|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
3-390 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 695.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 3 PSIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATA 82
Cdd:PRK05790 2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 83 WGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHC-AHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTA 161
Cdd:PRK05790 82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVlPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 162 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD-ITVDADEYIRHGATLDSMAKLRPAFDKEGT 240
Cdd:PRK05790 162 ENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDpVVVDTDEHPRPDTTAESLAKLRPAFDKDGT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 241 VTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFA 320
Cdd:PRK05790 242 VTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 321 AQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK05790 322 AQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVE 391
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
5-392 |
0e+00 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 601.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 84
Cdd:COG0183 4 VVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPAVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCA-HLRGGVKMgDFKMIDTMIKDGLTDAFYGYHMGTTAEN 163
Cdd:COG0183 84 VNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLpKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGETAEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 164 VAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTA 243
Cdd:COG0183 163 VAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 244 GNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQA 323
Cdd:COG0183 243 GNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAAQV 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2VTZ_B 324 CAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:COG0183 323 LAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
6-390 |
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: 599.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 6 VIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGM 85
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 86 NQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAENVA 165
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 166 KQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGN 245
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 246 ASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACA 325
Cdd:cd00751 241 ASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
2VTZ_B 326 VNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:cd00751 321 CLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
7-390 |
5.27e-177 |
|
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: 497.91 E-value: 5.27e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 7 IASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMN 86
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 87 QLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAP--HCAHLRGGVKMGDFKMIDTMIKDgLTDAFYGYHMGTTAENV 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPygVPRSLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 165 AKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAG 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 245 NASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQAC 324
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2VTZ_B 325 AVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
8-391 |
5.61e-172 |
|
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: 485.46 E-value: 5.61e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 8 ASAARTAVGSFNG---AFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 84
Cdd:cd00826 1 AGAAMTAFGKFGGengADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSmaphcahlrggvkmgdfkmidtmikdgltdafygyhmgTTAENV 164
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME--------------------------------------TSAENN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 165 AKQWQL--------SRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHG--ATLDSMAKLRPA 234
Cdd:cd00826 123 AKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGdeASLDEIAKLRPA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 235 FDKEGTVTAGNASGLNDGAAAALLMSEAEAS-------RRGIQPLGRIVSWATVGVDPK----VMGTGPIPASRKALERA 303
Cdd:cd00826 203 FDKEDFLTAGNACGLNDGAAAAILMSEAEAQkhglqskAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 304 GWKIGDLDLVEANEAFAAQACAVNKDLGWDP------------------SIVNVNGGAIAIGHPIGASGARILNTLLFEM 365
Cdd:cd00826 283 GLGIGDLDLIEAHDAFAANACATNEALGLCPegqggalvdrgdntyggkSIINPNGGAIAIGHPIGASGAAICAELCFEL 362
|
410 420 430
....*....|....*....|....*....|.
2VTZ_B 366 KRR-----GARKGLATLCIGGGMGVAMCIES 391
Cdd:cd00826 363 KGEagkrqGAGAGLALLCIGGGGGAAMCIES 393
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
5-392 |
9.52e-168 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 474.83 E-value: 9.52e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAgEGQNP--ARQAAMKAGVPQEATA 82
Cdd:PRK09051 5 VVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPT-EPRDMylSRVAAINAGVPQETPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 83 WGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCA-HLRGGVKMGDFKMIDTMIkDGLTDAFYGYHMGTTA 161
Cdd:PRK09051 84 FNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpAARWGARMGDAKLVDMMV-GALHDPFGTIHMGVTA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 162 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKE-GT 240
Cdd:PRK09051 163 ENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKEnGT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 241 VTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFA 320
Cdd:PRK09051 243 VTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAFA 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2VTZ_B 321 AQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:PRK09051 323 AQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFERL 394
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
5-390 |
7.80e-165 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 467.44 E-value: 7.80e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 84
Cdd:PRK05656 4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAMT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHC-AHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAEN 163
Cdd:PRK05656 84 LNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVlPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 164 VAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD-ITVDADEYIRHGATLDSMAKLRPAFDKEGTVT 242
Cdd:PRK05656 164 LVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEpLAFATDEQPRAGTTAESLAKLKPAFKKDGSVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 243 AGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQ 322
