|
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: 681.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVS 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGP-GDSHIIDSLVHDGLWDAFNDYHMGVT 159
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKmGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 160 AENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVVDTDEQPRADTSAEGLARLSPAFDRLG 239
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 240 SVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEAF 319
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501072875 320 AAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIERD 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: 607.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVS 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGPGDSHIIDSLVHDGLWDAFNDYHMGVTA 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPMINPGLTDPYTGLSMGETA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 161 ENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGApLVVDTDEQPRADTSAEGLARLSPAFDRLGS 240
Cdd:COG0183 161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKPAFKKDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 241 VTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEAFA 320
Cdd:COG0183 240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501072875 321 AQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 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: 600.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVS 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTG-GPGDSHIIDSLVHDGLWDAFNDYHMGVT 159
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGlRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 160 AENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVVDTDEQPRADTSAEGLARLSPAFDRLG 239
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 240 SVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEAF 319
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501072875 320 AAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIERD 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: 590.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 5 VIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVSAITI 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 85 NDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGPGDSHIIDSLVHDGLWDAFNDYHMGVTAENLA 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 165 REYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQmQGAPLVVDTDEQPRADTSAEGLARLSPAFDRLGSVTAG 244
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPG-RKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 245 NASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEAFAAQTL 324
Cdd:cd00751 240 NASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQAL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501072875 325 SVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 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 |
2.36e-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: 501.37 E-value: 2.36e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 6 IVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVSAITIN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 86 DVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGG--PGDSHIIDSLVHDgLWDAFNDYHMGVTAENL 163
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGvkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 164 AREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGaPLVVDTDEQPRADTSAEGLARLSPAFDRLGSVTA 243
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKG-PVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 244 GNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEAFAAQT 323
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501072875 324 LSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIE 390
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-390 |
2.04e-161 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 458.79 E-value: 2.04e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVS 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGP-GDSHIIDSLVHDGLWDAFNDYHMGVT 159
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRmGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 160 AENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVVDTDEQPRADTSAEGLARLSPAFDRLG 239
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 240 SVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEAF 319
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501072875 320 AAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIE 390
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-391 |
1.61e-151 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 433.62 E-value: 1.61e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVL-TAGAGQNPARQTALNSGLPWSV 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpTEPRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGP-GDSHIIDSLVhDGLWDAFNDYHMGV 158
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARmGDAKLVDMMV-GALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 159 TAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGaPLVVDTDEQPRADTSAEGLARLSPAFDR- 237
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKG-EVVFDTDEHVRADTTLEDLAKLKPVFKKe 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 238 LGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANE 317
Cdd:PRK09051 240 NGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501072875 318 AFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-391 |
2.82e-150 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 430.28 E-value: 2.82e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 2 KDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVSA 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 82 ITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGP-GDSHIIDSLVHDGLWDAFNDYHMGVTA 160
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRlGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 161 ENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAP-LVVDTDEQPrADTSAEGLARLSPAFDR-L 238
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPsVIVDKDEGL-GKFDPAKLRKLRPSFKEdG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 239 GSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEA 318
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501072875 319 FAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.79e-144 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 415.54 E-value: 2.79e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQvlTAGAGQNPA--RQTALNSGLPWS 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGPGDShiidSLVHDGLWDA---FNDYH 155
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGG----VQLHDRLARGretAGGRR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 156 MGV------TAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVVDTDEQPRADTSAEGLA 229
Cdd:PRK06205 155 FPVpggmieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 230 RLSP---AFDRLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQ 306
Cdd:PRK06205 235 KLRPimgKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 307 LNDVDLIEANEAFAAQTLSVGKLLAW---DERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQ 383
Cdd:PRK06205 315 LDDIDLIELNEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQ 394
|
....*...
gi 501072875 384 GVALAIER 391
Cdd:PRK06205 395 GLAAVFER 402
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-390 |
2.95e-144 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 415.20 E-value: 2.95e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVS 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVlTEGRTGGP-GDSHIIDSLVHDGLWDAFNDYHMGVT 159
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHG-SYIRAGAKfGDIKMVDLMQYDGLTDVFSGVFMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 160 AENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVvDTDEQPRADTSAEGLARLSPAFDRLG 239
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLF-DHDETVRPDTSLEILSKLRPAFDKNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 240 SVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEAF 319
Cdd:PRK06633 240 VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501072875 320 AAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIE 390
Cdd:PRK06633 320 AAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-391 |
2.45e-139 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 402.79 E-value: 2.45e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRT-GLNPQDVDEVILGQVLTAGA-GQNPARQTALNSGLPWS 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGPGDSHIIDS-----LVHDGLWDAFND 153
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSRQAEIFDTtigwrFVNPLMKAQYGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 154 YHMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVVDTDEQPRADTSAEGLARLSP 233
Cdd:PRK09050 161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALAKLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 234 AFDRLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLI 313
Cdd:PRK09050 241 VFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 314 EANEAFAAQTLSVGKLL--AWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:PRK09050 321 ELNEAFAAQGLAVLRQLglADDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIER 400
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-391 |
