|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
8-396 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 618.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWS 87
Cdd:PRK05790 4 VVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPALT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 88 CQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPH-LAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAEN 166
Cdd:PRK05790 84 INKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHvLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 167 VAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTgt 245
Cdd:PRK05790 164 LAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGdPVVVDTDEHPRPDTTAESLAKLRPAFDKDGT-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 246 VTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFA 325
Cdd:PRK05790 242 VTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539872 326 AVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PRK05790 322 AQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
9-396 |
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: 584.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 9 VIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSC 88
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 89 QMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVA 168
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 169 KKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFltDGTGTVTP 248
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAF--KKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 249 ANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVS 328
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539872 329 AAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
6-396 |
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: 556.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 6 DPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPA 85
Cdd:COG0183 2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 86 WSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAY-LRTGVKiGEMPLTDSILCDGLTDAFHNCHMGITA 164
Cdd:COG0183 82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPkARWGYR-MNAKLVDPMINPGLTDPYTGLSMGETA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 165 ENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTg 244
Cdd:COG0183 161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 245 tVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAF 324
Cdd:COG0183 240 -VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148539872 325 AAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:COG0183 319 AAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
10-395 |
1.84e-169 |
|
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: 479.03 E-value: 1.84e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 10 IVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQ 89
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 90 MICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAY--LRTGVKIGEMPLTDSILCDgLTDAFHNCHMGITAENV 167
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPrsLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 168 AKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFltDGTGTVT 247
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF--DPDGTVT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 248 PANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAV 327
Cdd:TIGR01930 238 AGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQ 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539872 328 SAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQ 395
Cdd:TIGR01930 318 VLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
8-396 |
5.42e-158 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 450.18 E-value: 5.42e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPV-RQASVGAGIPYSVPAW 86
Cdd:PRK09051 5 VVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLsRVAAINAGVPQETPAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 87 SCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLA-YLRTGVKIGEMPLTDSILcDGLTDAFHNCHMGITAE 165
Cdd:PRK09051 85 NVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpAARWGARMGDAKLVDMMV-GALHDPFGTIHMGVTAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 166 NVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGtGT 245
Cdd:PRK09051 164 NVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKEN-GT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 246 VTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFA 325
Cdd:PRK09051 243 VTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAFA 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539872 326 AVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PRK09051 323 AQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
8-396 |
8.34e-152 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 434.32 E-value: 8.34e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWS 87
Cdd:PRK05656 4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAMT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 88 CQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPH-LAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAEN 166
Cdd:PRK05656 84 LNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYvLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 167 VAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTgt 245
Cdd:PRK05656 164 LVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGePLAFATDEQPRAGTTAESLAKLKPAFKKDGS-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 246 VTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFA 325
Cdd:PRK05656 242 VTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539872 326 AVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PRK05656 322 AQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
7-395 |
6.19e-144 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 414.43 E-value: 6.19e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 7 PVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAW 86
Cdd:PRK06633 4 PVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 87 SCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAEN 166
Cdd:PRK06633 84 TINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 167 VAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFltDGTGTV 246
Cdd:PRK06633 164 ISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAF--DKNGVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 247 TPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAA 326
Cdd:PRK06633 242 TAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539872 327 VSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQ 395
Cdd:PRK06633 322 QSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
9-395 |
2.97e-139 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 402.55 E-value: 2.97e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 9 VIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSC 88
Cdd:PRK08235 5 VIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 89 QMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPH-LAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENV 167
Cdd:PRK08235 85 NKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYiLPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVYGGEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 168 AKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFltDGTGTV 246
Cdd:PRK08235 165 AKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGdPIVVAKDEAPRKDTTIEKLAKLKPVF--DKTGTI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 247 TPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAA 326
Cdd:PRK08235 243 TAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539872 327 VSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQ 395
Cdd:PRK08235 323 VALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
8-396 |
2.45e-135 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 392.53 E-value: 2.45e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWS 87
Cdd:PLN02644 3 VCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 88 CQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPH-LAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAEN 166
Cdd:PLN02644 83 VNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKyLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 167 VAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG--LIEVKTDEFPRHgSNIEAMSKLKPYFLTDGtG 244
Cdd:PLN02644 163 CADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGrpSVIVDKDEGLGK-FDPAKLRKLRPSFKEDG-G 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 245 TVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAF 324
Cdd:PLN02644 241 SVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148539872 325 AAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PLN02644 321 SVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
8-396 |
1.08e-124 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 365.85 E-value: 1.08e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWS 87
Cdd:PRK06205 4 AVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPGMQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 88 CQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAY-LRTGVKIGEMPLTDSiLCDGLTDAFHNCH-----MG 161
Cdd:PRK06205 84 LDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdMRWGVRGGGVQLHDR-LARGRETAGGRRFpvpggMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 162 ITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFL- 239
Cdd:PRK06205 163 ETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGdPTVVDRDEHPRADTTLESLAKLRPIMGk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 240 TDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFE 319
Cdd:PRK06205 243 QDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLIE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 320 INEAFAAVSAAIVKELGLNP---EKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PRK06205 323 LNEAFAAQVLAVLKEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAVFER 402
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-395 |
3.55e-119 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 351.50 E-value: 3.55e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 1 MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIP 80
Cdd:PRK06954 2 TAVDQDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 81 YSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHL-AYLRTGVKIGEMPLTDSILCDGLTDAFHNCH 159
Cdd:PRK06954 82 LSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLlPKARGGMRMGHGQVLDHMFLDGLEDAYDKGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 160 -MGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHgSNIEAMSKLKPYF 238
Cdd:PRK06954 162 lMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 239 LTDGTgtVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIF 318
Cdd:PRK06954 241 SKTGT--VTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539872 319 EINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQ 395
Cdd:PRK06954 319 EINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
8-396 |
5.95e-119 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 351.18 E-value: 5.95e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKR-ATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPA 85
Cdd:PRK09050 4 AFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGeDNRNVARMSALLAGLPVSVPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 86 WSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHL------AYLRTG----VKIG---------EMPLTDSi 146
Cdd:PRK09050 84 TTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVmgkadsAFSRQAeifdTTIGwrfvnplmkAQYGVDS- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 147 lcdgltdafhnchMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHG 225
Cdd:PRK09050 163 -------------MPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGdPVVVDRDEHPRPE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 226 SNIEAMSKLKPYFLTDGTgtVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAV 305
Cdd:PRK09050 230 TTLEALAKLKPVFRPDGT--VTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 306 TKAGWSLEDVDIFEINEAFAAVSAAIVKELGL--NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALC 383
Cdd:PRK09050 308 ARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMC 387
|
410
....*....|...
