|
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: 615.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWS 87
Cdd:PRK05790 4 VVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPALT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 88 CQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPH-LTHLRTGVRVGEVPLADSILCDGLTDAFHNYHMGITAEN 166
Cdd:PRK05790 84 INKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHvLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 167 VAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKG-LTEVKIDEFPRHGSNLEAMGKLKPYFLTDGTgt 245
Cdd:PRK05790 164 LAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGdPVVVDTDEHPRPDTTAESLAKLRPAFDKDGT-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 246 VTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYA 325
Cdd:PRK05790 242 VTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110625948 326 ALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 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: 582.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 9 VIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWSC 88
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 89 QMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHLRTGVRVGEVPLADSILCDGLTDAFHNYHMGITAENVA 168
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 169 KKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGSNLEAMGKLKPYFltDGTGTVTT 248
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAF--KKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 249 ANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYAALS 328
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110625948 329 VAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 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: 561.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 6 DPVVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPA 85
Cdd:COG0183 2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 86 WSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPH-LTHLRTGVRvGEVPLADSILCDGLTDAFHNYHMGITA 164
Cdd:COG0183 82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMlLPKARWGYR-MNAKLVDPMINPGLTDPYTGLSMGETA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 165 ENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGSNLEAMGKLKPYFLTDGTg 244
Cdd:COG0183 161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 245 tVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAY 324
Cdd:COG0183 240 -VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110625948 325 AALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 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 |
2.33e-170 |
|
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: 481.34 E-value: 2.33e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 10 IVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWSCQ 89
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 90 MICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTH--LRTGVRVGEVPLADSILCDgLTDAFHNYHMGITAENV 167
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPrsLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 168 AKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGSNLEAMGKLKPYFltDGTGTVT 247
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF--DPDGTVT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 248 TANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYAAL 327
Cdd:TIGR01930 238 AGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQ 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110625948 328 SVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQ 395
Cdd:TIGR01930 318 VLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
8-396 |
7.90e-161 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 457.50 E-value: 7.90e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLtagcgqnPT--------RQASVGAGI 79
Cdd:PRK09051 5 VVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVI-------PTeprdmylsRVAAINAGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 80 PYSVPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHL-THLRTGVRVGEVPLADSILcDGLTDAFHNY 158
Cdd:PRK09051 78 PQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLlPAARWGARMGDAKLVDMMV-GALHDPFGTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 159 HMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGSNLEAMGKLKPYF 238
Cdd:PRK09051 157 HMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 239 LTDGtGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLF 318
Cdd:PRK09051 237 KKEN-GTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVI 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110625948 319 EINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:PRK09051 316 EANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
8-397 |
2.79e-156 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 445.87 E-value: 2.79e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWS 87
Cdd:PRK05656 4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAMT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 88 CQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPH-LTHLRTGVRVGEVPLADSILCDGLTDAFHNYHMGITAEN 166
Cdd:PRK05656 84 LNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYvLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 167 VAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEV-KIDEFPRHGSNLEAMGKLKPYFLTDGTgt 245
Cdd:PRK05656 164 LVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAfATDEQPRAGTTAESLAKLKPAFKKDGS-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 246 VTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYA 325
Cdd:PRK05656 242 VTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110625948 326 ALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQRG 397
Cdd:PRK05656 322 AQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIERD 393
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
7-395 |
6.07e-149 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 427.14 E-value: 6.07e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 7 PVVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAW 86
Cdd:PRK06633 4 PVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 87 SCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHLRTGVRVGEVPLADSILCDGLTDAFHNYHMGITAEN 166
Cdd:PRK06633 84 TINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 167 VAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGSNLEAMGKLKPYFltDGTGTV 246
Cdd:PRK06633 164 ISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAF--DKNGVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 247 TTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYAA 326
Cdd:PRK06633 242 TAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110625948 327 LSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQ 395
Cdd:PRK06633 322 QSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
9-395 |
2.89e-142 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 410.26 E-value: 2.89e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 9 VIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWSC 88
Cdd:PRK08235 5 VIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 89 QMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPH-LTHLRTGVRVGEVPLADSILCDGLTDAFHNYHMGITAENV 167
Cdd:PRK08235 85 NKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYiLPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVYGGEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 168 AKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTE-VKIDEFPRHGSNLEAMGKLKPYFltDGTGTV 246
Cdd:PRK08235 165 AKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIvVAKDEAPRKDTTIEKLAKLKPVF--DKTGTI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 247 TTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYAA 326
Cdd:PRK08235 243 TAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110625948 327 LSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQ 395
Cdd:PRK08235 323 VALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
8-396 |
2.88e-139 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 402.55 E-value: 2.88e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWS 87
Cdd:PLN02644 3 VCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 88 CQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPH-LTHLRTGVRVGEVPLADSILCDGLTDAFHNYHMGITAEN 166
Cdd:PLN02644 83 VNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKyLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 167 VAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGS-NLEAMGKLKPYFLTDGtGT 245
Cdd:PLN02644 163 CADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIVDKDEGLGKfDPAKLRKLRPSFKEDG-GS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 246 VTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYA 325
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110625948 326 ALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
8-396 |
1.91e-127 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 372.78 E-value: 1.91e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWS 87