1.46e-126 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 369.68 E-value: 1.46e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRS-AVELGAVVIEALLTRT-GLNPQDVDEVILGQVL-TAGAGQNPARQTALNSGLPW 77
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAFRNVrAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQqTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 78 SVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvLTEGRTGGPGDSHIIdslvhdglwdAFNDYHMG 157
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--MNHGVDFHPGLSKNV----------AKAAGMMG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 158 VTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVVDTDEQPRADTSAEGLARLSPAFD- 236
Cdd:PRK08947 149 LTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFDp 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 237 RLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEAN 316
Cdd:PRK08947 229 VNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELN 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501072875 317 EAFAAQTLSVGKLLAWDER---KVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:PRK08947 309 EAFAAQSLPCLKDLGLLDKmdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFER 386
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-391 |
3.35e-125 |
|
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: 366.80 E-value: 3.35e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 2 KDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRT-GLNPQDVDEVILGQVLTAGA-GQNPARQTALNSGLPWSV 79
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTE-----GRTGGPGDSHIIDSLVHDGLWDAFNDY 154
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKadsafSRSAKIEDTTIGWRFINPLMKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 155 HMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVVDTDEQPRADTSAEGLARLSPA 234
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEGLAKLKPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 235 FDRLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIE 314
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501072875 315 ANEAFAAQTLSVGKLL--AWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:TIGR02430 321 LNEAFAAQALAVLRELglADDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
4-390 |
1.67e-119 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 352.27 E-value: 1.67e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 4 VVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVSAIT 83
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTG-GPGDSHIIDSLVHDGLWDAFNDYH-MGVTAE 161
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGmRMGHGQVLDHMFLDGLEDAYDKGRlMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 162 NLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGApLVVDTDEQPRAdTSAEGLARLSPAFDRLGSV 241
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGD-TVIDRDEQPFK-ANPEKIPTLKPAFSKTGTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 242 TAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEAFAA 321
Cdd:PRK06954 247 TAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501072875 322 QTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIE 390
Cdd:PRK06954 327 VTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-262 |
6.31e-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: 345.44 E-value: 6.31e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 4 VVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVSAIT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVL-TEGRTGGP-GDSHIIDSLVHDGLWDAFNDYHMGVTAE 161
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKhGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 162 NLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPlVVDTDEQPRADTSAEGLARLSPAFDRLGSV 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
|
250 260
....*....|....*....|.
gi 501072875 242 TAGNASSMNDGAAAVLMMSAS 262
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-391 |
5.14e-118 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 348.28 E-value: 5.14e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIG-CFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVL-TAGAGQNPARQTALNSGLPWS 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltegrTGGpgdsHIIDSLVHdgLWDAFNDYHMGV 158
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVP-------MMG----HVVRPNPR--LVEAAPEYYMGM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 159 --TAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQ--------MQGAPLVVDTDEQPRADTSAEGL 228
Cdd:PRK07661 148 ghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLrtvgennkLQEETITFSQDEGVRADTTLEIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 229 ARLSPAFDRLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLN 308
Cdd:PRK07661 228 GKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 309 DVDLIEANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALA 388
Cdd:PRK07661 308 DIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGV 387
|
...
gi 501072875 389 IER 391
Cdd:PRK07661 388 FEL 390
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-391 |
3.93e-116 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 343.63 E-value: 3.93e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRS------AVELGAVVIEALLTRTGLNPQDVDEVILGQVLtaGAGQN---PARQTAL 71
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKDPQKDvfnnirPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENwlyGGRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 72 NSGLPWSVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvLTEGRTGGPGDSHIIDS-LVHdglWDA 150
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP--MGDNPHIEPNPKLLTDPkYIE---YDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 151 FNDYHMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQmQGAPLVVDTDEQPRADTSAEGLAR 230
Cdd:PRK06445 154 TTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEV-EGKKKVVDVDQSVRPDTSLEKLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 231 LSPAFDRLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDV 310
Cdd:PRK06445 233 LPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 311 DLIEANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIE 390
Cdd:PRK06445 313 DLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLE 392
|
.
gi 501072875 391 R 391
Cdd:PRK06445 393 R 393
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-390 |
4.38e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 338.14 E-value: 4.38e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVS 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGPG-----DSHIIDSLVHDGLWDAFNDYH 155
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRWGPKhllhkNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 156 MGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVieqmqgaplVVDTDEQPRaDTSAEGLARLSPAF 235
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------DLDRDEGIR-KTTMEDLAKLPPAF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 236 DRLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEA 315
Cdd:PRK06366 231 DKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEH 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501072875 316 NEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIE 390
Cdd:PRK06366 311 NEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-392 |
9.22e-113 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 337.12 E-value: 9.22e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 3 DVVIVGAARTPIgCF--QGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQ-NPARQTALNSGLPWSV 79
Cdd:PLN02287 47 DVVIVAAYRTPI-CKakRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTegrtGGPGDSHIIDSLVHDGLWDafndyhMGVT 159
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWE----GGVNPRVESFSQAQDCLLP------MGIT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 160 AENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPV---VIEQMQGA--PLVVDTDEQPRADTSAEGLARLSPA 234
Cdd:PLN02287 196 SENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkIVDPKTGEekPIVISVDDGIRPNTTLADLAKLKPV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 235 FDRLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIE 314
Cdd:PLN02287 276 FKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 315 ANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKR--QARKGLATLCIGGGQGVALAIERD 392
Cdd:PLN02287 356 INEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRgkDCRFGVVSMCIGTGMGAAAVFERG 435
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-391 |
3.55e-111 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 331.20 E-value: 3.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIG-CFQGQLARRSAVELGAVVIEALLTRT-GLNPQDVDEVILGQVL-TAGAGQNPARQTALNSGLPW 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 78 SVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltegrTGGPGDS---HIIDSLVHDGLwdafnDY 154
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP-------MMGNKPSmspAIFARDENVGI-----AY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 155 HMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIE---------QMQGAPLVVDTDEQPRADTSA 225
Cdd:PRK09052 153 GMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITerfpdlatgEVDVKTRTVDLDEGPRADTSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 226 EGLARLSPAFDRLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGW 305
Cdd:PRK09052 233 EGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 306 QLNDVDLIEANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGV 385
Cdd:PRK09052 313 KQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGA 392
|
....*.