gi 148539872 384 IGGGMGIAMCVQR 396
Cdd:PRK09050 388 IGVGQGIALAIER 400
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
8-267 |
4.96e-110 |
|
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: 323.10 E-value: 4.96e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWS 87
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 88 CQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAY--LRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAE 165
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 166 NVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFltDGTGT 245
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAF--DKEGT 238
|
250 260
....*....|....*....|..
gi 148539872 246 VTPANASGINDGAAAVVLMKKS 267
Cdd:pfam00108 239 VTAGNASPINDGAAAVLLMSES 260
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
9-391 |
6.80e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 327.86 E-value: 6.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 9 VIVSAARTIIGSFN-GALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLA-AGCGQNPVRQASVGAGIPYSVPAW 86
Cdd:PRK07661 5 VIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPeAEQGLNMARNIGALAGLPYTVPAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 87 SCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAY-LRTGVKIGEmpltdsilcdglTDAFHNCHMGITAE 165
Cdd:PRK07661 85 TINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHvVRPNPRLVE------------AAPEYYMGMGHTAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 166 NVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRK-----GLIEVK----TDEFPRHGSNIEAMSKLKP 236
Cdd:PRK07661 153 QVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgennKLQEETitfsQDEGVRADTTLEILGKLRP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 237 YFLTDGTgtVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVD 316
Cdd:PRK07661 233 AFNVKGS--VTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIG 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539872 317 IFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIA 391
Cdd:PRK07661 311 LFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAA 385
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
1-397 |
1.86e-109 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 328.65 E-value: 1.86e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 1 MNAGSDPVVIVSAART-IIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQ-NPVRQASVGAG 78
Cdd:PLN02287 41 TTAFGDDVVIVAAYRTpICKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 79 IPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPltdsilcdgltDAfHNC 158
Cdd:PLN02287 121 FPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFS-----------QA-QDC 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 159 --HMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPV---LVSTRKG---LIEVKTDEFPRHGSNIEA 230
Cdd:PLN02287 189 llPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkIVDPKTGeekPIVISVDDGIRPNTTLAD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 231 MSKLKPYFLTDgtGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGW 310
Cdd:PLN02287 269 LAKLKPVFKKN--GTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 311 SLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSR--GVAALCIGGGM 388
Cdd:PLN02287 347 ELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKDCrfGVVSMCIGTGM 426
|
....*....