Cdd:PRK06205 4 AVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPGMQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 88 CQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTH-LRTGVRVGEVPLADSiLCDGLTDAFHNYH-----MG 161
Cdd:PRK06205 84 LDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdMRWGVRGGGVQLHDR-LARGRETAGGRRFpvpggMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 162 ITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKG-LTEVKIDEFPRHGSNLEAMGKLKPYFL- 239
Cdd:PRK06205 163 ETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGdPTVVDRDEHPRADTTLESLAKLRPIMGk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 240 TDGTGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFE 319
Cdd:PRK06205 243 QDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLIE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 320 INEAYAALSVAIAKELGLNP---EKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:PRK06205 323 LNEAFAAQVLAVLKEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAVFER 402
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-395 |
3.71e-119 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 351.50 E-value: 3.71e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 1 MNTRSDPVVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIP 80
Cdd:PRK06954 2 TAVDQDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 81 YSVPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLT-HLRTGVRVGEVPLADSILCDGLTDAFHNYH 159
Cdd:PRK06954 82 LSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpKARGGMRMGHGQVLDHMFLDGLEDAYDKGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 160 -MGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHgSNLEAMGKLKPYF 238
Cdd:PRK06954 162 lMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 239 LTDGTgtVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLF 318
Cdd:PRK06954 241 SKTGT--VTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625948 319 EINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQ 395
Cdd:PRK06954 319 EINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
8-396 |
2.59e-115 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 341.93 E-value: 2.59e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQR-AKVAPEEVSEVIFGHVLTAG-CGQNPTRQASVGAGIPYSVPA 85
Cdd:PRK09050 4 AFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGeDNRNVARMSALLAGLPVSVPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 86 WSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLthlrtgvrvgeVPLADSilcdgltdAF---------- 155
Cdd:PRK09050 84 TTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFV-----------MGKADS--------AFsrqaeifdtt 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 156 -----------HNY---HMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKG-LTEVKIDE 220
Cdd:PRK09050 145 igwrfvnplmkAQYgvdSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGdPVVVDRDE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 221 FPRHGSNLEAMGKLKPYFLTDGTgtVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPA 300
Cdd:PRK09050 225 HPRPETTLEALAKLKPVFRPDGT--VTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 301 IKQAVAKAGWSLEDVDLFEINEAYAALSVAIAKELGL--NPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRG 378
Cdd:PRK09050 303 TRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYA 382
|
410
....*....|....*...
gi 110625948 379 VAALCIGGGMGVAMCVQR 396
Cdd:PRK09050 383 LCTMCIGVGQGIALAIER 400
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
8-266 |
6.63e-112 |
|
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: 328.11 E-value: 6.63e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWS 87
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 88 CQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHL--THLRTGVRVGEVPLADSILCDGLTDAFHNYHMGITAE 165
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYAlpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 166 NVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGSNLEAMGKLKPYFltDGTGT 245
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAF--DKEGT 238
|
250 260
....*....|....*....|.
gi 110625948 246 VTTANATGMNDGAAAVVLMKK 266
Cdd:pfam00108 239 VTAGNASPINDGAAAVLLMSE 259
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
9-391 |
1.66e-109 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 326.71 E-value: 1.66e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 9 VIVSAARTAIGSFN-GALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVL-TAGCGQNPTRQASVGAGIPYSVPAW 86
Cdd:PRK07661 5 VIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYTVPAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 87 SCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTH-LRTGVRvgevpladsilcdgLTDAFHNYHMGI--T 163
Cdd:PRK07661 85 TINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHvVRPNPR--------------LVEAAPEYYMGMghT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 164 AENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRK-----GLTEVKI----DEFPRHGSNLEAMGKL 234
Cdd:PRK07661 151 AEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgennKLQEETItfsqDEGVRADTTLEILGKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 235 KPYFLTDGTgtVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLED 314
Cdd:PRK07661 231 RPAFNVKGS--VTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625948 315 VDLFEINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVA 391
Cdd:PRK07661 309 IGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAA 385
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
1-397 |
7.85e-109 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 327.11 E-value: 7.85e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 1 MNTRSDPVVIVSAARTAI-GSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQ-NPTRQASVGAG 78
Cdd:PLN02287 41 TTAFGDDVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 79 IPYSVPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHLRTGVRVGEVPLADSILCDgltdafhny 158
Cdd:PLN02287 121 FPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP--------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 159 hMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPV---LVSSRKGLTE---VKIDEFPRHGSNLEAMG 232
Cdd:PLN02287 192 -MGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkIVDPKTGEEKpivISVDDGIRPNTTLADLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 233 KLKPYFLTDGTgtvTTA-NATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWS 311
Cdd:PLN02287 271 KLKPVFKKNGT---TTAgNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 312 LEDVDLFEINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVG-GTR-GVAALCIGGGMG 389
Cdd:PLN02287 348 LDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkDCRfGVVSMCIGTGMG 427
|
....*...
gi 110625948 390 VAMCVQRG 397
Cdd:PLN02287 428 AAAVFERG 435
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
8-396 |
2.03e-107 |
|
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: 321.73 E-value: 2.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQR-AKVAPEEVSEVIFGHVLTAG-CGQNPTRQASVGAGIPYSVPA 85
Cdd:TIGR02430 3 AYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGeDNRNVARMAALLAGLPVSVPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 86 WSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHLRTGVRVGEVPLADSILC-----DGLTDAFHNYHM 160
Cdd:TIGR02430 83 TTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIEDTTIGwrfinPLMKALYGVDSM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 161 GITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGL-TEVKIDEFPRHGSNLEAMGKLKPYFL 239
Cdd:TIGR02430 163 PETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEpTVVDQDEHPRPETTLEGLAKLKPVVR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 240 TDGTgtVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFE 319
Cdd:TIGR02430 243 PDGT--VTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110625948 320 INEAYAALSVAIAKELGL--NPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:TIGR02430 321 LNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-391 |
2.55e-102 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 308.47 E-value: 2.55e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 1 MNTRSDPVVIVSAARTAIG-SFNGALSTVPVHEMGTTVIKEVLQRAK-VAPEEVSEVIFGHVL-TAGCGQNPTRQASVGA 77
Cdd:PRK09052 1 MSKQLQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVPgLDPKLIEDAIVGCAMpEAEQGLNVARIGALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 78 GIPYSVPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLthlrtgvrvGEVPLADSILCDGLTDAFHN 157
Cdd:PRK09052 81 GLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMM---------GNKPSMSPAIFARDENVGIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 158 YHMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRK-GLT---------EVKIDEFPRHGSN 227
Cdd:PRK09052 152 YGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpDLAtgevdvktrTVDLDEGPRADTS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 228 LEAMGKLKPYFltDGTGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAK 307
Cdd:PRK09052 232 LEGLAKLKPVF--ANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 308 AGWSLEDVDLFEINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGG 387
Cdd:PRK09052 310 AGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTG 389
|
....