gi 501072875 386 ALAIER 391
Cdd:PRK09052 393 AGIFER 398
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-391 |
4.43e-109 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 325.96 E-value: 4.43e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGA-GQNPARQTALNSGLPWSV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGPGDSHIIDSLV-----HDGLWDAFNDY 154
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTTIgarfpNPKIVAQYGND 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 155 HMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQ-MQGAPLVVDTDEQPRADTSAEGLARLSP 233
Cdd:PRK08131 161 SMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgRKLPPKLVAEDEHPRPSSTVEALTKLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 234 AFDRlGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLI 313
Cdd:PRK08131 241 LFEG-GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDII 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 314 EANEAFAAQTLSVGKLL--AWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:PRK08131 320 EINEAFASQVLGCLKGLgvDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIER 399
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-391 |
8.75e-108 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 322.72 E-value: 8.75e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIG-CFQGQLARRSAVELGAVVIEALLTRT-GLNPQDVDEVILGQVLTAG-AGQNPARQTALNSGLPw 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 78 SVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPH------------------VLTEGRTGGpGDSHII 139
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKgnsdslpdtknplfaeaqARTAARAEG-GAEAWH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 140 DSLVHDGLWDAFndYHMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQmqGAplVVDTDEQP 219
Cdd:PRK07851 159 DPREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPD--GT--VVSTDDGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 220 RADTSAEGLARLSPAFDRLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRC 299
Cdd:PRK07851 233 RAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 300 LERAGWQLNDVDLIEANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCI 379
Cdd:PRK07851 313 LARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCV 392
|
410
....*....|..
gi 501072875 380 GGGQGVALAIER 391
Cdd:PRK07851 393 GGGQGMAMVLER 404
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-391 |
6.61e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 315.28 E-value: 6.61e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQ--GQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAG-AGQNPARQTALNSGLPW 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 78 SVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHvlteGRTGG--PGDSHIidslvhdglwdAFNDYH 155
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPM----GSDGGawAMDPST-----------NFPTYF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 156 M--GVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVvieQMQGAPLVVDTDEQPRADTSAEGLARLSP 233
Cdd:PRK08242 146 VpqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV---KDQNGLTILDHDEHMRPGTTMESLAKLKP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 234 AFDRLGSV---------------------TAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAP 292
Cdd:PRK08242 223 SFAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 293 VYATRRCLERAGWQLNDVDLIEANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARK 372
Cdd:PRK08242 303 VPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRT 382
|
410
....*....|....*....
gi 501072875 373 GLATLCIGGGQGVALAIER 391
Cdd:PRK08242 383 ALITLCVGGGMGIATIIER 401
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-391 |
7.87e-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: 314.57 E-value: 7.87e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 3 DVVIVGAARTPIGCFQGQLARRSAVE-LGAVVIEALLTR-TGLNPQDVDEVILGQV-LTAGAGQNPARQTALNSGLPWSV 79
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTRAEdLSAHLMSKLLARnPKVDPAEVEDIYWGCVqQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHvltegrtggpgdSHIIDSLVHDGLWDAFNDYHMGVT 159
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPM------------MHGVDFHPGMSLHVAKAAGMMGLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 160 AENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVVDTDEQPRADTSAEGLARLSPAFDRL- 238
Cdd:TIGR02445 149 AEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPAFDPKn 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 239 GSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEA 318
Cdd:TIGR02445 229 GTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501072875 319 FAAQTLSVGK---LLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:TIGR02445 309 FAAQALPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-391 |
3.10e-100 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 303.86 E-value: 3.10e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVS 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTE-----------GRTGG----------PGDSHII 139
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEkmvrwlagwyaAKSIGqklaalgklrPSYLAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 140 DSLVHdGLWDAFNDYHMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRdEIVPVVIEQMQgaplVVDTDEQP 219
Cdd:PRK08170 162 IGLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDRDGK----FYDHDDGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 220 RADTSAEGLARLSPAFDR-LGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRR 298
Cdd:PRK08170 236 RPDSSMEKLAKLKPFFDRpYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 299 CLERAGWQLNDVDLIEANEAFAAQTLsvGKLLAW-------------------DERKVNVNGGAIALGHPIGASGCRILV 359
Cdd:PRK08170 316 LLQRHGLTLEDLDLWEINEAFAAQVL--ACLAAWadeeycreqlgldgalgelDRERLNVDGGAIALGHPVGASGARIVL 393
|
410 420 430
....*....|....*....|....*....|..