Cdd:PRK05656 244 AGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFAAQ 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2VTZ_B 323 ACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK05656 324 SLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
2-392 |
1.22e-162 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 461.81 E-value: 1.22e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 2 TPSIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEAT 81
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 82 AWGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTA 161
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 162 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTV 241
Cdd:PRK06633 162 ENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDKNGVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 242 TAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAA 321
Cdd:PRK06633 242 TAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2VTZ_B 322 QACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:PRK06633 322 QSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEAV 392
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
6-390 |
3.82e-148 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 424.90 E-value: 3.82e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 6 VIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGM 85
Cdd:PRK08235 5 VIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 86 NQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPH-CAHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAENV 164
Cdd:PRK08235 85 NKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYiLPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVYGGEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 165 AKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD-ITVDADEYIRHGATLDSMAKLRPAFDKEGTVTA 243
Cdd:PRK08235 165 AKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDpIVVAKDEAPRKDTTIEKLAKLKPVFDKTGTITA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 244 GNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQA 323
Cdd:PRK08235 245 GNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAAVA 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2VTZ_B 324 CAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK08235 325 LASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
5-390 |
1.82e-142 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 410.92 E-value: 1.82e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 84
Cdd:PRK06205 4 AVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPGMQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAH-LRGGVKMGDFKMIDTMIKDGLTD--AFYGY--HMGT 159
Cdd:PRK06205 84 LDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdMRWGVRGGGVQLHDRLARGRETAggRRFPVpgGMIE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 160 TAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD-ITVDADEYIRHGATLDSMAKLRP---AF 235
Cdd:PRK06205 164 TAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDpTVVDRDEHPRADTTLESLAKLRPimgKQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 236 DKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEA 315
Cdd:PRK06205 244 DPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLIEL 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2VTZ_B 316 NEAFAAQACAVNKDLGW---DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK06205 324 NEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAVFE 401
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
5-262 |
3.52e-131 |
|
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: 376.64 E-value: 3.52e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 84
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCA--HLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALptDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 163 NVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVT 242
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
|
250 260
....*....|....*....|
2VTZ_B 243 AGNASGLNDGAAAALLMSEA 262
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
7-390 |
2.02e-128 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 375.06 E-value: 2.02e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 7 IASAARTAVGSFNGAFANTPAHELGATVISAVLER-AGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWG 84
Cdd:PRK09050 6 ICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVSVPGTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCahlrggvkMG--------DFKMIDTMIK----DGLTDAF 152
Cdd:PRK09050 86 INRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFV--------MGkadsafsrQAEIFDTTIGwrfvNPLMKAQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 153 YGYH-MGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD-ITVDADEYIRHGATLDSMAK 230
Cdd:PRK09050 158 YGVDsMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDpVVVDRDEHPRPETTLEALAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 231 LRPAFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDL 310
Cdd:PRK09050 238 LKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 311 DLVEANEAFAAQACAVNKDLGW--DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMC 388
Cdd:PRK09050 318 DVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALA 397
|
..
2VTZ_B 389 IE 390
Cdd:PRK09050 398 IE 399
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
3-392 |
7.75e-124 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 363.26 E-value: 7.75e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 3 PSIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATA 82
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 83 WGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPH-CAHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTA 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKyLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 162 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD--ITVDADEYIRHgATLDSMAKLRPAFDKE- 238
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRpsVIVDKDEGLGK-FDPAKLRKLRPSFKEDg 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 239 GTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEA 318
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2VTZ_B 319 FAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELM 393
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
5-390 |
4.17e-119 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 351.12 E-value: 4.17e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 84
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPH-CAHLRGGVKMGDFKMIDTMIKDGLTDAF-YGYHMGTTAE 162
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYlLPKARGGMRMGHGQVLDHMFLDGLEDAYdKGRLMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 163 NVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHgATLDSMAKLRPAFDKEGTVT 242
