqdAYALSSQQ 184
Cdd:cd00829 94 GLADVVLVVGAEKMSDVP-----TGDEAGGRASDLEWEGPEPPGGLTPPALYALAARRYMHR-YGTTRE---DLAKVAVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 185 KARAAIDTGR--FKDEIvpivtqrngqtaivDTDEQPRADASAEGLALLHpafdslgsvtagnASSINDGAAAVMMMSEA 262
Cdd:cd00829 165 NHRNAARNPYaqFRKPI--------------TVEDVLNSRMIADPLRLLD-------------CCPVSDGAAAVVLASEE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 263 KAQALGLPvLARIRAFAsVGVDPALMG--------IAPVYATRRCLERAGWQLAEVDLIE------ANEAFAAQAL---- 324
Cdd:cd00829 218 RARELTDR-PVWILGVG-AASDTPSLSerddflslDAARLAARRAYKMAGITPDDIDVAElydcftIAELLALEDLgfce 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 325 --SVGKMLEWDERR------VNVNGGAIALGHPIGASGcrilVSLVHEMVK-----------RDARKGLATLCIGGGQGV 385
Cdd:cd00829 296 kgEGGKLVREGDTAiggdlpVNTSGGLLSKGHPLGATG----LAQAVEAVRqlrgeagarqvPGARVGLAHNIGGTGSAA 371
|
....
gi 446588633 386 ALTI 389
Cdd:cd00829 372 VVTI 375
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-386 |
7.15e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 59.96 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 1 MKEVVIVGALRTPIGcfqgtlaRHSAVELGSMVVKAL---IERTGVDANAIDEVILGQvLTAGAGQNPARQSAIKGGLPT 77
Cdd:PRK07516 1 MMTASIVGWAHTPFG-------KLDAETLESLIVRVAreaLAHAGIAAGDVDGIFLGH-FNAGFSPQDFPASLVLQADPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 78 T--VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvlNDSRTGALPDADNLV-DSLVHDGLWDAFnd 154
Cdd:PRK07516 73 LrfKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP---TAEVGDILLGASYLKeEGDTPGGFAGVF-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 155 yhiGVTAENLAREYGisrelqdayalsSQQKARAAIdtgrfkdeivpivTQRNGQTAIVDTDEQPRADASaeglallhpa 234
Cdd:PRK07516 148 ---GRIAQAYFQRYG------------DQSDALAMI-------------AAKNHANGVANPYAQMRKDLG---------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 235 FDSLGSVTAGN-----------ASSINDGAAAVMMMSEAKAQALGLPVlaRIRAFASVG-------VDPALMGiAPVYAT 296
Cdd:PRK07516 190 FEFCRTVSEKNplvagplrrtdCSLVSDGAAALVLADAETARALQRAV--RFRARAHVNdflplsrRDPLAFE-GPRRAW 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 297 RRCLERAGWQLAEVDLIEANEAF------------------AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASG---- 354
Cdd:PRK07516 267 QRALAQAGVTLDDLSFVETHDCFtiaelieyeamglappgqGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATGvsmh 346
|
410 420 430
....*....|....*....|....*....|....*
gi 446588633 355 ---CRILVSLVHEMVKRDARkgLATLCIGGGQGVA 386
Cdd:PRK07516 347 vlaAMQLTGEAGGMQIPGAK--LAGVFNMGGAAVA 379
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
28-368 |
9.48e-09 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 56.78 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 28 ELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPA----RQSAIKGGLPTTVSAitindVCGSGLKALHLATQAIQ 103
Cdd:PRK12578 23 ELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPApivaEYSGLTGKVPLRVEA-----MCATGLAASLTAYTAVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 104 CGEADIVIAGGQENMSRAphvlnDSRTgalpdadnlvdSLVHDG-----LWD------AFNDYHIGVTAENLAReYGISR 172
Cdd:PRK12578 98 SGLVDMAIAVGVDKMTEV-----DTST-----------SLAIGGrggnyQWEyhfygtTFPTYYALYATRHMAV-YGTTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 173 ElQDAYALSSQQKARAAIDTGRFKDEIVpivtqrngqtaivdTDEQPRADASAEGLALLhpafdslgsvtagNASSINDG 252
Cdd:PRK12578 161 E-QMALVSVKAHKYGAMNPKAHFQKPVT--------------VEEVLKSRAISWPIKLL-------------DSCPISDG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 253 AAAVMMMSEAKAQALGL--PVLARIRAFASvgvDPALMGI--------APVYATRRCLERAGWQLAEVDLIEANEAFA-A 321
Cdd:PRK12578 213 SATAIFASEEKVKELKIdsPVWITGIGYAN---DYAYVARrgewvgfkATQLAARQAYNMAKVTPNDIEVATVHDAFTiA 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446588633 322 QALSV-----------GKMLEWDERR------VNVNGGAIALGHPIGASGcrilVSLVHEMVKR 368
Cdd:PRK12578 290 EIMGYedlgftekgkgGKFIEEGQSEkggkvgVNLFGGLKAKGHPLGATG----LSMIYEITKQ 349
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
81-114 |
3.67e-05 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 44.93 E-value: 3.67e-05
10 20 30
....*....|....*....|....*....|....