gi 501072875 360 SLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:PRK08170 394 HLLHALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-391 |
3.79e-99 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 300.10 E-value: 3.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGA-GQNPARQTALNSGLPWSV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHvlteGRTGGPGDSHIIDSlvhDGLWDAFNDYhmgVT 159
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPL----GANAGPGRGLPRPD---SWDIDMPNQF---EA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 160 AENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVI------EQMQGAPLVVDTDEQPRaDTSAEGLARLSP 233
Cdd:PRK07850 151 AERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQApvldeeGQPTGETRLVTRDQGLR-DTTMEGLAGLKP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 234 AFDRlGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLI 313
Cdd:PRK07850 230 VLEG-GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLV 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501072875 314 EANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:PRK07850 309 EINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-391 |
5.33e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 294.31 E-value: 5.33e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAG--AGqNPARQTALNSGLPWS 78
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpqAG-NIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvLTEGRTGGPgDSHIIDSLVHDGLWDA-FNDYHMG 157
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTAGE-QLGFTSPFAESKGWLHrYGDQEVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 158 --VTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVvieqmqgapLVVDTDEQPRaDTSAEGLARLSPAF 235
Cdd:PRK07801 157 qfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV---------GGVTVDEGPR-ETSLEKMAGLKPLV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 236 DRlGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEA 315
Cdd:PRK07801 227 EG-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEI 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501072875 316 NEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:PRK07801 306 NEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-386 |
1.66e-93 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 285.51 E-value: 1.66e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIG-CFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGA-GQNPARQTALNSGLPWS 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAP-----HVLTEGrtggpgdshiidslvhdglWDAFND 153
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQnemnrHMLREG-------------------WLVEHK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 154 ----YHMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIE---------QMQGAPLVVDTDEQPR 220
Cdd:PRK07108 142 peiyWSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTagvadkatgRLFTKEVTVSADEGIR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 221 ADTSAEGLARLSPAFDRlGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCL 300
Cdd:PRK07108 222 PDTTLEGVSKIRSALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 301 ERAGWQLNDVDLIEANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIG 380
Cdd:PRK07108 301 KQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIG 380
|
....*.
gi 501072875 381 GGQGVA 386
Cdd:PRK07108 381 GGQGAA 386
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.36e-91 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 280.85 E-value: 1.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAG-AGQNPARQTALNSGLPWSV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltegrTGGPGDSHIIDSLVH---DGLWDAFND--Y 154
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP-------MGSPSTLPAKNGLGHyksPGMEERYPGiqF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 155 HMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVVDTDEQPRADTSAEGLARLSPA 234
Cdd:PRK06504 154 SQFTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 235 FDRlGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIE 314
Cdd:PRK06504 234 AEG-GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501072875 315 ANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:PRK06504 313 VNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-392 |
3.05e-90 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 278.41 E-value: 3.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 4 VVIVGAARTPigcfqgqLARR-------SAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLP 76
Cdd:PRK08963 7 IAIVSGLRTP-------FAKQatafhgiPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 77 WSVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAP--------HVLTE---GRTGGPGDShIIDSLvhd 145
Cdd:PRK08963 80 VHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaRALVDlnkARTLGQRLK-LFSRL--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 146 GLWD------AFNDY----HMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAplvVDT 215
Cdd:PRK08963 156 RLRDllpvppAVAEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQP---LEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 216 DEQPRADTSAEGLARLSPAFDR-LGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDP---ALMGia 291
Cdd:PRK08963 233 DNNIRGDSTLEDYAKLRPAFDRkHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwqdMLLG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 292 PVYATRRCLERAGWQLNDVDLIEANEAFAAQTLSVGKLLA-----------------WDERKVNVNGGAIALGHPIGASG 354
Cdd:PRK08963 311 PAYATPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFAserfareklgrsqaigeVDMSKFNVLGGSIAYGHPFAATG 390
|
410 420 430
....*....|....*....|....*....|....*...
gi 501072875 355 CRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIERD 392
Cdd:PRK08963 391 ARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLEVE 428
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-390 |
6.92e-86 |
|
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238422 [Multi-domain] Cd Length: 393 Bit Score: 266.28 E-value: 6.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 7 VGAARTPIGCFQGQLARRS---AVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVSAIT 83
Cdd:cd00826 1 AGAAMTAFGKFGGENGADAndlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 84 INDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSraphvltegrtggpgdshiidslvhdglwdafndyhmgVTAENL 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME--------------------------------------TSAENN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 164 AREYNI--------SREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGApLVVDTDE--QPRADTSAEGLARLSP 233
Cdd:cd00826 123 AKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGD-IHSDADEyiQFGDEASLDEIAKLRP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 234 AFDRLGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPV-------LARIRAFASVGVDPA----LMGIAPVYATRRCLER 302
Cdd:cd00826 202 AFDKEDFLTAGNACGLNDGAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 303 AGWQLNDVDLIEANEAFAAQTLSVGKLLAWDERK------------------VNVNGGAIALGHPIGASGCRILVSLVHE 364
Cdd:cd00826 282 AGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFE 361
|
410 420 430
....*....|....*....|....*....|.