gi 110625948 388 MGVA 391
Cdd:PRK09052 390 MGAA 393
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
10-396 |
1.40e-99 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 301.70 E-value: 1.40e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 10 IVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAG-CGQNPTRQASVGAGIPYSVPAWSC 88
Cdd:PRK08131 6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGeDSRNVARNALLLAGLPVTVPGQTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 89 QMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHLRTGVRVGEVPLADSILCD-----GLTDAFHNYHMGIT 163
Cdd:PRK08131 86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTTIGArfpnpKIVAQYGNDSMPET 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 164 AENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTE--VKIDEFPRHGSNLEAMGKLKPYFltD 241
Cdd:PRK08131 166 GDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLPPklVAEDEHPRPSSTVEALTKLKPLF--E 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 242 GtGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEIN 321
Cdd:PRK08131 244 G-GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEIN 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625948 322 EAYAALSVAIAKELGL--NPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:PRK08131 323 EAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIER 399
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
8-396 |
2.55e-99 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 300.34 E-value: 2.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIG-SFNGALSTVPVHEMGTTVIKEVLQR-AKVAPEEVSEVIFGHVL-TAGCGQNPTRQASVGAGIPYSVP 84
Cdd:PRK08947 4 VVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQqTLEQGFNIARNAALLAGIPHSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 85 AWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPhLTHlrtGVRVGevPLAdsilcdGLTDAFHNYHMGITA 164
Cdd:PRK08947 84 AVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP-MNH---GVDFH--PGL------SKNVAKAAGMMGLTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 165 ENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKG-LTEVKIDEFPRHGSNLEAMGKLKPYFlTDGT 243
Cdd:PRK08947 152 EMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGvLKLFDYDEVIRPETTVEALAALRPAF-DPVN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 244 GTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEA 323
Cdd:PRK08947 231 GTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEA 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625948 324 YAALSVAIAKELGL---NPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:PRK08947 311 FAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFER 386
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
8-389 |
3.05e-99 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 300.39 E-value: 3.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWS 87
Cdd:PRK06366 4 VYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTKYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 88 CQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHL--THLRTGVR---VGEVPLADSILCDGLTDAFHNYHMGI 162
Cdd:PRK06366 84 VNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLlpSDLRWGPKhllHKNYKIDDAMLVDGLIDAFYFEHMGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 163 TAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVlvssrkglTEVKIDEFPRHgSNLEAMGKLKPYFltDG 242
Cdd:PRK06366 164 SAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPF--------NDLDRDEGIRK-TTMEDLAKLPPAF--DK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 243 TGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINE 322
Cdd:PRK06366 233 NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625948 323 AYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMG 389
Cdd:PRK06366 313 AFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGA 379
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
8-396 |
1.48e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 298.94 E-value: 1.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSFN------GALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLtaGCGQNPT---RQASVGAG 78
Cdd:PRK06445 4 VYLVDFARTAFSRFRpkdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENWLyggRHPIFLAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 79 IPYSVPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLT--HLRTGVRVgevpLADSILCDglTDAFH 156
Cdd:PRK06445 82 LPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDnpHIEPNPKL----LTDPKYIE--YDLTT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 157 NYHMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGSNLEAMGKLKP 236
Cdd:PRK06445 156 GYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 237 YFLTDGTgtVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVD 316
Cdd:PRK06445 236 AFKPDGV--ITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDID 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 317 LFEINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:PRK06445 314 LWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLER 393
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
9-396 |
3.11e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 298.46 E-value: 3.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 9 VIVSAARTAIG-SFNGALSTVPVHEMGTTVIKEVLqrAKV---APEEVSEVIFGHVLTAGC-GQNPTRQASVGAGIPySV 83
Cdd:PRK07851 5 VIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAAL--DKVpalDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYD-FL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 84 PAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLT---------------HLRTGVRV--GEVPLADSI 146
Cdd:PRK07851 82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNsdslpdtknplfaeaQARTAARAegGAEAWHDPR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 147 LCDGLTDAFhnYHMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVlvsSRKGLTEVKIDEFPRHGS 226
Cdd:PRK07851 162 EDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPV---TLPDGTVVSTDDGPRAGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 227 NLEAMGKLKPYFLTDGTgtVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVA 306
Cdd:PRK07851 237 TYEKVSQLKPVFRPDGT--VTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 307 KAGWSLEDVDLFEINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGG 386
Cdd:PRK07851 315 RAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGG 394
|
410
....*....|
gi 110625948 387 GMGVAMCVQR 396
Cdd:PRK07851 395 GQGMAMVLER 404
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
10-396 |
1.89e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 295.46 E-value: 1.89e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 10 IVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGcGQ--NPTRQASVGAGIPYSVPAWS 87
Cdd:PRK07801 6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQagNIARTSWLAAGLPEEVPGVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 88 CQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHLRTGVRVG-EVPLADSILC-----DGLTDAFHNyhmg 161
Cdd:PRK07801 85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGfTSPFAESKGWlhrygDQEVSQFRG---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 162 itAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVlvssrkglTEVKIDEFPRHgSNLEAMGKLKPyfLTD 241
Cdd:PRK07801 161 --AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV--------GGVTVDEGPRE-TSLEKMAGLKP--LVE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 242 GtGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEIN 321
Cdd:PRK07801 228 G-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEIN 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625948 322 EAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:PRK07801 307 EAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
11-395 |
2.20e-96 |
|
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: 293.25 E-value: 2.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 11 VSAARTAIGSFNG---ALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWS 87
Cdd:cd00826 1 AGAAMTAFGKFGGengADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 88 CQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSkaphlthlrtgvrvgevpladsilcdgltdafhnyhmgITAENV 167
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME--------------------------------------TSAENN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 168 AKKWQV--------SREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGS--NLEAMGKLKPY 237
Cdd:cd00826 123 AKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGDeaSLDEIAKLRPA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 238 FltDGTGTVTTANATGMNDGAAAVVLMKKTEAE-------RRMLKPLARIVSWSQAGVEPS----VMGVGPIPAIKQAVA 306
Cdd:cd00826 203 F--DKEDFLTAGNACGLNDGAAAAILMSEAEAQkhglqskAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 307 KAGWSLEDVDLFEINEAYAALSVAIAKELGLNPEK------------------VNINGGAIALGHPLGASGCRILVTLLH 368
Cdd:cd00826 281 KAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCF 360
|
410 420 430
....*....|....*....|....*....|..