gi 148539872 389 GIAMCVQRE 397
Cdd:PLN02287 427 GAAAVFERG 435
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
8-396 |
7.11e-109 |
|
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: 325.58 E-value: 7.11e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKR-ATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPA 85
Cdd:TIGR02430 3 AYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGeDNRNVARMAALLAGLPVSVPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 86 WSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHL------AYLRTgVKIGEMPLTDSILCDGLTDAFHNCH 159
Cdd:TIGR02430 83 TTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVmgkadsAFSRS-AKIEDTTIGWRFINPLMKALYGVDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 160 MGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGL-IEVKTDEFPRHGSNIEAMSKLKPYF 238
Cdd:TIGR02430 162 MPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEpTVVDQDEHPRPETTLEGLAKLKPVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 239 LTDGTgtVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIF 318
Cdd:TIGR02430 242 RPDGT--VTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 319 EINEAFAAVSAAIVKELGL--NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:TIGR02430 320 ELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
10-396 |
4.53e-103 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 310.56 E-value: 4.53e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 10 IVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWSC 88
Cdd:PRK08131 6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGeDSRNVARNALLLAGLPVTVPGQTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 89 QMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHL------AYLRTgVKIGEMPLTDSILCDGLTDAFHNCHMGI 162
Cdd:PRK08131 86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVmgkaesAFSRD-AKVFDTTIGARFPNPKIVAQYGNDSMPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 163 TAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVST--RKGLIEVKTDEFPRHGSNIEAMSKLKPYFlt 240
Cdd:PRK08131 165 TGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgrKLPPKLVAEDEHPRPSSTVEALTKLKPLF-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 241 DGtGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEI 320
Cdd:PRK08131 243 EG-GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEI 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539872 321 NEAFAAVSAAIVKELGL--NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PRK08131 322 NEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIER 399
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
10-391 |
2.03e-100 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 303.85 E-value: 2.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 10 IVSAARTIIG-SFNGALAAVPVQDLGSTVIKEVLKRA-TVAPEDVSEVIFGHVLA-AGCGQNPVRQASVGAGIPYSVPAW 86
Cdd:PRK09052 10 IVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPeAEQGLNVARIGALLAGLPNSVGGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 87 SCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLaylrtgvkiGEMP-LTDSILC--DGLTDAFHnchMGIT 163
Cdd:PRK09052 90 TVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMM---------GNKPsMSPAIFArdENVGIAYG---MGLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 164 AENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRK-----GLIEVKT-----DEFPRHGSNIEAMSK 233
Cdd:PRK09052 158 AEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatGEVDVKTrtvdlDEGPRADTSLEGLAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 234 LKPYFltDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLE 313
Cdd:PRK09052 238 LKPVF--ANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQD 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539872 314 DVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIA 391
Cdd:PRK09052 316 DLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAA 393
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
8-396 |
2.86e-100 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 303.04 E-value: 2.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIG-SFNGALAAVPVQDLGSTVIKEVLKR-ATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVP 84
Cdd:PRK08947 4 VVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPHSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 85 AWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMskaphlaylrtgvkiGEMPLTDSIlcD-----GLTDAFHNCH 159
Cdd:PRK08947 84 AVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM---------------GHVPMNHGV--DfhpglSKNVAKAAGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 160 MGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYF 238
Cdd:PRK08947 147 MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGvLKLFDYDEVIRPETTVEALAALRPAF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 239 lTDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIF 318
Cdd:PRK08947 227 -DPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 319 EINEAFAAVSAAIVKELGL---NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQ 395
Cdd:PRK08947 306 ELNEAFAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
.
gi 148539872 396 R 396
Cdd:PRK08947 386 R 386
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
9-396 |
1.87e-99 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 301.54 E-value: 1.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 9 VIVSAARTIIG-SFNGALAAVPVQDLGSTVIKEVL-KRATVAPEDVSEVIFGHVLAAGC-GQNPVRQASVGAGIPySVPA 85
Cdd:PRK07851 5 VIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALdKVPALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYD-FLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 86 WSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPH---------------LAYLRTG--VKIGEMPLTDSILC 148
Cdd:PRK07851 84 TTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKgnsdslpdtknplfaEAQARTAarAEGGAEAWHDPRED 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 149 DGLTDAFhnCHMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVlvSTRKGLIeVKTDEFPRHGSNI 228
Cdd:PRK07851 164 GLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPV--TLPDGTV-VSTDDGPRAGTTY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 229 EAMSKLKPYFLTDGTgtVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKA 308
Cdd:PRK07851 239 EKVSQLKPVFRPDGT--VTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 309 GWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGM 388
Cdd:PRK07851 317 GMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGGGQ 396
|
....*...
gi 148539872 389 GIAMCVQR 396
Cdd:PRK07851 397 GMAMVLER 404
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
10-396 |
4.87e-99 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 299.70 E-value: 4.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 10 IVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGcGQ--NPVRQASVGAGIPYSVPAWS 87
Cdd:PRK07801 6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQagNIARTSWLAAGLPEEVPGVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 88 CQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIG-EMPLTDSILC-----DGLTDAFHNchmg 161