gi 501072875 365 MVKRQ-----ARKGLATLCIGGGQGVALAIE 390
Cdd:cd00826 362 LKGEAgkrqgAGAGLALLCIGGGGGAAMCIE 392
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
5-390 |
3.91e-83 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 258.16 E-value: 3.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 5 VIVGAARTPIGCFQGQLARRSAVELGAVVIEALltRTGLNPQdVDEVILGQVLtaGAGQNPARQTALNSGLPWSVSAITI 84
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGMERE-IDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 85 NDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvLTEGRTGGPgdshiidslvhdglwDAFNDYHMGVTAENLA 164
Cdd:PRK06690 79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSP--FQNRARFSP---------------ETIGDPDMGVAAEYVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 165 REYNISREHQDAYALASQHKARVAIDSGRFRDEIVPvvieqMQGAplvvdTDEQPRADTSAEGL-ARLSPAFDRLGSVTA 243
Cdd:PRK06690 142 ERYNITREMQDEYACLSYKRTLQALEKGYIHEEILS-----FNGL-----LDESIKKEMNYERIiKRTKPAFLHNGTVTA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 244 GNASSMNDGAAAVLMMSASKAQEMGL-PVLARIRAfASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEAFAAQ 322
Cdd:PRK06690 212 GNSCGVNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASK 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501072875 323 TLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIE 390
Cdd:PRK06690 291 VVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-391 |
7.80e-82 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 256.63 E-value: 7.80e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIG---CFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGA-GQNPARQTALNSGLP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 77 WSVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMS-RAPHVLTEGRTGGPgdSHIIDSlVHDGLWDAFNDYH 155
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGKP--PLGMGS-GNLRLRALHPQSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 156 MGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQmqgAPLVVDTDEQPRADTSAEGLARLSPAF 235
Cdd:PRK06025 158 QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDD---GSVALDHEEFPRPQTTAEGLAALKPAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 236 DRLGSVT--------------------------AGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVGVDPALMG 289
Cdd:PRK06025 235 TAIADYPlddkgttyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLML 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 290 IAPVYATRRCLERAGWQLNDVDLIEANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEMVKRQ 369
Cdd:PRK06025 315 NAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRG 394
|
410 420
....*....|....*....|..
gi 501072875 370 ARKGLATLCIGGGQGVALAIER 391
Cdd:PRK06025 395 LKRGLVTMCAAGGMAPAIIIER 416
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-391 |
4.70e-68 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 220.93 E-value: 4.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQGQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVS 80
Cdd:PRK09268 6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEG-----------RTGG----------PGDshii 139
Cdd:PRK09268 86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGlrkillelnraKTTGdrlkalgklrPKH---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 140 dsLVHD---------GLwdafndyHMGVTAENLAREYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVvieqmqgap 210
Cdd:PRK09268 162 --LAPEiprngeprtGL-------SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF--------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 211 LVVDTDEQPRADTSAEGLARLSPAFDR--LGSVTAGNASSMNDGAAAVLMMSASKAQEMGLPVLARIRAF--ASV----G 282
Cdd:PRK09268 224 LGLTRDNNLRPDSSLEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetAAVdfvhG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 283 VDPALMgiAPVYATRRCLERAGWQLNDVDLIEANEAFAAQTLSVgkLLAW-------------------DERKVNVNGGA 343
Cdd:PRK09268 304 KEGLLM--APAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLAT--LKAWedeeycrerlgldaplgsiDRSKLNVNGSS 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 501072875 344 IALGHPIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:PRK09268 380 LAAGHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
269-391 |
8.36e-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: 8.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 269 LPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEANEAFAAQTLSVGKLLAWDERKVNVNGGAIALGH 348
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 501072875 349 PIGASGCRILVSLVHEMVKRQARKGLATLCIGGGQGVALAIER 391
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
24-389 |
4.24e-22 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 94.43 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 24 RSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPwSVSAITINDVCGSGLKALHLATQAIQ 103
Cdd:cd00327 5 ITASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 104 CGEADVVIAGGqenmsraphvltegrtggpgdshiidslvhdglwdafndyhmgvtaenlareynisrehqdayalasqh 183
Cdd:cd00327 84 NGKADIVLAGG--------------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 184 karvaidsgrfrdeivpvvieqmqgaplvvdtdeqpradtsaeglarlspafdrlgsvtaGNASSMNDGAAAVLMMSASK 263
Cdd:cd00327 95 ------------------------------------------------------------SEEFVFGDGAAAAVVESEEH 114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 264 AQEMGLPVLARIRAFASVGVD----PALMGIAPVYATRRCLERAGWQLNDVDLIEANEAFAAQTLSVGKLLAWDE---RK 336
Cdd:cd00327 115 ALRRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPdgvRS 194