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:pfam00109 166 SVTVDTACSSSLVAIHAAVQSIRSGEADVALAGG 199
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
34-354 |
4.13e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 45.27 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 34 VKALIERTGVDANAIDEVILGQVltagAGQNPARQSAIKGGLPTTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAG 113
Cdd:PRK08256 30 GRAALADAGIDYDAVQQAYVGYV----YGDSTSGQRALYEVGMTGIPIVNVNNNCSTGSTALFLARQAVRSGAADCALAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 114 GQENMSraPHVLN---DSRTGALPDADNLVDSLVhdglwdafndyhiGVTAENLAREY--GISRELQDAYALSSQQKARA 188
Cdd:PRK08256 106 GFEQMQ--PGALGsvwDDRPSPLERFDKALAELQ-------------GFDPAPPALRMfgGAGREHMEKYGTTAETFAKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 189 AIDTGR---------FKDEIvpivtqrngqtaivdTDEQPRADAsaeglallhPAFDSLgsvTAGNASSINDGAAAVMMM 259
Cdd:PRK08256 171 GVKARRhaannpyaqFRDEY---------------TLEDVLASP---------MIWGPL---TRLQCCPPTCGAAAAIVC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 260 SEAKAQALGLPVLARIRA------FAS----------VGVDPALMGIAPVYatrrclERAGWQLAEVDLIEANEAFAAQA 323
Cdd:PRK08256 224 SEEFARKHGLDRAVEIVAqamttdTPStfdgrsmidlVGYDMTRAAAQQVY------EQAGIGPEDIDVVELHDCFSANE 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446588633 324 L------------SVGKMLEWDER----RVNVN--GGAIALGHPIGASG 354
Cdd:PRK08256 298 LltyealglcpegEAEKFIDDGDNtyggRWVVNpsGGLLSKGHPLGATG 346
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
81-114 |
5.06e-05 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 45.24 E-value: 5.06e-05
10 20 30
....*....|....*....|....*....|....
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:cd00833 163 SLTVDTACSSSLVALHLACQSLRSGECDLALVGG 196
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
223-381 |
2.96e-04 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 42.75 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 223 ASAEGLALLHPAF---DSLGSVTAG-----NASSINDGAAAVMMMSEAKAQAL-GLPVLARIRAFasvGVDPALMGIAPV 293
Cdd:PRK06289 188 AQTRGWAFPDEATnddDATNPVVEGrlrrqDCSQVTDGGAGVVLASDAYLRDYaDARPIPRIKGW---GHRTAPLGLEQK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 294 YA-----------TRRCLE----RAGWQLAEVDLIEANEAFAA------------------QALSVGKMLEWDERRVNVN 340
Cdd:PRK06289 265 LDrsagdpyvlphVRQAVLdayrRAGVGLDDLDGFEVHDCFTPseylaidhigltgpgeswKAIENGEIAIGGRLPINPS 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446588633 341 GGAIALGHPIGASGCRILVSLVHEMVKR------DARKGLATLCIGG 381
Cdd:PRK06289 345 GGLIGGGHPVGASGVRMLLDAAKQVTGTagdyqvEGAKTFGTLNIGG 391
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
81-114 |
3.06e-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: 3.06e-04
10 20 30
....*....|....*....|....*....|....