gi 110625948 369 TLERVGGTR-----GVAALCIGGGMGVAMCVQ 395
Cdd:cd00826 361 ELKGEAGKRqgagaGLALLCIGGGGGAAMCIE 392
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
10-396 |
2.70e-93 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 285.62 E-value: 2.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 10 IVSAART--AIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAG-CGQNPTRQASVGAGIPYSVPAW 86
Cdd:PRK08242 6 IYDAVRTprGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 87 SCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPhlthlrTGVRVGEVPLADSIlcdgltdAFHNYHM--GITA 164
Cdd:PRK08242 86 QINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP------MGSDGGAWAMDPST-------NFPTYFVpqGISA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 165 ENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVlvSSRKGLTEVKIDEFPRHGSNLEAMGKLKPYFLT---- 240
Cdd:PRK08242 153 DLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV--KDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMmgem 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 241 ---DGTGT-----------VTTA-NATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAV 305
Cdd:PRK08242 231 ggfDAVALqkypeverinhVHHAgNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 306 AKAGWSLEDVDLFEINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIG 385
Cdd:PRK08242 311 AKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVG 390
|
410
....*....|.
gi 110625948 386 GGMGVAMCVQR 396
Cdd:PRK08242 391 GGMGIATIIER 401
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
5-397 |
6.05e-88 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 272.66 E-value: 6.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 5 SDPVVIVSAART-------AIGSFNGAlstvpvhEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGA 77
Cdd:PRK08170 2 ARPVYIVDGARTpflkargGPGPFSAS-------DLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 78 GIPYSVPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPhLTHLRTGVR-VGEVPLADSI---------- 146
Cdd:PRK08170 75 GCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAP-LLFSEKMVRwLAGWYAAKSIgqklaalgkl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 147 ----------LCDGLTDAFHNYHMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFdKEIVPVLvsSRKGlTEV 216
Cdd:PRK08170 154 rpsylapvigLLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPLF--DRDG-KFY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 217 KIDEFPRHGSNLEAMGKLKPYFlTDGTGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVG 296
Cdd:PRK08170 230 DHDDGVRPDSSMEKLAKLKPFF-DRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 297 PIPAIKQAVAKAGWSLEDVDLFEINEAYAALSVAI----------AKELGL-------NPEKVNINGGAIALGHPLGASG 359
Cdd:PRK08170 309 PVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLAClaawadeeycREQLGLdgalgelDRERLNVDGGAIALGHPVGASG 388
|
410 420 430
....*....|....*....|....*....|....*...
gi 110625948 360 CRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQRG 397
Cdd:PRK08170 389 ARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
8-396 |
2.03e-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: 262.19 E-value: 2.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIG-SFNGALSTVPVHEMGTTVIKEVLQR-AKVAPEEVSEVIFGHV-LTAGCGQNPTRQASVGAGIPYSVP 84
Cdd:TIGR02445 2 VVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVqQTLEQGFNIARNAALLAQIPHTSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 85 AWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPhLTHlrtGVRVGEVPLADSILCDGLtdafhnyhMGITA 164
Cdd:TIGR02445 82 AVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP-MMH---GVDFHPGMSLHVAKAAGM--------MGLTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 165 ENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKG-LTEVKIDEFPRHGSNLEAMGKLKPYFLTDGt 243
Cdd:TIGR02445 150 EMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGfLKQFDYDEVIRPETTVESLAALRPAFDPKN- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 244 GTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEA 323
Cdd:TIGR02445 229 GTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625948 324 YAALSVAIAKELGL---NPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:TIGR02445 309 FAAQALPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
10-396 |
2.26e-83 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 259.66 E-value: 2.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 10 IVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAG-CGQNPTRQASVGAGIPYSVPAWSC 88
Cdd:PRK06504 6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESVPGTSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 89 QMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLT----HLRTGVRVGEVPladsilcdGLTDAFHNYH----M 160
Cdd:PRK06504 86 DRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSpstlPAKNGLGHYKSP--------GMEERYPGIQfsqfT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 161 GitAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEV-KIDEFPRHGSNLEAMGKLKPyfL 239
Cdd:PRK06504 158 G--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMhTVDEGIRFDATLEGIAGVKL--I 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 240 TDGtGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFE 319
Cdd:PRK06504 234 AEG-GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625948 320 INEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:PRK06504 313 VNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
9-391 |
6.29e-83 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 258.55 E-value: 6.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 9 VIVSAARTAIG-SFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGC-GQNPTRQASVGAGIPYSVPAW 86
Cdd:PRK07108 5 VIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVTVPGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 87 SCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMS--KAPHLTHLrtgvrvgevpLADSILCDGLTDAFHNyhMGITA 164
Cdd:PRK07108 85 TVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIScvQNEMNRHM----------LREGWLVEHKPEIYWS--MLQTA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 165 ENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLV--------SSRKGLTEVKI--DEFPRHGSNLEAMGKL 234
Cdd:PRK07108 153 ENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVtagvadkaTGRLFTKEVTVsaDEGIRPDTTLEGVSKI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 235 KPYFltdGTGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLED 314
Cdd:PRK07108 233 RSAL---PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDD 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625948 315 VDLFEINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVA 391
Cdd:PRK07108 310 IDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
9-396 |
6.38e-83 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 258.50 E-value: 6.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 9 VIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAG-CGQNPTRQASVGAGIPYSVPAWS 87
Cdd:PRK07850 5 VIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHVGATT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 88 CQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPhlthLRTGVRVGE-VPLADSILCDgLTDAFHnyhmgiTAEN 166
Cdd:PRK07850 85 IDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP----LGANAGPGRgLPRPDSWDID-MPNQFE------AAER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 167 VAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPV----------------LVSSRKGLTEvkidefprhgSNLEA 230
Cdd:PRK07850 154 IAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVqapvldeegqptgetrLVTRDQGLRD----------TTMEG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 231 MGKLKPyfLTDGtGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGW 310
Cdd:PRK07850 224 LAGLKP--VLEG-GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGM 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 311 SLEDVDLFEINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGV 390
Cdd:PRK07850 301 KIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALST 380
|
....*.