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAFSKTGTVT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 243 AGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQ 322
Cdd:PRK06954 248 AANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVV 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2VTZ_B 323 ACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK06954 328 TMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
6-392 |
2.54e-117 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 346.35 E-value: 2.54e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 6 VIASAARTAVGSFN-GAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAW 83
Cdd:PRK07661 5 VIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEqGLNMARNIGALAGLPYTVPAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 84 GMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAH-LRGGVKMGDfkmidtmikdglTDAFYGYHMGTTAE 162
Cdd:PRK07661 85 TINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHvVRPNPRLVE------------AAPEYYMGMGHTAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 163 NVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD---------ITVDADEYIRHGATLDSMAKLRP 233
Cdd:PRK07661 153 QVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGennklqeetITFSQDEGVRADTTLEILGKLRP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 234 AFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLV 313
Cdd:PRK07661 233 AFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLF 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2VTZ_B 314 EANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:PRK07661 313 ELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFELL 391
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
5-390 |
5.63e-116 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 342.72 E-value: 5.63e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVG-SFNGAFANTPAHELGATVISAVLER-AGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEAT 81
Cdd:PRK08947 4 VVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLEqGFNIARNAALLAGIPHSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 82 AWGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMsmaphcahlrGGVKMGdfKMIDTMIKDGLTDAFYGYHMGTTA 161
Cdd:PRK08947 84 AVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM----------GHVPMN--HGVDFHPGLSKNVAKAAGMMGLTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 162 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPfiVKGRKGD---ITVDADEYIRHGATLDSMAKLRPAFD-K 237
Cdd:PRK08947 152 EMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIP--TEGHDADgvlKLFDYDEVIRPETTVEALAALRPAFDpV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 238 EGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANE 317
Cdd:PRK08947 230 NGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2VTZ_B 318 AFAAQACAVNKDLGWDPSI---VNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK08947 310 AFAAQSLPCLKDLGLLDKMdekVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
7-392 |
6.19e-116 |
|
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: 343.30 E-value: 6.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 7 IASAARTAVGSFNGAFANTPAHELGATVISAVLER-AGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWG 84
Cdd:TIGR02430 5 ICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSVPGTT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIK----DGLTDAFYGYH-MGT 159
Cdd:TIGR02430 85 VNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIEDTTIGwrfiNPLMKALYGVDsMPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 160 TAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDIT-VDADEYIRHGATLDSMAKLRPAFDKE 238
Cdd:TIGR02430 165 TAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTvVDQDEHPRPETTLEGLAKLKPVVRPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 239 GTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEA 318
Cdd:TIGR02430 245 GTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIELNEA 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2VTZ_B 319 FAAQACAVNKDLGW--DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:TIGR02430 325 FAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIERV 400
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
7-392 |
8.02e-114 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 337.75 E-value: 8.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 7 IASAARTAVG-SFNGAFANTPAHELGATVISAVLERA-GVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAW 83
Cdd:PRK09052 10 IVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEqGLNVARIGALLAGLPNSVGGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 84 GMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPhcahlrggvKMGDFKMIDTMIKDGLTDAFYGYHMGTTAEN 163
Cdd:PRK09052 90 TVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP---------MMGNKPSMSPAIFARDENVGIAYGMGLTAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 164 VAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDI----------TVDADEYIRHGATLDSMAKLRP 233
Cdd:PRK09052 161 VAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDLatgevdvktrTVDLDEGPRADTSLEGLAKLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 234 AFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLV 313
Cdd:PRK09052 241 VFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2VTZ_B 314 EANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:PRK09052 321 ELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFERL 399
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
5-390 |
8.99e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 337.46 E-value: 8.99e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVGSFN------GAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQN-PARQAAMKAGVP 77
Cdd:PRK06445 4 VYLVDFARTAFSRFRpkdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPIFLARLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 78 QEATAWGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPhcahlrggvkMGDFKMIDTMIKdGLTDAFY---- 153
Cdd:PRK06445 84 YNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP----------MGDNPHIEPNPK-LLTDPKYieyd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 154 ---GYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAK 230
Cdd:PRK06445 153 lttGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 231 LRPAFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDL 310
Cdd:PRK06445 233 LPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 311 DLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK06445 313 DLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLE 392
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
5-390 |
1.27e-113 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 339.05 E-value: 1.27e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAV-GSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVL-PAGEGQNPARQAAMKAGVPQEATA 82