Cdd:PRK07801 85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGfTSPFAESKGWlhrygDQEVSQFRG---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 162 itAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLvstrkgliEVKTDEFPRHgSNIEAMSKLKPyfLTD 241
Cdd:PRK07801 161 --AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG--------GVTVDEGPRE-TSLEKMAGLKP--LVE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 242 GtGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEIN 321
Cdd:PRK07801 228 G-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEIN 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539872 322 EAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PRK07801 307 EAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
32-397 |
5.54e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 297.40 E-value: 5.54e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 32 DLGSTVIKEVLKRATVAPEDVSEVIFGhvLAAGCGQNPV---RQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGI 108
Cdd:PRK06445 34 ELAAMLINRLIEKTGIKPEEIDDIITG--CALQVGENWLyggRHPIFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIAT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 109 GDSSIVVAGGMENMSKAPhlAYLRTGVKIGEMPLTDSILCD-GLTDAFHnchMGITAENVAKKWQVSREDQDKVAVLSQN 187
Cdd:PRK06445 112 GMADIVIAGGVEHMTRTP--MGDNPHIEPNPKLLTDPKYIEyDLTTGYV---MGLTAEKLAEEAGIKREEMDRWSLRSHQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 188 RTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTgtVTPANASGINDGAAAVVLMKKS 267
Cdd:PRK06445 187 LAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKPDGV--ITAGNSSPLNSGASYVLLMSKK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 268 EADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGG 347
Cdd:PRK06445 265 AVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGG 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 148539872 348 AIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE 397
Cdd:PRK06445 345 AIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
8-389 |
4.55e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 292.30 E-value: 4.55e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWS 87
Cdd:PRK06366 4 VYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTKYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 88 CQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHL--AYLRTGVK---IGEMPLTDSILCDGLTDAFHNCHMGI 162
Cdd:PRK06366 84 VNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLlpSDLRWGPKhllHKNYKIDDAMLVDGLIDAFYFEHMGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 163 TAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLvstrkgliEVKTDEFPRHgSNIEAMSKLKPYFltDG 242
Cdd:PRK06366 164 SAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIRK-TTMEDLAKLPPAF--DK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 243 TGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINE 322
Cdd:PRK06366 233 NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539872 323 AFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMG 389
Cdd:PRK06366 313 AFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGA 379
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
22-396 |
5.63e-95 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 289.86 E-value: 5.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 22 NGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVC 100
Cdd:PRK08242 20 DGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPGVQINRFCASGLEAVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 101 LAVQSIGIGDSSIVVAGGMENMSKAPhlaylrTGVKIGEMPLTDSIlcdgltdAFHNCHM--GITAENVAKKWQVSREDQ 178
Cdd:PRK08242 100 LAAAKVRSGWDDLVIAGGVESMSRVP------MGSDGGAWAMDPST-------NFPTYFVpqGISADLIATKYGFSREDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 179 DKVAVLSQNRTENAQKAGHFDKEIVPVlvSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLT-------DGTGTV----- 246
Cdd:PRK08242 167 DAYAVESQQRAAAAWAEGYFAKSVVPV--KDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMmgemggfDAVALQkypev 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 247 -------TPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFE 319
Cdd:PRK08242 245 erinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDLFE 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539872 320 INEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PRK08242 325 LNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIER 401
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
11-395 |
9.42e-94 |
|
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: 286.70 E-value: 9.42e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 11 VSAARTIIGSF---NGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWS 87
Cdd:cd00826 1 AGAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 88 CQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSkaphlaylrtgvkigempltdsilcdgltdafhnchmgITAENV 167
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME--------------------------------------TSAENN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 168 AKKWQV--------SREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGS--NIEAMSKLKPY 237
Cdd:cd00826 123 AKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGDeaSLDEIAKLRPA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 238 FltDGTGTVTPANASGINDGAAAVVLMKKSEADK-------RGLTPLARIVSWSQVGVEPS----IMGIGPIPAIKQAVT 306
Cdd:cd00826 203 F--DKEDFLTAGNACGLNDGAAAAILMSEAEAQKhglqskaREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 307 KAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEK------------------VNIEGGAIALGHPLGASGCRILVTLLH 368
Cdd:cd00826 281 KAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCF 360
|
410 420 430
....*....|....*....|....*....|..
gi 148539872 369 TL-----ERMGRSRGVAALCIGGGMGIAMCVQ 395
Cdd:cd00826 361 ELkgeagKRQGAGAGLALLCIGGGGGAAMCIE 392
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
5-397 |
2.41e-91 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 281.52 E-value: 2.41e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 5 SDPVVIVSAARTI-------IGSFNGAlaavpvqDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGA 77
Cdd:PRK08170 2 ARPVYIVDGARTPflkarggPGPFSAS-------DLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 78 GIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHL---AYLR----------TGVKIGEMP--- 141
Cdd:PRK08170 75 GCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLfseKMVRwlagwyaaksIGQKLAALGklr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 142 ---LTDSI-LCDGLTDAFHNCHMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFdKEIVPVLvsTRKGLIEVK 217
Cdd:PRK08170 155 psyLAPVIgLLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPLF--DRDGKFYDH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 218 TDEFpRHGSNIEAMSKLKPYFlTDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGP 297
Cdd:PRK08170 232 DDGV-RPDSSMEKLAKLKPFF-DRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 298 IPAIKQAVTKAGWSLEDVDIFEINEAFAA-VSAAIV---------KELGL-------NPEKVNIEGGAIALGHPLGASGC 360
Cdd:PRK08170 310 VHAATPLLQRHGLTLEDLDLWEINEAFAAqVLACLAawadeeycrEQLGLdgalgelDRERLNVDGGAIALGHPVGASGA 389
|
410 420 430
....*....|....*....|....*....|....*..