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 337 VNVNGGAIALGHPIGASGCRILVSLVHEM-------VKRQARKGLATLCIGGGQGVALAI 389
Cdd:cd00327 195 PAVSATLIMTGHPLGAAGLAILDELLLMLehefippTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
7-371 |
8.15e-22 |
|
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: 95.79 E-value: 8.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 7 VGAARTPIGCFQGqlarRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPwSVSAITIND 86
Cdd:cd00829 1 VGVGMTPFGRRSD----RSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLL-GKPATRVEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 87 VCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPHVLTEGRTGGPGDshiidslvhdglwDAFNDYHMGVTAENLAre 166
Cdd:cd00829 76 AGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLE-------------WEGPEPPGGLTPPALY-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 167 YNISREHQDAYALASQHKARVAIDSGR---------FRDEIvpvVIEQMQGAPLVVDtdeqPradtsaeglarlspafdr 237
Cdd:cd00829 141 ALAARRYMHRYGTTREDLAKVAVKNHRnaarnpyaqFRKPI---TVEDVLNSRMIAD----P------------------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 238 lgsVTAGNASSMNDGAAAVLMMSASKAQEMGLPvLARIRAFAsVGVDPALMG--------IAPVYATRRCLERAGWQLND 309
Cdd:cd00829 196 ---LRLLDCCPVSDGAAAVVLASEERARELTDR-PVWILGVG-AASDTPSLSerddflslDAARLAARRAYKMAGITPDD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 310 VDLIEANEAF------------------AAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGcrilVSLVHEMVkRQAR 371
Cdd:cd00829 271 IDVAELYDCFtiaellaledlgfcekgeGGKLVREGDTAIGGDLPVNTSGGLLSKGHPLGATG----LAQAVEAV-RQLR 345
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-373 |
1.15e-19 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 89.57 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGcfqgQLARRS----AVELGAVVIEAlltrTGLNPQDVDEVILGQVLTAG-AGQ-NPARQTALNSG 74
Cdd:PRK06064 1 MRDVAIIGVGQTKFG----ELWDVSlrdlAVEAGLEALED----AGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 75 LPwSVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvltegrtggPGDSHIIDSLVHDGLWDAFndy 154
Cdd:PRK06064 73 LA-PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVP----------TPDATEAIARAGDYEWEEF--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 155 hMGVTAENLAREynISREHQDAYALASQHKARVAIDS---------GRFRDEIvpvVIEQMQGAPLVvdtdeqpradtsA 225
Cdd:PRK06064 139 -FGATFPGLYAL--IARRYMHKYGTTEEDLALVAVKNhyngsknpyAQFQKEI---TVEQVLNSPPV------------A 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 226 EGLaRLspaFDrlgsvtagnASSMNDGAAAVLMMSASKAQEMGL-PVlaRIRAFASVGVDPAL------MGI-APVYATR 297
Cdd:PRK06064 201 DPL-KL---LD---------CSPITDGAAAVILASEEKAKEYTDtPV--WIKASGQASDTIALhdrkdfTTLdAAVVAAE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 298 RCLERAGWQLNDVDLIEANEAFA-AQTLSV-----------GKLLAWDERK------VNVNGGAIALGHPIGASGCRILV 359
Cdd:PRK06064 266 KAYKMAGIEPKDIDVAEVHDCFTiAEILAYedlgfakkgegGKLAREGQTYiggdipVNPSGGLKAKGHPVGATGVSQAV 345
|
410
....*....|....
gi 501072875 360 SLVHEMvKRQARKG 373
Cdd:PRK06064 346 EIVWQL-RGEAEKG 358
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
14-368 |
1.51e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 62.17 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 14 IGCFQGQLARRSAVELGAVVIEAL---LTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPWSVSaITINDVCGS 90
Cdd:PRK12578 6 IGVGNSKFGRRDDVSVQELAWESIkeaLNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVP-LRVEAMCAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 91 GLKALHLATQAIQCGEADVVIAGGQENMSRApHVLTEGRTGGPGDSHiidslvhdgLWD------AFNDYHMGVTAENLA 164
Cdd:PRK12578 85 GLAASLTAYTAVASGLVDMAIAVGVDKMTEV-DTSTSLAIGGRGGNY---------QWEyhfygtTFPTYYALYATRHMA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 165 ReYNISrEHQDAYALASQHKARVAIDSGRFRDEIV--PVVIEQMQGAPLvvdtdeqpradtsaeglaRLspaFDrlgsvt 242
Cdd:PRK12578 155 V-YGTT-EEQMALVSVKAHKYGAMNPKAHFQKPVTveEVLKSRAISWPI------------------KL---LD------ 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 243 agnASSMNDGAAAVLMMSASKAQEMGL--PVLARIRAFASvgvDPALMGI--------APVYATRRCLERAGWQLNDVDL 312
Cdd:PRK12578 206 ---SCPISDGSATAIFASEEKVKELKIdsPVWITGIGYAN---DYAYVARrgewvgfkATQLAARQAYNMAKVTPNDIEV 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501072875 313 IEANEAFAAQTLSVGKLLAWDER----------------KVNVN--GGAIALGHPIGASGcrilVSLVHEMVKR 368
Cdd:PRK12578 280 ATVHDAFTIAEIMGYEDLGFTEKgkggkfieegqsekggKVGVNlfGGLKAKGHPLGATG----LSMIYEITKQ 349
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
73-354 |
2.03e-10 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 61.84 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 73 SGLPwsvsAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRaphvlteGRTGGPGDSHIIDSLVHDGLWDAFN 152
Cdd:PRK08256 69 TGIP----IVNVNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQP-------GALGSVWDDRPSPLERFDKALAELQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 153 DYHMGVTAenlAREY-NISREHQDAYALASQHKARVAIDSGR---------FRDeivPVVIEQMQGAPLVVDtdeqprad 222
Cdd:PRK08256 138 GFDPAPPA---LRMFgGAGREHMEKYGTTAETFAKIGVKARRhaannpyaqFRD---EYTLEDVLASPMIWG-------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 223 tsaeGLARLSpafdrlgsvtagnASSMNDGAAAVLMMSASKAQEMGLPVLARIRA------FAS----------VGVDPA 286
Cdd:PRK08256 204 ----PLTRLQ-------------CCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAqamttdTPStfdgrsmidlVGYDMT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 287 LMGIAPVYatrrclERAGWQLNDVDLIEANEAFAAQTL------------SVGKLLAWDER----KVNVN--GGAIALGH 348
Cdd:PRK08256 267 RAAAQQVY------EQAGIGPEDIDVVELHDCFSANELltyealglcpegEAEKFIDDGDNtyggRWVVNpsGGLLSKGH 340
|
....*.