gi 110625948 391 AMCVQR 396
Cdd:PRK07850 381 GTIIER 386
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
9-392 |
1.12e-77 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 244.29 E-value: 1.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 9 VIVSAARTAIGSFNGALSTVPVHEMGTTVIKevlQRAKVAPEEVSEVIFGHVLtaGCGQNPTRQASVGAGIPYSVPAWSC 88
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLT---FLSKGMEREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 89 QMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHLRTGvrvgevpladsilcdglTDAFHNYHMGITAENVA 168
Cdd:PRK06690 79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFS-----------------PETIGDPDMGVAAEYVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 169 KKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVlvssrKGLtevkIDEFPRHGSNLEAM-GKLKPYFLTDGTgtVT 247
Cdd:PRK06690 142 ERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF-----NGL----LDESIKKEMNYERIiKRTKPAFLHNGT--VT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 248 TANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYAAL 327
Cdd:PRK06690 211 AGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASK 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625948 328 SVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAM 392
Cdd:PRK06690 291 VVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLAL 355
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
10-396 |
6.80e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 241.22 E-value: 6.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 10 IVSAART--AIGSF-NGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGC-GQNPTRQASVGAGIPYSVPA 85
Cdd:PRK06025 6 IIDAVRTprGIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYDIKASG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 86 WSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHlRTGVRVGEVPLADSilCDGLTDAFH-NYHMGITA 164
Cdd:PRK06025 86 VTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAA-EDMAAGKPPLGMGS--GNLRLRALHpQSHQGVCG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 165 ENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLvsSRKGLTEVKIDEFPRHGSNLEAMGKLKPYFLT---- 240
Cdd:PRK06025 163 DAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY--RDDGSVALDHEEFPRPQTTAEGLAALKPAFTAiady 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 241 --DGTGTV------------------TTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPA 300
Cdd:PRK06025 241 plDDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 301 IKQAVAKAGWSLEDVDLFEINEAYAALSVAIAKELGLNPEKVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVA 380
Cdd:PRK06025 321 AKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGLV 400
|
410
....*....|....*.
gi 110625948 381 ALCIGGGMGVAMCVQR 396
Cdd:PRK06025 401 TMCAAGGMAPAIIIER 416
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
2-396 |
3.47e-72 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 232.18 E-value: 3.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 2 NTRSDPVVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPY 81
Cdd:PRK08963 1 TRQGDRIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 82 SVPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAP------------HLTHLRT---------GVRVGE- 139
Cdd:PRK08963 81 HTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaralvDLNKARTlgqrlklfsRLRLRDl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 140 --VPLADSILCDGLTdafhnyhMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSS-RKGLTEv 216
Cdd:PRK08963 161 lpVPPAVAEYSTGLR-------MGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPyKQPLEE- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 217 kiDEFPRHGSNLEAMGKLKPYFLTDgTGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEP-SVMGV 295
Cdd:PRK08963 233 --DNNIRGDSTLEDYAKLRPAFDRK-HGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 296 GPIPAIKQAVAKAGWSLEDVDLFEINEAYAALSVA---------IAKE-LGLN-------PEKVNINGGAIALGHPLGAS 358
Cdd:PRK08963 310 GPAYATPLALERAGLTLADLTLIDMHEAFAAQTLAnlqmfaserFAREkLGRSqaigevdMSKFNVLGGSIAYGHPFAAT 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 110625948 359 GCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:PRK08963 390 GARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
274-396 |
2.96e-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: 195.94 E-value: 2.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 274 LKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYAALSVAIAKELGLNPEKVNINGGAIALGH 353
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 110625948 354 PLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
7-396 |
4.39e-57 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 192.42 E-value: 4.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 7 PVVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAW 86
Cdd:PRK09268 8 RVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 87 SCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAP-------------------------HLTHLRTGVRVGEVP 141
Cdd:PRK09268 88 DLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPiavneglrkillelnrakttgdrlkALGKLRPKHLAPEIP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 142 lADSILCDGLTdafhnyhMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLvssrkGLTEvkiDEF 221
Cdd:PRK09268 168 -RNGEPRTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFL-----GLTR---DNN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 222 PRHGSNLEAMGKLKPYFLTDGTGTVTTANATGMNDGAAAVVLMKKTEAERRMLKPLARIVsWSQA-------GVEPSVMG 294