gi 148539872 361 RILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE 397
Cdd:PRK08170 390 RIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
9-396 |
3.89e-85 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 264.28 E-value: 3.89e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 9 VIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWS 87
Cdd:PRK07850 5 VIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHVGATT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 88 CQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPhlayLRTGVKIGE-MPLTDSILCDgLTDAFHnchmgiTAEN 166
Cdd:PRK07850 85 IDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP----LGANAGPGRgLPRPDSWDID-MPNQFE------AAER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 167 VAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRK-------GLIEVKTDEFPRHgSNIEAMSKLKPyfL 239
Cdd:PRK07850 154 IAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDeegqptgETRLVTRDQGLRD-TTMEGLAGLKP--V 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 240 TDGtGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFE 319
Cdd:PRK07850 231 LEG-GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539872 320 INEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PRK07850 310 INEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
10-396 |
3.82e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 261.59 E-value: 3.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 10 IVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWSC 88
Cdd:PRK06504 6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESVPGTSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 89 QMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGemplTDSILCDGLTDAFHNCH----MGitA 164
Cdd:PRK06504 86 DRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNG----LGHYKSPGMEERYPGIQfsqfTG--A 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 165 ENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKT-DEFPRHGSNIEAMSKLKPyfLTDGt 243
Cdd:PRK06504 160 EMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTvDEGIRFDATLEGIAGVKL--IAEG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 244 GTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEA 323
Cdd:PRK06504 237 GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEA 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539872 324 FAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PRK06504 317 FASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
8-396 |
4.24e-84 |
|
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: 261.42 E-value: 4.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIG-SFNGALAAVPVQDLGSTVIKEVLKR-ATVAPEDVSEVIFGHVLAA-GCGQNPVRQASVGAGIPYSVP 84
Cdd:TIGR02445 2 VVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVQQTlEQGFNIARNAALLAQIPHTSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 85 AWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPhlayLRTGVKIGEMPLTDSILCDGLtdafhnchMGITA 164
Cdd:TIGR02445 82 AVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP----MMHGVDFHPGMSLHVAKAAGM--------MGLTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 165 ENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFLTDGt 243
Cdd:TIGR02445 150 EMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGfLKQFDYDEVIRPETTVESLAALRPAFDPKN- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 244 GTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEA 323
Cdd:TIGR02445 229 GTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539872 324 FAAVSAAIVKELGL---NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:TIGR02445 309 FAAQALPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
9-392 |
3.62e-81 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 253.15 E-value: 3.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 9 VIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRAtvaPEDVSEVIFGHVLaaGCGQNPVRQASVGAGIPYSVPAWSC 88
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFLSKGM---EREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 89 QMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLR-TGVKIGEmPltdsilcdgltdafhncHMGITAENV 167
Cdd:PRK06690 79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARfSPETIGD-P-----------------DMGVAAEYV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 168 AKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVlvstrKGLIevktDEFPRHGSNIEAM-SKLKPYFLTDGTgtV 246
Cdd:PRK06690 141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF-----NGLL----DESIKKEMNYERIiKRTKPAFLHNGT--V 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 247 TPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAA 326
Cdd:PRK06690 210 TAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFAS 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539872 327 VSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAM 392
Cdd:PRK06690 290 KVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLAL 355
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
9-391 |
4.28e-79 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 248.92 E-value: 4.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 9 VIVSAARTIIG-SFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGC-GQNPVRQASVGAGIPYSVPAW 86
Cdd:PRK07108 5 VIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVTVPGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 87 SCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHlaylrtgvKIGEMPLTDSILCDGLTDAFHNchMGITAEN 166
Cdd:PRK07108 85 TVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQN--------EMNRHMLREGWLVEHKPEIYWS--MLQTAEN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 167 VAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLV------------STRKglIEVKTDEFPRHGSNIEAMSKL 234
Cdd:PRK07108 155 VAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVtagvadkatgrlFTKE--VTVSADEGIRPDTTLEGVSKI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 235 KPYFltdGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLED 314
Cdd:PRK07108 233 RSAL---PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDD 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539872 315 VDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIA 391
Cdd:PRK07108 310 IDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
10-396 |
6.93e-77 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 243.91 E-value: 6.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 10 IVSAARTI--IGSF-NGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGC-GQNPVRQASVGAGIPYSVPA 85
Cdd:PRK06025 6 IIDAVRTPrgIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYDIKASG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 86 WSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGeMPLTDSilCDGLTDAFH-NCHMGITA 164
Cdd:PRK06025 86 VTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGKP-PLGMGS--GNLRLRALHpQSHQGVCG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 165 ENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLvsTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLT---- 240
Cdd:PRK06025 163 DAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY--RDDGSVALDHEEFPRPQTTAEGLAALKPAFTAiady 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 241 --DGTGT--------VTP----------ANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPA 300
Cdd:PRK06025 241 plDDKGTtyrglinqKYPdleikhvhhaGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 301 IKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVA 380
Cdd:PRK06025 321 AKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGLV 400
|
410
....*....|....*.
gi 148539872 381 ALCIGGGMGIAMCVQR 396
Cdd:PRK06025 401 TMCAAGGMAPAIIIER 416
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
2-397 |
7.02e-70 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 226.02 E-value: 7.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 2 NAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPY 81
Cdd:PRK08963 1 TRQGDRIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 82 SVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAP------------HLAYLRT---------GVKIGE- 139
Cdd:PRK08963 81 HTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaralvDLNKARTlgqrlklfsRLRLRDl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 140 MPLTDSI--LCDGLTdafhnchMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEvk 217
Cdd:PRK08963 161 LPVPPAVaeYSTGLR-------MGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPLE-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 218 TDEFPRHGSNIEAMSKLKPYFLTDgTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEP-SIMGIG 296
Cdd:PRK08963 232 EDNNIRGDSTLEDYAKLRPAFDRK-HGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 297 PIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVK----------ELGLN-------PEKVNIEGGAIALGHPLGASG 359
Cdd:PRK08963 311 PAYATPLALERAGLTLADLTLIDMHEAFAAQTLANLQmfaserfareKLGRSqaigevdMSKFNVLGGSIAYGHPFAATG 390
|
410 420 430
....*....|....*....|....*....|....*...