Cdd:PLN02287 48 VVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLaPGSQRANECRMAAFYAGFPETVPV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 83 WGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPhcAHLRGGV--KMGDFKMI-DTMIKdgltdafygyhMGT 159
Cdd:PLN02287 128 RTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNP--MAWEGGVnpRVESFSQAqDCLLP-----------MGI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 160 TAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPF---IVKGRKGD---ITVDADEYIRHGATLDSMAKLRP 233
Cdd:PLN02287 195 TSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkIVDPKTGEekpIVISVDDGIRPNTTLADLAKLKP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 234 AFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLV 313
Cdd:PLN02287 275 VFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLF 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2VTZ_B 314 EANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRG--ARKGLATLCIGGGMGVAMCIE 390
Cdd:PLN02287 355 EINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFE 433
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
5-390 |
1.27e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 329.28 E-value: 1.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 84
Cdd:PRK06366 4 VYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTKYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHC--AHLRGGVKM---GDFKMIDTMIKDGLTDAFYGYHMGT 159
Cdd:PRK06366 84 VNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLlpSDLRWGPKHllhKNYKIDDAMLVDGLIDAFYFEHMGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 160 TAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIvkgrkgdiTVDADEYIRHgATLDSMAKLRPAFDKEG 239
Cdd:PRK06366 164 SAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIRK-TTMEDLAKLPPAFDKNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 240 TVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAF 319
Cdd:PRK06366 235 ILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNEAF 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2VTZ_B 320 AAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK06366 315 SIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
19-390 |
9.94e-104 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 312.20 E-value: 9.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 19 NGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWGMNQLAGSGLRAVA 97
Cdd:PRK08242 20 DGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDqGADIARTAVLAAGLPETVPGVQINRFCASGLEAVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 98 LGMQQIATGDASIIVAGGMESMSMAPHcahlrgGVKMGDFKMiDTMIkdgltdAFYGYHM--GTTAENVAKQWQLSRDEQ 175
Cdd:PRK08242 100 LAAAKVRSGWDDLVIAGGVESMSRVPM------GSDGGAWAM-DPST------NFPTYFVpqGISADLIATKYGFSREDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 176 DAFAVASQNKAEAAQKDGRFKDEIVPfiVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTV-------------- 241
Cdd:PRK08242 167 DAYAVESQQRAAAAWAEGYFAKSVVP--VKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMggfdavalqkypev 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 242 -------TAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVE 314
Cdd:PRK08242 245 erinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDLFE 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2VTZ_B 315 ANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK08242 325 LNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIE 400
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
3-392 |
2.67e-102 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 308.24 E-value: 2.67e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 3 PSIVIASAARTAVG-SFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAG-EGQNPARQAAMKAGVPQEA 80
Cdd:PRK07108 2 TEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 81 TAWGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHcahlrggvKMGDFKMIDTMIKDGLTDAFYgyHMGTT 160
Cdd:PRK07108 82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQN--------EMNRHMLREGWLVEHKPEIYW--SMLQT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 161 AENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD----------ITVDADEYIRHGATLDSMAK 230
Cdd:PRK07108 152 AENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADkatgrlftkeVTVSADEGIRPDTTLEGVSK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 231 LRPAFDKeGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDL 310
Cdd:PRK07108 232 IRSALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 311 DLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK07108 311 DLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
|
..
2VTZ_B 391 SL 392
Cdd:PRK07108 391 VL 392
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
7-390 |
3.91e-101 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 305.55 E-value: 3.91e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 7 IASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWGM 85
Cdd:PRK08131 6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 86 NQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMI-----KDGLTDAFYGYHMGTT 160
Cdd:PRK08131 86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTTIgarfpNPKIVAQYGNDSMPET 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 161 AENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVK--GRKGDITVDADEYIRHGATLDSMAKLRPAFDkE 238
Cdd:PRK08131 166 GDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPqgRKLPPKLVAEDEHPRPSSTVEALTKLKPLFE-G 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 239 GTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEA 318
Cdd:PRK08131 245 GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEA 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2VTZ_B 319 FAAQACAVNKDLG--WDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK08131 325 FASQVLGCLKGLGvdFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
3-392 |
1.73e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 298.84 E-value: 1.73e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 3 PSIVIASAARTAVG-SFNGAFANTPAHELGATVISAVLERA-GVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQE 79
Cdd:PRK07851 2 PEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 80 ATAwGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMS---------------------MAPHCAHLRGGVKMGDfk 138
Cdd:PRK07851 82 PGT-TVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnsdslpdtknplfaeaQARTAARAEGGAEAWH-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 139 miDTMIKDGLTDAFYGyhMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPfiVKGRKGdITVDADEY 218
Cdd:PRK07851 159 --DPREDGLLPDVYIA--MGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITP--VTLPDG-TVVSTDDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 219 IRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRK 298
Cdd:PRK07851 232 PRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 299 ALERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLC 378
Cdd:PRK07851 312 ALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMC 391
|
410
....*....|....