Cdd:PRK09268 232 LRPDSSLEKLAKLKPVFGKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLV-DAETaavdfvhGKEGLLMA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 295 vgPIPAIKQAVAKAGWSLEDVDLFEINEAYAALSVAIAK----------ELGLN-------PEKVNINGGAIALGHPLGA 357
Cdd:PRK09268 311 --PAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKawedeeycreRLGLDaplgsidRSKLNVNGSSLAAGHPFAA 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 110625948 358 SGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQR 396
Cdd:PRK09268 389 TGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
30-394 |
3.27e-25 |
|
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: 102.91 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 30 VHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPySVPAWSCQMICGSGLKAVCLAAQSIAMG 109
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 110 DSTIVVAGGMEnmskaphlthlrtgvrvgevpladsilcdgltdafhnyhmgitaenvakkwqvsreaqdkvavlsqnra 189
Cdd:cd00327 86 KADIVLAGGSE--------------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 190 ehaqkaghfdkeivpvlvssrkgltevkidefprhgsnleamgklkpyfltdgtgtvttanATGMNDGAAAVVLMKKTEA 269
Cdd:cd00327 97 -------------------------------------------------------------EFVFGDGAAAAVVESEEHA 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 270 ERRMLKPLARIVSWSQ----AGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYAALSVAIAKELGLNPEKV--- 342
Cdd:cd00327 116 LRRGAHPQAEIVSTAAtfdgASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrsp 195
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 110625948 343 NINGGAIALGHPLGASGCRILVTLLHTLE-------RVGGTRGVAALCIGGGMGVAMCV 394
Cdd:cd00327 196 AVSATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
23-394 |
7.98e-20 |
|
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: 90.02 E-value: 7.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 23 GALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYsVPAWSCQMICGSGLKAVCLA 102
Cdd:cd00829 9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 103 AQSIAMGDSTIVVAGGMENMSKAPHLTHLRTgvRVGEVPLADSILCDGLTdaFHNYHmGITAENVAKKWQVSREAQDKVA 182
Cdd:cd00829 88 AAAIASGLADVVLVVGAEKMSDVPTGDEAGG--RASDLEWEGPEPPGGLT--PPALY-ALAARRYMHRYGTTREDLAKVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 183 VLSQNRAEHAQKAgHFDKEIVpvlvssrkgLTEVKidefprhGSNLEAmgklKPYFLTDgtgtvttanATGMNDGAAAVV 262
Cdd:cd00829 163 VKNHRNAARNPYA-QFRKPIT---------VEDVL-------NSRMIA----DPLRLLD---------CCPVSDGAAAVV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 263 LMKkTEAERRMLKPLARIVSWSQAGVEPSVMGVGPI-------PAIKQAVAKAGWSLEDVDLFEINEAYAALSVAIAKEL 335
Cdd:cd00829 213 LAS-EERARELTDRPVWILGVGAASDTPSLSERDDFlsldaarLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 336 GLNPE------------------KVNINGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVA----ALCIG-GGMGVAM 392
Cdd:cd00829 292 GFCEKgeggklvregdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPgarvGLAHNiGGTGSAA 371
|
..
gi 110625948 393 CV 394
Cdd:cd00829 372 VV 373
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
254-386 |
1.18e-09 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 59.70 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 254 MNDGAAAVVLMKKTEAER-RMLKPLARIVSWS--------QAGVEPSVMGVGPIPAIKQAV----AKAGWSLEDVDLFEI 320
Cdd:PRK06289 222 VTDGGAGVVLASDAYLRDyADARPIPRIKGWGhrtaplglEQKLDRSAGDPYVLPHVRQAVldayRRAGVGLDDLDGFEV 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 321 NEA-----YAALS------------------VAIAKELGLNPekvniNGGAIALGHPLGASGCRILVTLLHTLE------ 371
Cdd:PRK06289 302 HDCftpseYLAIDhigltgpgeswkaiengeIAIGGRLPINP-----SGGLIGGGHPVGASGVRMLLDAAKQVTgtagdy 376
|
170
....*....|....*
gi 110625948 372 RVGGTRGVAALCIGG 386
Cdd:PRK06289 377 QVEGAKTFGTLNIGG 391
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
254-359 |
1.05e-08 |
|
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: 56.78 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 254 MNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAG-----VEPSVMGVGPIPAIKQAVAKAGWSLEDVDLfeINeAYA--- 325
Cdd:cd00834 229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDY--IN-AHGtst 305
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 110625948 326 -----ALSVAIAKELGLNPEKVNING--GAIalGHPLGASG 359
Cdd:cd00834 306 plndaAESKAIKRVFGEHAKKVPVSStkSMT--GHLLGAAG 344
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
83-391 |
3.46e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 51.82 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 83 VPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHLRTGVRVGevpladsilcdgltDAFHNYHMGI 162
Cdd:PRK06064 76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAG--------------DYEWEEFFGA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 163 T--------AENVAKKWQVSREAQDKVAVLSQNRAEHAQKAgHFDKEIvpvlvssrkgltevKIDEFprhgsnLEAMGKL 234
Cdd:PRK06064 142 TfpglyaliARRYMHKYGTTEEDLALVAVKNHYNGSKNPYA-QFQKEI--------------TVEQV------LNSPPVA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 235 KPYFLTDgtgtvttanATGMNDGAAAVVLMKKTEAERRMLKPLaRIVSWSQA-------------GVEPSVMgvgpipAI 301
Cdd:PRK06064 201 DPLKLLD---------CSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQAsdtialhdrkdftTLDAAVV------AA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 302 KQAVAKAGWSLEDVDLFEINEAYAALSVAIAKELGLnPEK-------------------VNINGGAIALGHPLGASGCRI 362
Cdd:PRK06064 265 EKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGF-AKKgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQ 343
|
330 340 350
....*....|....*....|....*....|.