gi 148539872 360 CRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE 397
Cdd:PRK08963 391 ARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLEVE 428
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
274-396 |
9.10e-62 |
|
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: 194.78 E-value: 9.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 274 LTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGH 353
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 148539872 354 PLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-396 |
2.72e-53 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 182.79 E-value: 2.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 1 MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIP 80
Cdd:PRK09268 2 TMPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 81 YSVPAWSCQMICGSGLKAVCLAVQSIGIG--DSSIvvAGGMENMSKAP-------------------------HLAYLRT 133
Cdd:PRK09268 82 PYTPAYDLQQACGTGLEAAILVANKIALGqiDSGI--AGGVDTTSDAPiavneglrkillelnrakttgdrlkALGKLRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 134 GVKIGEMPLTDSILCdGLTdafhnchMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRkgl 213
Cdd:PRK09268 160 KHLAPEIPRNGEPRT-GLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 214 ievktDEFPRHGSNIEAMSKLKPYFLTDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVsWSQV------- 286
Cdd:PRK09268 229 -----DNNLRPDSSLEKLAKLKPVFGKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLV-DAETaavdfvh 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 287 GVEPSIMGigPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVK----------ELGLN-------PEKVNIEGGAI 349
Cdd:PRK09268 303 GKEGLLMA--PAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKawedeeycreRLGLDaplgsidRSKLNVNGSSL 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 148539872 350 ALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 396
Cdd:PRK09268 381 AAGHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
26-394 |
4.42e-24 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 99.83 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 26 AAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPySVPAWSCQMICGSGLKAVCLAVQS 105
Cdd:cd00327 3 LGITASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 106 IGIGDSSIVVAGGMEnmskaphlaylrtgvkigempltdsilcdgltdafhnchmgitaenvakkwqvsredqdkvavls 185
Cdd:cd00327 82 VQNGKADIVLAGGSE----------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 186 qnrtenaqkaghfdkeivpvlvstrkglievktdefprhgsnieamsklkpyfltdgtgtvtpanASGINDGAAAVVLMK 265
Cdd:cd00327 97 -----------------------------------------------------------------EFVFGDGAAAAVVES 111
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 266 KSEADKRGLTPLARIVSWSQVGVEPS----IMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEK 341
Cdd:cd00327 112 EEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDG 191
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539872 342 V---NIEGGAIALGHPLGASGCRILVTLLHTLERMGRSR-------GVAALCIGGGMGIAMCV 394
Cdd:cd00327 192 VrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtpreprtVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
28-389 |
1.32e-13 |
|
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: 71.53 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 28 VPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYsVPAWSCQMICGSGLKAVCLAVQSIG 107
Cdd:cd00829 14 RSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 108 IGDSSIVVAGGMENMSKAPhlaylrTGVKIGEMPLTDSILCDGLTDAFHNCHM-GITAENVAKKWQVSREDQDKVAVlsQ 186
Cdd:cd00829 93 SGLADVVLVVGAEKMSDVP------TGDEAGGRASDLEWEGPEPPGGLTPPALyALAARRYMHRYGTTREDLAKVAV--K 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 187 NRtENAQK---AgHFDKEIVP--VLVStrkglievktdefPRHGSnieamsklkPYFLTDgtgtvtpanASGINDGAAAV 261
Cdd:cd00829 165 NH-RNAARnpyA-QFRKPITVedVLNS-------------RMIAD---------PLRLLD---------CCPVSDGAAAV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 262 VLMKKSEADKRGLTPlARIVSWSQVGVEPSIMGIGPI-------PAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKE 334
Cdd:cd00829 212 VLASEERARELTDRP-VWILGVGAASDTPSLSERDDFlsldaarLAARRAYKMAGITPDDIDVAELYDCFTIAELLALED 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539872 335 LGLNPE------------------KVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVA----ALCIGGGMG 389
Cdd:cd00829 291 LGFCEKgeggklvregdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPgarvGLAHNIGGT 367
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
252-364 |
2.71e-09 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 58.55 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 252 SGINDGAAAVVLMKKSEA-DKRGLTPLARIVSWSQ----VGVEPSIMGIGPIP--------AIKQAVTKAGWSLEDVDIF 318
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLrDYADARPIPRIKGWGHrtapLGLEQKLDRSAGDPyvlphvrqAVLDAYRRAGVGLDDLDGF 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148539872 319 EINEAFAAVSAAIVKELGLNPE------------------KVNIEGGAIALGHPLGASGCRILV 364
Cdd:PRK06289 300 EVHDCFTPSEYLAIDHIGLTGPgeswkaiengeiaiggrlPINPSGGLIGGGHPVGASGVRMLL 363
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
8-391 |
5.45e-09 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 57.60 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSFNGalaaVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCgqnpVRQASVGAGIP-YS---- 82
Cdd:PRK06064 4 VAIIGVGQTKFGELWD----VSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLF----VSQEHIAALIAdYAglap 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 83 VPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGempltdsilcdgltDAFHNCHMGI 162
Cdd:PRK06064 76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAG--------------DYEWEEFFGA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 163 T--------AENVAKKWQVSREDQDKVAVlsqNRTENAQK--AGHFDKEIV--PVLVSTRKGlievktdefprhgsniea 230
Cdd:PRK06064 142 TfpglyaliARRYMHKYGTTEEDLALVAV---KNHYNGSKnpYAQFQKEITveQVLNSPPVA------------------ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 231 msklKPYFLTDgtgtvtpanASGINDGAAAVVLMKKSEADKRGLTPLaRIVSWSQ------VGVEPSIMGIGP-IPAIKQ 303
Cdd:PRK06064 201 ----DPLKLLD---------CSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQasdtiaLHDRKDFTTLDAaVVAAEK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 304 AVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLnPEK-------------------VNIEGGAIALGHPLGASGCRILV 364
Cdd:PRK06064 267 AYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGF-AKKgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQAV 345
|
410 420
....*....|....*....|....*..