2VTZ_B 379 IGGGMGVAMCIESL 392
Cdd:PRK07851 392 VGGGQGMAMVLERL 405
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
5-390 |
4.74e-98 |
|
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: 297.24 E-value: 4.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVG-SFNGAFANTPAHELGATVISAVLER-AGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEAT 81
Cdd:TIGR02445 2 VVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVQQTLEqGFNIARNAALLAQIPHTSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 82 AWGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPhcahLRGGVKMGDFKMIDTMIKDGLtdafygyhMGTTA 161
Cdd:TIGR02445 82 AVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP----MMHGVDFHPGMSLHVAKAAGM--------MGLTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 162 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPfiVKGRKGD---ITVDADEYIRHGATLDSMAKLRPAFD-K 237
Cdd:TIGR02445 150 EMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIP--TQGHDADgflKQFDYDEVIRPETTVESLAALRPAFDpK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 238 EGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANE 317
Cdd:TIGR02445 228 NGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2VTZ_B 318 AFAAQACAVNKDLGWDPSI---VNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:TIGR02445 308 AFAAQALPCLKDLGLLDKMdekVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
11-392 |
1.39e-93 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 286.91 E-value: 1.39e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 11 ARTAVGSFNGAfantpahELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLAG 90
Cdd:PRK08170 18 ARGGPGPFSAS-------DLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 91 SGLRAVALGMQQIATGDASIIVAGGMESMSMAP----------------------HCAHLrGGVKMGDFKMIDTMIKdGL 148
Cdd:PRK08170 91 SGMQALDSAAANIALGRADLVLAGGVEAMSHAPllfsekmvrwlagwyaaksigqKLAAL-GKLRPSYLAPVIGLLR-GL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 149 TDAFYGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKdEIVPFIvkGRKGDItVDADEYIRHGATLDSM 228
Cdd:PRK08170 169 TDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLF--DRDGKF-YDHDDGVRPDSSMEKL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 229 AKLRPAFDKE-GTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKI 307
Cdd:PRK08170 245 AKLKPFFDRPyGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 308 GDLDLVEANEAFAAQ--AC--AVNKD------LGW-------DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGA 370
Cdd:PRK08170 325 EDLDLWEINEAFAAQvlAClaAWADEeycreqLGLdgalgelDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGT 404
|
410 420
....*....|....*....|..
2VTZ_B 371 RKGLATLCIGGGMGVAMCIESL 392
Cdd:PRK08170 405 KRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
7-392 |
2.40e-91 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 279.67 E-value: 2.40e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 7 IASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAG-EGQNPARQAAMKAGVPQEATAWGM 85
Cdd:PRK07801 6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpQAGNIARTSWLAAGLPEEVPGVTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 86 NQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMG------DFKMIDTMIKDGLTDAFYGyhmgt 159
Cdd:PRK07801 86 DRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGftspfaESKGWLHRYGDQEVSQFRG----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 160 tAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFivkgrkGDITVDadEYIRHgATLDSMAKLRPAFDkEG 239
Cdd:PRK07801 161 -AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV------GGVTVD--EGPRE-TSLEKMAGLKPLVE-GG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 240 TVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAF 319
Cdd:PRK07801 230 RLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAF 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2VTZ_B 320 AAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:PRK07801 310 APVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIERL 382
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
6-392 |
3.11e-88 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 271.98 E-value: 3.11e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 6 VIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWG 84
Cdd:PRK07850 5 VIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGATT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLrgGVKMGDFKMIDTMIKDGltDAFygyhmgTTAENV 164
Cdd:PRK07850 85 IDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANA--GPGRGLPRPDSWDIDMP--NQF------EAAERI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 165 AKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFI--VKGRKGDIT-----VDADEYIRHgATLDSMAKLRPAFDk 237
Cdd:PRK07850 155 AKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapVLDEEGQPTgetrlVTRDQGLRD-TTMEGLAGLKPVLE- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 238 EGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANE 317
Cdd:PRK07850 233 GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2VTZ_B 318 AFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:PRK07850 313 AFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIERI 387
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
5-390 |
4.32e-87 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 270.32 E-value: 4.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 5 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 84
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 85 MNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAP-----HCAH----LRGGVKMGD-FKMIDTM-IKD------G 147
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskKLARalvdLNKARTLGQrLKLFSRLrLRDllpvppA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 148 LTDAFYGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGdiTVDADEYIRHGATLDS 227
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ--PLEEDNNIRGDSTLED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 228 MAKLRPAFD-KEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDP-KVMGTGPIPASRKALERAGW 305
Cdd:PRK08963 245 YAKLRPAFDrKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLALERAGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 306 KIGDLDLVEANEAFAAQACA----------VNKDLGW-------DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRR 368
Cdd:PRK08963 325 TLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLGRsqaigevDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRR 404
|
410 420
....*....|....*....|..