gi 110625948 363 LVTLLHTL--ERVGGTRGVaalcIGGGMGVA 391
Cdd:PRK06064 344 AVEIVWQLrgEAEKGRQQV----IGAGYGLT 370
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
9-117 |
7.52e-06 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 47.43 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 9 VIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHvlTAGCGQNPTRQASVGA--GIPySVPAW 86
Cdd:cd00827 27 VDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVAT--ESPIDKGKSAATYLAEllGLT-NAEAF 103
|
90 100 110
....*....|....*....|....*....|...
gi 110625948 87 SCQMICGSGLKAVCLAAQSIAMGDST--IVVAG 117
Cdd:cd00827 104 DLKQACYGGTAALQLAANLVESGPWRyaLVVAS 136
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
257-367 |
2.60e-05 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 46.18 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 257 GAAAVVLMKKTEAERRMLKPLARIVSWSQA-----GVEPSVmgVGPIPAIKQAVAKAGWSLEDVDLfeINeAYAALSVA- 330
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMRldanrGPDPSL--EGEMRVIRAALRRAGLGPEDIDY--VN-PHGTGSPLg 314
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 110625948 331 ----IAKELGLNPEKVNINGGAIALGHPLGASGC-RILVTLL 367
Cdd:PRK07103 315 deteLAALFASGLAHAWINATKSLTGHGLSAAGIvELIATLL 356
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
256-359 |
2.75e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 45.81 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 256 DGAAAVVLMKKTEAERRMLKPLARIVSWSQA-----GVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLF-------EINEA 323
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFGLTcdayhMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQ 289
|
90 100 110
....*....|....*....|....*....|....*.
gi 110625948 324 YAALSVAiakelGLNPEKVNINGGAIALGHPLGASG 359
Cdd:PRK05952 290 REANLIQ-----ALFPHRVAVSSTKGATGHTLGASG 320
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
249-359 |
1.02e-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: 43.93 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 249 ANATGMN--DGAAAVVLMKKTEAERRMLKPLARIVSWSQAG-----VEPSVMGVGPIPAIKQAVAKAGWSLEDVDLfeIN 321
Cdd:COG0304 222 KDRDGFVlgEGAGVLVLEELEHAKARGAKIYAEVVGYGASSdayhiTAPAPDGEGAARAMRAALKDAGLSPEDIDY--IN 299
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 110625948 322 ------------EAyaalsVAIAKELGLNPEKVNINggAI--ALGHPLGASG 359
Cdd:COG0304 300 ahgtstplgdaaET-----KAIKRVFGDHAYKVPVS--STksMTGHLLGAAG 344
|
|
| ASKHA_NBD_HSP70_DDRA |
cd24030 |
nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) ... |
295-346 |
2.73e-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: 42.20 E-value: 2.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 110625948 295 VGPIPAIKQAVAKAGWSLEDVDLFEINEAYAALSVAIAKELGLnpeKVNING 346
Cdd:cd24030 46 PGIIKALELALEKAGINLSDIDLIRLNEAMQQIARELEEELGI---PVEIGG 94
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
40-375 |
3.17e-04 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 42.71 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 40 EVLQRAKVAPEEVSEVIFGHVLTAgcgqnptrQASVGAGIPYS-------VPAWSCQMICGSGLKAVCLAAQSIAMGDST 112
Cdd:PRK06157 37 EALADAGIEPKDIDAAWFGTHYDE--------IGSGKSGTPLSralrlpnIPVTRVENFCATGSEAFRGAVYAVASGAYD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 113 IVVAGGMENMSKAPHlthlrTGVRVGEVPLADSILCDGLTdAFHNYHMGITAenVAKKWQVSRE----AQDKVAVLSQNR 188
Cdd:PRK06157 109 IALALGVEKLKDTGY-----GGLPVANPGTLADMTMPNVT-APGNFAQLASA--YAAKYGVSREdlkrAMAHVSVKSHAN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 189 AEHAQKAgHFdkeivpvlvssRKGLTEVKIDEFPRHGSNLEAMgklkpyfltdgtgtvttaNATGMNDGAAAVVLMKKTE 268
Cdd:PRK06157 181 GARNPKA-HL-----------RKAVTEEQVLKAPMIAGPLGLF------------------DCCGVSDGAAAAIVTTPEI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 269 AeRRMLKPLARIVSWSQAGVEP--SVMGVG--------PIPAIKQAVAKAGWS--LEDVDLFEINEAYAALSVAIAKELG 336
Cdd:PRK06157 231 A-RALGKKDPVYVKALQLAVSNgwELQYNGwdgsyfptTRIAARKAYREAGITdpREELSMAEVHDCFSITELVTMEDLG 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 110625948 337 LNPE------------------KVNINGGAIALGHPLGASGCRILVTL-LHTLERVGG 375
Cdd:PRK06157 310 LSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRMLYEMyLQLLGRAGE 367
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
299-345 |
3.40e-04 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 42.40 E-value: 3.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 110625948 299 PAIKQAVAKAGWSLEDVDLFEINEAYAALSVAIAKELGLNPEKVNIN 345
Cdd:COG0332 228 EVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVN 274
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
254-359 |
4.06e-04 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 42.08 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 254 MNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAG-----VEPSVMGVGPIPAIKQAVAKAGWSLEDVDLfeINeAYA--- 325
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDY--IN-AHGtst 306
|
90 100 110
....*....|....*....|....*....|....*....