gi 148539872 365 TLlhTLERMGRSRGVAALCIGGGMGIA 391
Cdd:PRK06064 346 EI--VWQLRGEAEKGRQQVIGAGYGLT 370
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
28-359 |
2.82e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 52.16 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 28 VPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAwSCQMICGSGLKAVCLAVQSIG 107
Cdd:PRK12578 19 VSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPL-RVEAMCATGLAASLTAYTAVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 108 IGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLtdsilcdgltdAFHN------CHMGITAENVAKKWQVSREDQDKV 181
Cdd:PRK12578 98 SGLVDMAIAVGVDKMTEVDTSTSLAIGGRGGNYQW-----------EYHFygttfpTYYALYATRHMAVYGTTEEQMALV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 182 AVLSQNRTENAQKAgHFDKEIvpvlvsTRKGLIEVKTDEFPrhgsnieamskLKPYfltdgtgtvtpaNASGINDGAAAV 261
Cdd:PRK12578 167 SVKAHKYGAMNPKA-HFQKPV------TVEEVLKSRAISWP-----------IKLL------------DSCPISDGSATA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 262 VLMKKSEADKRGL-TP--------------LARIVSWsqVGVEPSIMgigpipAIKQAVTKAGWSLEDVDIFEINEAFAA 326
Cdd:PRK12578 217 IFASEEKVKELKIdSPvwitgigyandyayVARRGEW--VGFKATQL------AARQAYNMAKVTPNDIEVATVHDAFTI 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 148539872 327 VSAAIVKELGL-------------NPEK-----VNIEGGAIALGHPLGASG 359
Cdd:PRK12578 289 AEIMGYEDLGFtekgkggkfieegQSEKggkvgVNLFGGLKAKGHPLGATG 339
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
249-359 |
3.12e-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: 48.69 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 249 ANASGIN--DGAAAVVLMKKSEADKRGLTPLARIVSWSQVG-----VEPSIMGIGPIPAIKQAVTKAGWSLEDVDIfeIN 321
Cdd:cd00834 222 KDRDGFVlgEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDY--IN 299
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148539872 322 ------------EafaavSAAIVKELGLNPEKVnieggAI-----ALGHPLGASG 359
Cdd:cd00834 300 ahgtstplndaaE-----SKAIKRVFGEHAKKV-----PVsstksMTGHLLGAAG 344
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
257-316 |
7.17e-06 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 47.72 E-value: 7.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539872 257 GAAAVVLMKKSEADKRGLTPLARIVSWSQV-----GVEPSImgIGPIPAIKQAVTKAGWSLEDVD 316
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMRldanrGPDPSL--EGEMRVIRAALRRAGLGPEDID 302
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
256-359 |
3.14e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 45.81 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 256 DGAAAVVLMKKSEADKRGLTPLARIVSWSQV-----GVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIF-------EINEA 323
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFGLTcdayhMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQ 289
|
90 100 110
....*....|....*....|....*....|....*.
gi 148539872 324 FaavSAAIVKELglNPEKVNIEGGAIALGHPLGASG 359
Cdd:PRK05952 290 R---EANLIQAL--FPHRVAVSSTKGATGHTLGASG 320
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
72-361 |
3.61e-05 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 45.65 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 72 QASVGAGIPYSvPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAP------HLA----YLRTGVkigemp 141
Cdd:PTZ00455 101 QSGASNALLYK-PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSarvggdYLAraadYRRQRK------ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 142 ltdsilcdgLTDAFHNCHMGITAENVAKKWQVSREDQDKVAVLS-QNRTENAQKAGHfdkeivpvlvsTRKGLIEVKTDE 220
Cdd:PTZ00455 174 ---------LDDFTFPCLFAKRMKYIQEHGHFTMEDTARVAAKAyANGNKNPLAHMH-----------TRKLSLEFCTGA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 221 FPRHgSNIEAMSKLKPYFLTdgtgtvtpANASGINDGAAAVVLMKKSEADKRGLTPL-ARIVSWSQVGVEPSIMGIGP-- 297
Cdd:PTZ00455 234 SDKN-PKFLGNETYKPFLRM--------TDCSQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEIKSLACASGNLYEDPpd 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 298 -------IPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPE------------------KVNIEGGAIALG 352
Cdd:PTZ00455 305 atrmftsRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYghakdlirngatalegriPVNTGGGLLSFG 384
|
....*....