2VTZ_B 369 GARKGLATLCIGGGMGVAMCIE 390
Cdd:PRK08963 405 GGGLGLTTACAAGGLGAAMVLE 426
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
7-392 |
1.87e-85 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 265.05 E-value: 1.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 7 IASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWGM 85
Cdd:PRK06504 6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEqATNVARNAVLASKLPESVPGTSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 86 NQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGttAENVA 165
Cdd:PRK06504 86 DRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNGLGHYKSPGMEERYPGIQFSQFTG--AEMMA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 166 KQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITV-DADEYIRHGATLDSMAKLRPaFDKEGTVTAG 244
Cdd:PRK06504 164 KKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMhTVDEGIRFDATLEGIAGVKL-IAEGGRLTAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 245 NASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQAC 324
Cdd:PRK06504 243 TASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASVPL 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2VTZ_B 325 AVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:PRK06504 323 AWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL 390
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
3-392 |
5.68e-77 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 243.91 E-value: 5.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 3 PSIVIASAARTAVG---SFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAG-EGQNPARQAAMKAGVPQ 78
Cdd:PRK06025 2 AEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGkQGGDLGRMAALDAGYDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 79 EATAWGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKdgLTDAFYGYHMG 158
Cdd:PRK06025 82 KASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGKPPLGMGSGNLR--LRALHPQSHQG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 159 TTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPfiVKGRKGDITVDADEYIRHGATLDSMAKLRPAF--- 235
Cdd:PRK06025 160 VCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVP--VYRDDGSVALDHEEFPRPQTTAEGLAALKPAFtai 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 236 -----DKEGTV------------------TAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGP 292
Cdd:PRK06025 238 adyplDDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 293 IPASRKALERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARK 372
Cdd:PRK06025 318 VPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKR 397
|
410 420
....*....|....*....|
2VTZ_B 373 GLATLCIGGGMGVAMCIESL 392
Cdd:PRK06025 398 GLVTMCAAGGMAPAIIIERV 417
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
6-392 |
2.24e-74 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 235.43 E-value: 2.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 6 VIASAARTAVGSFNGAFANTPAHELGATVI---SAVLERagvaagEVNEVILGQVLpaGEGQNPARQAAMKAGVPQEATA 82
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLtflSKGMER------EIDDVILGNVV--GPGGNVARLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 83 WGMNQLAGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLR-GGVKMGDfkmidtmikdgltdafygYHMGTTA 161
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARfSPETIGD------------------PDMGVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 162 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFivkgrkGDITVDADEYIRHGATLDSMAKlrPAFDKEGTV 241
Cdd:PRK06690 138 EYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF------NGLLDESIKKEMNYERIIKRTK--PAFLHNGTV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 242 TAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAA 321
Cdd:PRK06690 210 TAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFAS 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2VTZ_B 322 QACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 392
Cdd:PRK06690 290 KVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
270-390 |
9.82e-65 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 202.10 E-value: 9.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 270 QPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHP 349
Cdd:pfam02803 2 KPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
2VTZ_B 350 IGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 390
Cdd:pfam02803 82 LGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
19-391 |
1.66e-55 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 188.19 E-value: 1.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 19 NGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLAGSGLRAVAL 98
Cdd:PRK09268 23 NGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYDLQQACGTGLEAAIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 99 GMQQIATGDASIIVAGGMESMSMAPHCAH--LR-------------------GGVKMGDFKMIDTMIKDGLTdafyGYHM 157
Cdd:PRK09268 103 VANKIALGQIDSGIAGGVDTTSDAPIAVNegLRkillelnrakttgdrlkalGKLRPKHLAPEIPRNGEPRT----GLSM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 158 GTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFivkgrKGditVDADEYIRHGATLDSMAKLRPAFDK 237
Cdd:PRK09268 179 GEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-----LG---LTRDNNLRPDSSLEKLAKLKPVFGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 238 --EGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDpKVMG-----TGPIPASRKALERAGWKIGDL 310
Cdd:PRK09268 251 ggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVD-FVHGkegllMAPAYAVPRLLARNGLTLQDF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 311 DLVEANEAFAAQACAVNK----------DLGW-------DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKG 373
Cdd:PRK09268 330 DFYEIHEAFASQVLATLKawedeeycreRLGLdaplgsiDRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEKGSGRG 409
|
410
....*....|....*...