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:smart00825 90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
176-354 |
8.16e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 41.21 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 176 DAYALSSQQkARAAIDTGRFKDEIVPIVTQRNgqtaivdtdeqpRADASAEGLALLHPAFDSLGS-------VTAGNASS 248
Cdd:PRK07937 137 DSVSMAGLQ-ARAGLDAGKWTEEQMAEVAARS------------RADARRNPSAEPSISVDELLArpyfadpLRRHDIAP 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 249 INDGAAAVMMMSEAKAQALgLPVLARIRAFASvGVDPALMG---IAPVYATRRCLERA-GWQLAEVDLIEANEAFAAQAL 324
Cdd:PRK07937 204 ITDGAAAVVLAAGDRAREL-RERPAWITGIEH-RIESPSLGardLTRSPSTALAAEAAtGGDAGGVDVAELHAPFTHQEL 281
|
170 180 190
....*....|....*....|....*....|.
gi 446588633 325 SVGKMLEWDER-RVNVNGGAIAlGHPIGASG 354
Cdd:PRK07937 282 ILREALGLGDKtKVNPSGGALA-ANPMFAAG 311
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
82-119 |
8.65e-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: 8.65e-04
10 20 30
....*....|....*....|....*....|....*...
gi 446588633 82 ITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMS 119
Cdd:cd00828 156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
229-354 |
1.42e-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: 40.60 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 229 ALLHP----AFDSLGSVTAGN-----AS----------SINDGAAAVMMMSEAKAQALGLPVLARIRAFASVG-----VD 284
Cdd:cd00834 190 ALITPltlaGFAALRALSTRNddpekASrpfdkdrdgfVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTA 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 285 PALMGIAPVYATRRCLERAGWQLAEVDLIEA----------NEAFAAQALsvgkMLEWDER-RVNVNGGAIalGHPIGAS 353
Cdd:cd00834 270 PDPDGEGAARAMRAALADAGLSPEDIDYINAhgtstplndaAESKAIKRV----FGEHAKKvPVSSTKSMT--GHLLGAA 343
|
.
gi 446588633 354 G 354
Cdd:cd00834 344 G 344
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
71-116 |
1.42e-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: 40.46 E-value: 1.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446588633 71 IKGGLPTTVSAitindvCGSGLKALHLATQAIQCGEADIVIAGGQE 116
Cdd:COG0304 150 LKGPNYTVSTA------CASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
81-114 |
1.63e-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: 40.63 E-value: 1.63e-03
10 20 30
....*....|....*....|....*....|....
gi 446588633 81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:COG3321 167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGG 200
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
247-365 |
1.90e-03 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 40.26 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 247 SSINDGAAAVMMMSEAKAQALGLP--------VLARIRAFASVGVDP--ALMGIAPVYATRRCLERAGWQLAEVDLIEAN 316
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSpndsrlveIKSLACASGNLYEDPpdATRMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446588633 317 EAFAA------QALSV------------GKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEM 365
Cdd:PTZ00455 336 DCFTIaellmyEALGIaeyghakdlirnGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQM 402
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
251-354 |
2.86e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 39.65 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588633 251 DGAAAVMMMSEAKAQALGLPVLARIRAF-----ASVGVDPALMGIAPVYATRRCLERAGWQLAEVDLIEA-------NEA 318
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAhgtatrlNDQ 289
|
90 100 110
....*....|....*....|....*....|....*.
gi 446588633 319 FAAQALSvgkmlEWDERRVNVNGGAIALGHPIGASG 354
Cdd:PRK05952 290 REANLIQ-----ALFPHRVAVSSTKGATGHTLGASG 320
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
71-116 |
4.29e-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: 4.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446588633 71 IKGGLPTTVSAitindvCGSGLKALHLATQAIQCGEADIVIAGGQE 116
Cdd:cd00834 150 LRGPNYTVSTA------CASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| |