gi 110625948 326 -----ALSVAIAKELGLNPEKVNINGGAIALGHPLGASG 359
Cdd:PRK07314 307 pagdkAETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAG 345
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
72-361 |
6.14e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 41.80 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 72 QASVGAGIPYSvPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAphlthlrtGVRVGEVPLADsilcdgl 151
Cdd:PTZ00455 101 QSGASNALLYK-PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTV--------SARVGGDYLAR------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 152 tdafhnyhmgitaenvAKKWQVSREAQD-KVAVLSQNRAEHAQKAGHFDKEIVPVLVS---------------SRKGLTE 215
Cdd:PTZ00455 165 ----------------AADYRRQRKLDDfTFPCLFAKRMKYIQEHGHFTMEDTARVAAkayangnknplahmhTRKLSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 216 VKIDEFPrhgSNLEAMGK--LKPYfltdgtgtVTTANATGMNDGAAAVVLMKKTEAERRMLKP----LARIVSWSQAG-- 287
Cdd:PTZ00455 229 FCTGASD---KNPKFLGNetYKPF--------LRMTDCSQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASgn 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 288 -----VEPSVMgVGPIPAIKQAVAKAGWSLEDV------DLFEINEA--YAALSVA---IAKELGLNPE-------KVNI 344
Cdd:PTZ00455 298 lyedpPDATRM-FTSRAAAQKALSMAGVKPSDLqvaevhDCFTIAELlmYEALGIAeygHAKDLIRNGAtalegriPVNT 376
|
330
....*....|....*..
gi 110625948 345 NGGAIALGHPLGASGCR 361
Cdd:PTZ00455 377 GGGLLSFGHPVGATGVK 393
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
254-372 |
6.63e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 41.43 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 254 MNDGAAAVVLMKKTEAERRMLKPLarIVSWSQAG---VEPSVMGVGPIP--------------------------AIKQA 304
Cdd:PRK06365 225 MSDGAACAILASEDKAFEITDKPV--LIKAIGTGsdtLRLADRPFGEVPllpnespddykdlrypgvhsfragrmAAKEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 305 VAKAGWS--LEDVDLFEINEAYAALSVAIAKELGLNPE------------------KVNINGGAIALGHPLGASGCR--- 361
Cdd:PRK06365 303 YEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLCKYgeggqfiesgkpelpgklPVNPSGGLLAAGHAVGATGIMqav 382
|
170
....*....|..
gi 110625948 362 -ILVTLLHTLER 372
Cdd:PRK06365 383 fMFWQLQGRIKK 394
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
8-359 |
7.71e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 41.47 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 8 VVIVSAARTAIGSfngaLSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHvLTAGCGQNPTRQASVGAGIP--YSVPA 85
Cdd:PRK07516 4 ASIVGWAHTPFGK----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLGH-FNAGFSPQDFPASLVLQADPalRFKPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 86 WSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPhlthlrtGVRVGEVPLADSILCD------GLTDAFhnyh 159
Cdd:PRK07516 79 TRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP-------TAEVGDILLGASYLKEegdtpgGFAGVF---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 160 mGITAENVAKKWQVSREAQDKVAVlsQNRAE-----HAQKaghfdkeivpvlvssRKGLTEvkidEFPRHGS--NLEAMG 232
Cdd:PRK07516 148 -GRIAQAYFQRYGDQSDALAMIAA--KNHANgvanpYAQM---------------RKDLGF----EFCRTVSekNPLVAG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 233 KLKpyfLTDgtgtvttanATGMNDGAAAVVLmkkteAERRMLKPLARIVSWSQAGVEPSVMGV---------GPIPAIKQ 303
Cdd:PRK07516 206 PLR---RTD---------CSLVSDGAAALVL-----ADAETARALQRAVRFRARAHVNDFLPLsrrdplafeGPRRAWQR 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110625948 304 AVAKAGWSLEDVDLFEINEAYAALSVAIAKELGLNPE------------------KVNINGGAIALGHPLGASG 359
Cdd:PRK07516 269 ALAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATG 342
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
256-374 |
1.31e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 40.44 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 256 DGAAAVVLMKKTEAERRMLKPlARIVSWSQAgVEPSVMGVGPI---PAIKQAVAKA-GWSLEDVDLFEINEAYAALSVAI 331
Cdd:PRK07937 206 DGAAAVVLAAGDRARELRERP-AWITGIEHR-IESPSLGARDLtrsPSTALAAEAAtGGDAGGVDVAELHAPFTHQELIL 283
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 110625948 332 AKELGLNPE-KVNINGGAIAlGHPLGASGcrilvtllhtLERVG 374
Cdd:PRK07937 284 REALGLGDKtKVNPSGGALA-ANPMFAAG----------LERIG 316
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
256-371 |
4.81e-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: 38.77 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 256 DGAAAVVLMKKTEAERRMLKPLARIVSWSQ-----AGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAYAALSVA 330
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAAtidgaGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDV 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 110625948 331 IAKELGLN---PEKVNINGGAIALGHPLGASGCRILVTLLHTLE 371
Cdd:cd00825 241 KELKLLRSefgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
306-345 |
6.46e-03 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 35.55 E-value: 6.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110625948 306 AKAGWSLEDVDLFEINEAYAALSVAIAKELGLNPEKVNIN 345
Cdd:pfam08541 2 EKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVN 41
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
256-359 |
6.70e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 38.34 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625948 256 DGAAAVVLMKKTEAERRMLKPLARIVSwsQAGV--------EPSVMGVGPIP----AIKQAVAKAGWSLEDVDLFEINEA 323
Cdd:PRK08256 215 CGAAAAIVCSEEFARKHGLDRAVEIVA--QAMTtdtpstfdGRSMIDLVGYDmtraAAQQVYEQAGIGPEDIDVVELHDC 292
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 110625948 324 YAALSVAIAKELGLNPEK------------------VNINGGAIALGHPLGASG 359
Cdd:PRK08256 293 FSANELLTYEALGLCPEGeaekfiddgdntyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
299-345 |
7.35e-03 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 37.90 E-value: 7.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 110625948 299 PAIKQAVAKAGWSLEDVDLFEINEAYAALSVAIAKELGLNPEKVNIN 345
Cdd:cd00830 227 ESIEEALEKAGLTPDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVN 273
|
|
| |