2VTZ_B 374 LATLCIGGGMGVAMCIES 391
Cdd:PRK09268 410 LISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
27-389 |
7.67e-51 |
|
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: 171.09 E-value: 7.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 27 AHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPqEATAWGMNQLAGSGLRAVALGMQQIATG 106
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 107 DASIIVAGGMESmsmaphcahlrggvkmgdfkmidtmikdgltdafygyhmgttaenvakqwqlsrdeqdafavasqnka 186
Cdd:cd00327 86 KADIVLAGGSEE-------------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 187 eaaqkdgrfkdeivpfivkgrkgditvdadeyirhgatldsmaklrpafdkegtvtagnaSGLNDGAAAALLMSEAEASR 266
Cdd:cd00327 98 ------------------------------------------------------------FVFGDGAAAAVVESEEHALR 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 267 RGIQPLGRIVSWATVGVD----PKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIV---NV 339
Cdd:cd00327 118 RGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspAV 197
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
2VTZ_B 340 NGGAIAIGHPIGASGARILNTLLFEMK-------RRGARKGLATLCIGGGMGVAMCI 389
Cdd:cd00327 198 SATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
20-361 |
4.88e-09 |
|
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: 57.66 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 20 GAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPqEATAWGMNQLAGSGLRAVALG 99
Cdd:cd00829 9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLL-GKPATRVEAAGASGSAAVRAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 100 MQQIATGDASIIVAGGMESMSMAPHCAHLRGGVkmGDFKMIDTMIKDGLT--DAF------YGYHMGTTAENVAKqwqls 171
Cdd:cd00829 88 AAAIASGLADVVLVVGAEKMSDVPTGDEAGGRA--SDLEWEGPEPPGGLTppALYalaarrYMHRYGTTREDLAK----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 172 rdeqdafaVASQNKAEA-----AQkdgrfkdeivpfivkgRKGDITVDadeyirhgatlDSMAKlRPAFDKegtVTAGNA 246
Cdd:cd00829 161 --------VAVKNHRNAarnpyAQ----------------FRKPITVE-----------DVLNS-RMIADP---LRLLDC 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 247 SGLNDGAAAALLMSEAEASRRGIQPLgRIVSWAtVGVDPKVMG--------TGPIPASRKALERAGWKIGDLDLVEANEA 318
Cdd:cd00829 202 CPVSDGAAAVVLASEERARELTDRPV-WILGVG-AASDTPSLSerddflslDAARLAARRAYKMAGITPDDIDVAELYDC 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
2VTZ_B 319 FAA---------------QACAVNKD----LGWDPSiVNVNGGAIAIGHPIGASGARILNTL 361
Cdd:cd00829 280 FTIaellaledlgfcekgEGGKLVREgdtaIGGDLP-VNTSGGLLSKGHPLGATGLAQAVEA 340
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
238-381 |
1.30e-06 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 50.07 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 238 EGTVTAGNASGLNDGAAAALLMSEAEASR-RGIQPLGRIVSW----ATVGVDPKVMGT--GP--IPASRK----ALERAG 304
Cdd:PRK06289 211 EGRLRRQDCSQVTDGGAGVVLASDAYLRDyADARPIPRIKGWghrtAPLGLEQKLDRSagDPyvLPHVRQavldAYRRAG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 305 WKIGDLDLVEANEAFAAQACAVNKDLG-------W----DPSI-------VNVNGGAIAIGHPIGASGARILNTLLFEMK 366
Cdd:PRK06289 291 VGLDDLDGFEVHDCFTPSEYLAIDHIGltgpgesWkaieNGEIaiggrlpINPSGGLIGGGHPVGASGVRMLLDAAKQVT 370
|
170 180
....*....|....*....|..
2VTZ_B 367 RR-------GARKGLaTLCIGG 381
Cdd:PRK06289 371 GTagdyqveGAKTFG-TLNIGG 391
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
235-355 |
1.54e-06 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 49.67 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 235 FDK--EGTVtagnasgLNDGAAAALLMSEAEASRRGIQPLGRIVSW-----ATVGVDPKVMGTGPIPASRKALERAGWKI 307
Cdd:PRK05952 199 FDRqrEGLV-------LGEGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTP 271
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
2VTZ_B 308 GDLDLVEA-------NEAFAAQACAVnkdlgWDPSIVNVNGGAIAIGHPIGASGA 355
Cdd:PRK05952 272 EDIDYIHAhgtatrlNDQREANLIQA-----LFPHRVAVSSTKGATGHTLGASGA 321
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
232-355 |
8.13e-06 |
|
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: 47.53 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 232 RPaFDKE--GTVtagnasgLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVG-----VDPKVMGTGPIPASRKALERAG 304
Cdd:cd00834 218 RP-FDKDrdGFV-------LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAG 289
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
2VTZ_B 305 WKIGDLDLV-------EANEAFAAQAC-AVNKDLGWDPSIVNVNGgaiAIGHPIGASGA 355
Cdd:cd00834 290 LSPEDIDYInahgtstPLNDAAESKAIkRVFGEHAKKVPVSSTKS---MTGHLLGAAGA 345
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
226-355 |
4.87e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 45.11 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 226 DSMAKLRPaFDKegtvtagNASGLNDGAAAALLMSEAE--ASRRGIQPLGRIVSWATVG-----VDPKVMGTGPIPASRK 298
Cdd:PRK07910 223 DPAGACRP-FDK-------DRDGFVFGEGGALMVIETEehAKARGANILARIMGASITSdgfhmVAPDPNGERAGHAMTR 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
2VTZ_B 299 ALERAGWKIGDLDLVEANEAFA-----AQACAVNKDLGWDPSIVNVNGGAIaiGHPIGASGA 355
Cdd:PRK07910 295 AIELAGLTPGDIDHVNAHATGTsvgdvAEGKAINNALGGHRPAVYAPKSAL--GHSVGAVGA 354
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
295-356 |
5.91e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 44.89 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 295 ASRKALERAGWKIGDLDLVEANEAFA-AQACAVnKDLGW-----------------DPSI-VNVNGGAIAIGHPIGASGA 355
Cdd:PRK06064 263 AAEKAYKMAGIEPKDIDVAEVHDCFTiAEILAY-EDLGFakkgeggklaregqtyiGGDIpVNPSGGLKAKGHPVGATGV 341
|
.