gi 148539872 353 HPLGASGCR 361
Cdd:PTZ00455 385 HPVGATGVK 393
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
8-359 |
9.90e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 44.17 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 8 VVIVSAARTIIGSfngaLAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHvLAAGCGQNPVRQASVGAGIP--YSVPA 85
Cdd:PRK07516 4 ASIVGWAHTPFGK----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLGH-FNAGFSPQDFPASLVLQADPalRFKPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 86 WSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPhlaylrtGVKIGEMPLTDSILcdgltdafhnchmgitae 165
Cdd:PRK07516 79 TRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP-------TAEVGDILLGASYL------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 166 nvakkwqvsREDQDKVAVLsqnrtenaqkAGHFDKeivpvlvstrkglieVKTDEFPRHGSNIEAMSKL----------K 235
Cdd:PRK07516 134 ---------KEEGDTPGGF----------AGVFGR---------------IAQAYFQRYGDQSDALAMIaaknhangvaN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 236 PY------FLTDGTGTVTPAN-----------ASGINDGAAAVVLMkkSEADKRGLTPLARIVSWSQVGvepSIMGI--- 295
Cdd:PRK07516 180 PYaqmrkdLGFEFCRTVSEKNplvagplrrtdCSLVSDGAAALVLA--DAETARALQRAVRFRARAHVN---DFLPLsrr 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 296 ------GPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPE------------------KVNIEGGAIAL 351
Cdd:PRK07516 255 dplafeGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAK 334
|
....*...
gi 148539872 352 GHPLGASG 359
Cdd:PRK07516 335 GHPIGATG 342
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
256-359 |
2.52e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 42.96 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 256 DGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIP----------AIKQAVTKAGWSLEDVDIFEINEAFA 325
Cdd:PRK08256 215 CGAAAAIVCSEEFARKHGLDRAVEIVAQAMTTDTPSTFDGRSMIdlvgydmtraAAQQVYEQAGIGPEDIDVVELHDCFS 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 148539872 326 AVSAAIVKELGLNPEK------------------VNIEGGAIALGHPLGASG 359
Cdd:PRK08256 295 ANELLTYEALGLCPEGeaekfiddgdntyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
256-359 |
2.55e-04 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 42.85 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 256 DGAAAVVLMKKSEADKRGLTPLARIVSWSQVG-----VEPSIMGIGPIPAIKQAVTKAGWSLEDVD----------IFEI 320
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDyinahgtstpAGDK 311
|
90 100 110
....*....|....*....|....*....|....*....
gi 148539872 321 NEAfaavsAAIVKELGLNPEKVNIEGGAIALGHPLGASG 359
Cdd:PRK07314 312 AET-----QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAG 345
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
249-359 |
4.24e-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: 42.00 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 249 ANASGIN--DGAAAVVLMKKSEADKRGLTPLARIVSWS-------QVGVEPSimGIGPIPAIKQAVTKAGWSLEDVDIfe 319
Cdd:COG0304 222 KDRDGFVlgEGAGVLVLEELEHAKARGAKIYAEVVGYGassdayhITAPAPD--GEGAARAMRAALKDAGLSPEDIDY-- 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 148539872 320 IN------------EAfaavsAAIVKELGLNPEKVNIegGAI--ALGHPLGASG 359
Cdd:COG0304 298 INahgtstplgdaaET-----KAIKRVFGDHAYKVPV--SSTksMTGHLLGAAG 344
|
|
| ASKHA_NBD_HSP70_DDRA |
cd24030 |
nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) ... |
295-346 |
5.05e-04 |
|
nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) and similar proteins; DDRA, also called DDR large subunit, diol dehydratase-reactivase large subunit, diol dehydratase-reactivating factor alpha subunit, or DDR alpha subunit, is the large subunit of the diol dehydratase-reactivating factor (DDR), which reactivates suicidally inhibited adenosylcobalamin-dependent diol dehydratase (DD, pddA, pddB, pddC). DDR acts as a chaperone, reactivating inactivated DD holoenzyme in the presence of ATP, Mg(2+) and free adenosylcobalamin (AdoCbl), by mediating the exchange of the tightly bound damaged cofactor AdoCbl for a free intact one. DDR has weak ATPase activity which is required for DD reactivation. DDRA contains the adenosine nucleotide binding site. DDRA has four domains, the ATPase domain, the swiveling domain, the linker domain, and the insert domain. The model corresponds to the ATPase domain. DDRA belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation.
Pssm-ID: 466880 Cd Length: 260 Bit Score: 41.43 E-value: 5.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 148539872 295 IGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLnpeKVNIEG 346
Cdd:cd24030 46 PGIIKALELALEKAGINLSDIDLIRLNEAMQQIARELEEELGI---PVEIGG 94
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
299-394 |
6.12e-03 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 38.17 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 299 PAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKV--NIEggaiALGHPLGASgcriLVTLLHTLERMGR- 375
Cdd:COG0332 228 EVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVvvNID----RYGNTSAAS----IPLALDEALREGRi 299
|
90 100
....*....|....*....|.
gi 148539872 376 SRG-VAALC-IGGGMGIAMCV 394
Cdd:COG0332 300 KPGdLVLLAgFGAGLTWGAAV 320
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
254-371 |
7.55e-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: 38.00 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539872 254 INDGAAAVVLMKKSEADKRGLTPLARIVSWSQV-----GVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVS 328
Cdd:cd00825 159 FGDGAGALVVEELEHALARGAHIYAEIVGTAATidgagMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIG 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 148539872 329 AAIVKELGLN---PEKVNIEGGAIALGHPLGASGCRILVTLLHTLE 371
Cdd:cd00825 239 DVKELKLLRSefgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
|
|
| |