gi 501072875 349 PIGASG 354
Cdd:PRK08256 341 PLGATG 346
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-369 |
3.11e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 61.12 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGcfqgQLARRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNS--GLPWs 78
Cdd:PRK07516 1 MMTASIVGWAHTPFG----KLDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAGFSPQDFPASLVLQAdpALRF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 79 VSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAP------------HVLTEGRTGGpgdshiidslvhdG 146
Cdd:PRK07516 76 KPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPtaevgdillgasYLKEEGDTPG-------------G 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 147 LWDAFndyhmGVTAENLAREYnisREHQDAYAL--ASQHKARVAidsgrfrdeivpvvieqmqgAPLVvdtdeQPRADts 224
Cdd:PRK07516 143 FAGVF-----GRIAQAYFQRY---GDQSDALAMiaAKNHANGVA--------------------NPYA-----QMRKD-- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 225 aeglarLSPAFDRLGS----VTAG-----NASSMNDGAAAVLMMSASKAQEMGLPVlaRIRAFASVG-------VDPALM 288
Cdd:PRK07516 188 ------LGFEFCRTVSeknpLVAGplrrtDCSLVSDGAAALVLADAETARALQRAV--RFRARAHVNdflplsrRDPLAF 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 289 GiAPVYATRRCLERAGWQLNDVDLIEANEAF------------------AAQTLSVGKLLAWDERKVNVNGGAIALGHPI 350
Cdd:PRK07516 260 E-GPRRAWQRALAQAGVTLDDLSFVETHDCFtiaelieyeamglappgqGARAIREGWTAKDGKLPVNPSGGLKAKGHPI 338
|
410
....*....|....*....
gi 501072875 351 GASGcrilVSLvHEMVKRQ 369
Cdd:PRK07516 339 GATG----VSM-HVLAAMQ 352
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
1-381 |
2.39e-07 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 52.38 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPigcFQGQLAR--RSAVELGAVVIEALLTRTGLNPQDVDEVILGQV---LTAGAGQNPARQTALNSGL 75
Cdd:PRK06289 2 SDDVWVLGGYQSD---FARNWTKegRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFfgeLFAGQGHLGAMPATVHPAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 76 pWSVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSRAPhvlteGRTGgpgdshiidslvhdglwdafndyh 155
Cdd:PRK06289 79 -WGVPASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVP-----GDVA------------------------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 156 mgvtAENLAREYNISREHQDAY--------ALASQHKARVAIDSGRFRdeivpvVIEQMQGAplvvDTDEQPRADTsaEG 227
Cdd:PRK06289 129 ----AEHLGAAAWTGHEGQDARfpwpsmfaRVADEYDRRYGLDEEHLR------AIAEINFA----NARRNPNAQT--RG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 228 LARLSPAFDR---LGSVTAG-----NASSMNDGAAAVLMMSASKAQEM-GLPVLARIRAFasvGVDPALMGIAPVYA--- 295
Cdd:PRK06289 193 WAFPDEATNDddaTNPVVEGrlrrqDCSQVTDGGAGVVLASDAYLRDYaDARPIPRIKGW---GHRTAPLGLEQKLDrsa 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 296 --------TRRCLE----RAGWQLNDVDLIEANEAFAA------------------QTLSVGKLLAWDERKVNVNGGAIA 345
Cdd:PRK06289 270 gdpyvlphVRQAVLdayrRAGVGLDDLDGFEVHDCFTPseylaidhigltgpgeswKAIENGEIAIGGRLPINPSGGLIG 349
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 501072875 346 LGHPIGASGCRILVSLVHEMVKRQ-------ARKGLaTLCIGG 381
Cdd:PRK06289 350 GGHPVGASGVRMLLDAAKQVTGTAgdyqvegAKTFG-TLNIGG 391
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
81-114 |
1.36e-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: 46.09 E-value: 1.36e-05
10 20 30
....*....|....*....|....*....|....
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGG 114
Cdd:pfam00109 166 SVTVDTACSSSLVAIHAAVQSIRSGEADVALAGG 199
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
81-114 |
3.68e-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: 3.68e-05
10 20 30
....*....|....*....|....*....|....
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGG 114
Cdd:cd00833 163 SLTVDTACSSSLVALHLACQSLRSGECDLALVGG 196
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
1-281 |
7.18e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 44.75 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 1 MKDVVIVGAARTPIGCFQgqlarRSAVELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTaLNSGLPWS-V 79
Cdd:PRK06059 3 PEPVYILGAGMHPWGKWG-----RDFVEYGVVAARAALADAGLDWRDVQLVVGADTIRNGYPGFVAGAT-FAQALGWNgA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 80 SAITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMSR---APhvltegrTGG--PGDshiidslvHDglWDAFNdy 154
Cdd:PRK06059 77 PVSSSYAACASGSQALQSARAQILAGLCDVALVVGADTTPKgffAP-------VGGerPDD--------PD--WLRFH-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 155 HMGVT-----AENLAREYNISREHQDAYALASQHKARVAIDSG--RFRDeivPVVIEQMQGAPLVVDtdeqpradtsaeg 227
Cdd:PRK06059 138 LIGATnpvyfALLARRRMDLYGATVEDFAQVKVKNARHGLLNPnaRYRK---EVTVEDVLASPVVSD------------- 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 501072875 228 larlsPAfdRLGSVTAgnassMNDGAAAVLMMSASKAQEMGLPV--LARIRAFASV 281
Cdd:PRK06059 202 -----PL--RLLDICA-----TSDGAAALIVASKSFARRHLGSVagVPSVRAISTV 245
|
|
| PRK08257 |
PRK08257 |
acetyl-CoA acetyltransferase; Validated |
245-342 |
1.18e-04 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 236204 [Multi-domain] Cd Length: 498 Bit Score: 44.13 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 245 NASSMNDGAAAVLMMSASKAQEMGLP------------------VLARIRAFASVGVDPALmgiapvyatRRCLERAGWQ 306
Cdd:PRK08257 238 NANDMVDQGAAVLLTSVAKARRLGVPedrwvylhggadahdpydILERPDLHRSPAIRAAG---------RRALALAGLG 308
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 501072875 307 LNDVDLIEANEAF------AAQTLSvgklLAWDE-RKVNVNGG 342
Cdd:PRK08257 309 IDDIDAFDLYSCFpsavqvAARELG----LDLDDpRPLTVTGG 347
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
61-114 |
1.52e-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: 43.09 E-value: 1.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 501072875 61 AGQNPAR----QTALNSGLPWSVSAITINDVCGSGLKALHLATQAIQCGEADVVIAGG 114
Cdd:smart00825 66 AGIDPESlrgsRTGVFVGVSSSDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
28-120 |
2.52e-04 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 42.54 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 28 ELGAVVIEALLTRTGLNPQDVDEVILGQVLTAGAGQNPARQTALNSGLPwSVSAITINDVCGSGLKALHLATQAIQCGEA 107
Cdd:PRK12879 55 DLAIKAAERALARAGLDAEDIDLIIVATTTPDYLFPSTASQVQARLGIP-NAAAFDINAACAGFLYGLETANGLITSGLY 133
|
90
....*....|...