2VTZ_B 356 R 356
Cdd:PRK06064 342 S 342
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
247-366 |
1.72e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 43.34 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 247 SGLNDGAAAALLMSEAEASRRGIQPL-GRIVSWATVGV----------DPKVMGTGpIPASRKALERAGWKIGDLDLVEA 315
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEIKSLACasgnlyedppDATRMFTS-RAAAQKALSMAGVKPSDLQVAEV 334
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2VTZ_B 316 NEAFAAQACAVNKDLGW-DPS-----------------IVNVNGGAIAIGHPIGASGARILNTLLFEMK 366
Cdd:PTZ00455 335 HDCFTIAELLMYEALGIaEYGhakdlirngatalegriPVNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
251-386 |
4.23e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 42.24 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 251 DGAAAALLMSEAEASRrgiqpLGRIVSW-ATVGV---------DPKVMgTGPIPASRKALERAGWKIGDLDLVEANEAF- 319
Cdd:PRK07516 217 DGAAALVLADAETARA-----LQRAVRFrARAHVndflplsrrDPLAF-EGPRRAWQRALAQAGVTLDDLSFVETHDCFt 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 320 -----------------AAQACA---VNKDlGWDPsiVNVNGGAIAIGHPIGASG-------ARILNTLLFEMKRRGARk 372
Cdd:PRK07516 291 iaelieyeamglappgqGARAIRegwTAKD-GKLP--VNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPGAK- 366
|
170
....*....|....
2VTZ_B 373 gLATLCIGGGMGVA 386
Cdd:PRK07516 367 -LAGVFNMGGAAVA 379
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
232-355 |
5.85e-04 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 41.62 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 232 RPaFDKegtvtagNASGLN--DGAAAALLMSEAEASRRGIQPLGRIVSWAT-------VGVDPKvmGTGPIPASRKALER 302
Cdd:COG0304 218 RP-FDK-------DRDGFVlgEGAGVLVLEELEHAKARGAKIYAEVVGYGAssdayhiTAPAPD--GEGAARAMRAALKD 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
2VTZ_B 303 AGWKIGDLDLV-------EANEafAAQACAVNKDLGWDPSIVNVNggAI--AIGHPIGASGA 355
Cdd:COG0304 288 AGLSPEDIDYInahgtstPLGD--AAETKAIKRVFGDHAYKVPVS--STksMTGHLLGAAGA 345
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
251-366 |
1.02e-03 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 40.70 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 251 DGAAAALLMSEAEASRRGIQPLGRIVSWA-----TVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACA 325
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAatidgAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDV 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....
2VTZ_B 326 VNKDLGWD---PSIVNVNGGAIAIGHPIGASGARILNTLLFEMK 366
Cdd:cd00825 241 KELKLLRSefgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
241-354 |
1.56e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 40.28 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 241 VTAGNASGLNDGAAAALLMSEAEASRRGIQPLgrIVSWATVGVD---PKVMGTGPIP----------------------- 294
Cdd:PRK06365 217 LTRLDVCAMSDGAACAILASEDKAFEITDKPV--LIKAIGTGSDtlrLADRPFGEVPllpnespddykdlrypgvhsfra 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VTZ_B 295 ---ASRKALERAGWK--IGDLDLVEANEAFAAQACAVNKDLGW-------------DPSI-----VNVNGGAIAIGHPIG 351
Cdd:PRK06365 295 grmAAKEAYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgKPELpgklpVNPSGGLLAAGHAVG 374
|
...
2VTZ_B 352 ASG 354
Cdd:PRK06365 375 ATG 377
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
252-315 |
1.77e-03 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 40.01 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2VTZ_B 252 GAAAALLMSEAEASRRGIQPLGRIVSW-----ATVGVDPKVmgTGPIPASRKALERAGWKIGDLDLVEA 315
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWsmrldANRGPDPSL--EGEMRVIRAALRRAGLGPEDIDYVNP 306
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
252-315 |
5.09e-03 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 38.57 E-value: 5.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2VTZ_B 252 GAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERA----GWKIGDLDLVEA 315
Cdd:cd00828 232 GAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGIARAIRTAlakaGLSLDDLDVISA 299
|
|
| |