gi 501072875 108 DVVIAGGQENMSR 120
Cdd:PRK12879 134 KKVLVIGAERLSK 146
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
251-354 |
3.74e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 42.35 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 251 DGAAAVLMMSASKAQEMGLPVLARIRAF-----ASVGVDPALMGIAPVYATRRCLERAGWQLNDVDLIEA-------NEA 318
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAhgtatrlNDQ 289
|
90 100 110
....*....|....*....|....*....|....*.
gi 501072875 319 FAAQTLSvgkllAWDERKVNVNGGAIALGHPIGASG 354
Cdd:PRK05952 290 REANLIQ-----ALFPHRVAVSSTKGATGHTLGASG 320
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
28-365 |
6.57e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 41.80 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 28 ELGAVVIEALLTRTGLNPQD--VDEVILGQVLTA---------GAGQNPARQTALNSGLPWSvSAITINDVCGSGLKALH 96
Cdd:PTZ00455 50 ELLATAIQGTLENTGLDGKAalVDKVVVGNFLGElfssqghlgPAAVGSLGQSGASNALLYK-PAMRVEGACASGGLAVQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 97 LATQAIQCGEADVVIAGGQENMSRAphvltEGRTGGP--------GDSHIIDSLVHDGLWDAFNDY---HMGVTAENLAR 165
Cdd:PTZ00455 129 SAWEALLAGTSDIALVVGVEVQTTV-----SARVGGDylaraadyRRQRKLDDFTFPCLFAKRMKYiqeHGHFTMEDTAR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 166 EYNISREHQDAYALASQHKARVAIDSGRFRDEIVPVVIEQMQGAPLVVDTDEQPRADTSA-------EGLAR--LSPAFD 236
Cdd:PTZ00455 204 VAAKAYANGNKNPLAHMHTRKLSLEFCTGASDKNPKFLGNETYKPFLRMTDCSQVSDGGAglvlaseEGLQKmgLSPNDS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 237 RLGSVTAGNASSMNdgaaavLMMSASKAQEMGLPVLARIRAFASVGVDPALMGIAPVYatrRCLERAGWQLNDVdLIEAN 316
Cdd:PTZ00455 284 RLVEIKSLACASGN------LYEDPPDATRMFTSRAAAQKALSMAGVKPSDLQVAEVH---DCFTIAELLMYEA-LGIAE 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 501072875 317 EAFAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASGCRILVSLVHEM 365
Cdd:PTZ00455 354 YGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQM 402
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
234-354 |
7.21e-04 |
|
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: 41.37 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072875 234 AFDRLGSVTAGN-----AS----------SMNDGAAAVLMMSASKAQEMGLPVLARIRAFASVG-----VDPALMGIAPV 293
Cdd:cd00834 199 GFAALRALSTRNddpekASrpfdkdrdgfVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAA 278
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501072875 294 YATRRCLERAGWQLNDVDLI-------EANEafAAQTLSVGKLLAWDERKVNVNGGAIALGHPIGASG 354
Cdd:cd00834 279 RAMRAALADAGLSPEDIDYInahgtstPLND--AAESKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAG 344
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
82-119 |
9.78e-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: 40.89 E-value: 9.78e-04
10 20 30
....*....|....*....|....*....|....*...
gi 501072875 82 ITINDVCGSGLKALHLATQAIQCGEADVVIAGGQENMS 119
Cdd:cd00828 156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
81-114 |
1.29e-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: 1.29e-03
10 20 30
....*....|....*....|....*....|....
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGG 114
Cdd:COG3321 167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGG 200
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
81-116 |
3.60e-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: 3.60e-03
10 20 30
....*....|....*....|....*....|....*.
gi 501072875 81 AITINDVCGSGLKALHLATQAIQCGEADVVIAGGQE 116
Cdd:cd00834 154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
88-116 |
9.21e-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: 37.77 E-value: 9.21e-03
10 20
....*....|....*....|....*....
gi 501072875 88 CGSGLKALHLATQAIQCGEADVVIAGGQE 116
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| |
