|
Name |
Accession |
Description |
Interval |
E-value |
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
8-394 |
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: 577.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 8 FVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKETPALT 87
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQ-NPARQAALLAGLPESVPATT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDiKLEDSLWVSLTDQHVQLPMAMTAEN 167
Cdd:cd00751 80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLN-TLDGMLDDGLTDPFTGLSMGITAEN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTA 247
Cdd:cd00751 159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 248 GNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 328 LAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
5-393 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 564.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSdAIYLARHVGLRVGIPKETP 84
Cdd:PRK05790 2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGA-GQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGsDIKLEDSL-WVSLTDQHVQLPMAM 163
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMG-DVELVDTMiHDGLTDAFNGYHMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 164 TAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKLPPVFKKD 242
Cdd:PRK05790 160 TAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVvDTDEHPRPDTTAESLAKLRPAFDKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 243 GTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEA 322
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614485 323 FAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVII 393
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIV 390
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
7-393 |
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: 551.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 7 VFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKETPAL 86
Cdd:COG0183 4 VVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQ-NPARQAALLAGLPESVPAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLgsDIKLEDSL-WVSLTDQHVQLPMAMTA 165
Cdd:COG0183 83 TVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM--NAKLVDPMiNPGLTDPYTGLSMGETA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 166 ENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTV 245
Cdd:COG0183 161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 246 TAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAP 325
Cdd:COG0183 241 TAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167614485 326 QYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVII 393
Cdd:COG0183 321 QVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALII 388
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
9-394 |
8.45e-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: 479.80 E-value: 8.45e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 9 VVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKETPALTI 88
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAYTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 89 NRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV-RNVRFGTKLGsDIKLEDSLWVSLTDQHVQLPMAMTAEN 167
Cdd:TIGR01930 80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVpRSLRWGVKPG-NAELEDARLKDLTDANTGLPMGVTAEN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTA 247
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 248 GNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 328 LAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
5-394 |
8.82e-165 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 467.51 E-value: 8.82e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETP 84
Cdd:PRK09051 3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQETP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGsDIKLEDSLWVSLTDQHVQLPMAMT 164
Cdd:PRK09051 83 AFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMG-DAKLVDMMVGALHDPFGTIHMGVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 165 AENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKD-G 243
Cdd:PRK09051 162 AENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKEnG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 244 TVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAF 323
Cdd:PRK09051 242 TVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAF 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614485 324 APQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK09051 322 AAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFE 392
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
4-394 |
6.12e-137 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 397.02 E-value: 6.12e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 4 LRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSA-GKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKE 82
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 83 TPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRnvRFGTKLGSDIKLEDSL--W----VSLTDQH 156
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMG--KADSAFSRQAEIFDTTigWrfvnPLMKAQY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 157 VQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQT-MQVDEHARPQTTLEQLQKL 235
Cdd:PRK09050 159 GVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVvVDRDEHPRPETTLEALAKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 236 PPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMD 315
Cdd:PRK09050 239 KPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 316 LVEVNEAFAPQYLAVERSLDL--DISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVII 393
Cdd:PRK09050 319 VIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAI 398
|
.
gi 167614485 394 Q 394
Cdd:PRK09050 399 E 399
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
4-397 |
1.60e-136 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 395.90 E-value: 1.60e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 4 LRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGnvlQS--SSDAIYLARHVGLRVGIPK 81
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFG---QGypNGEAPAIGRVAALDAGLPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 82 ETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSdIKLEDSLWVS-LTDQHVQLP 160
Cdd:PRK06205 78 TVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGG-VQLHDRLARGrETAGGRRFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 ----MAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKL 235
Cdd:PRK06205 157 vpggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVvDRDEHPRADTTLESLAKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 236 PPVFKK---DGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLK 312
Cdd:PRK06205 237 RPIMGKqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 313 DMDLVEVNEAFAPQYLAVERSL---DLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGI 389
Cdd:PRK06205 317 DIDLIELNEAFAAQVLAVLKEWgfgADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGL 396
|
....*...
gi 167614485 390 AVIIQSTA 397
Cdd:PRK06205 397 AAVFERVN 404
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
9-394 |
2.10e-130 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 380.21 E-value: 2.10e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 9 VVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIyLARHVGLRVGIPKETPALTI 88
Cdd:PRK08235 6 IVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQI-PSRQAARAAGIPWEVQTETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 89 NRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGS----DIKLEDSLWVSLTDQHvqlpMAMT 164
Cdd:PRK08235 85 NKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDneviDLMVADGLTCAFSGVH----MGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 165 AENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQ-TMQVDEHARPQTTLEQLQKLPPVFKKDG 243
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPiVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 244 TVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAF 323
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614485 324 APQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
5-394 |
7.66e-130 |
|
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: 378.74 E-value: 7.66e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAG-KVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKET 83
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 84 PALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRnvRFGTKLGSDIKLEDSL--WVSLTDQHVQL-- 159
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMG--KADSAFSRSAKIEDTTigWRFINPLMKALyg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 160 --PMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQT-MQVDEHARPQTTLEQLQKLP 236
Cdd:TIGR02430 159 vdSMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTvVDQDEHPRPETTLEGLAKLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 237 PVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDL 316
Cdd:TIGR02430 239 PVVRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 317 VEVNEAFAPQYLAVERSLDL--DISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:TIGR02430 319 IELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIE 398
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
3-395 |
1.00e-120 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 355.49 E-value: 1.00e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 3 LLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKE 82
Cdd:PRK06633 1 MTKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQ-NPARQTLIHAGIPKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 83 TPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMS---QAPYcvrnVRFGTKLGsDIKLEDSL-WVSLTDQHVQ 158
Cdd:PRK06633 80 VPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSY----IRAGAKFG-DIKMVDLMqYDGLTDVFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 159 LPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPV 238
Cdd:PRK06633 155 VFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 239 FKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVE 318
Cdd:PRK06633 235 FDKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIE 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 319 VNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQS 395
Cdd:PRK06633 315 VNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
7-394 |
1.04e-119 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 353.15 E-value: 1.04e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 7 VFVVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALS-AGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETP 84
Cdd:PRK09052 8 AYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAqVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPNSVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcvrnvrfgtkLGSDIKLEDSLWVSltDQHVQLP--MA 162
Cdd:PRK09052 88 GVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM----------MGNKPSMSPAIFAR--DENVGIAygMG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 163 MTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKK----------GKQTMQVDEHARPQTTLEQL 232
Cdd:PRK09052 156 LTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatgevdvKTRTVDLDEGPRADTSLEGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 233 QKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLK 312
Cdd:PRK09052 236 AKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 313 DMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVI 392
Cdd:PRK09052 316 DLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGI 395
|
..
gi 167614485 393 IQ 394
Cdd:PRK09052 396 FE 397
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
7-266 |
1.21e-117 |
|
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: 342.75 E-value: 1.21e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 7 VFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIyLARHVGLRVGIPKETPAL 86
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQN-PARQAALKAGIPDSAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV-RNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTA 165
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 166 ENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTV 245
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
|
250 260
....*....|....*....|.
gi 167614485 246 TAGNASGVADGAGAVIIASED 266
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
8-394 |
1.51e-117 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 347.54 E-value: 1.51e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 8 FVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALT 87
Cdd:PRK08131 5 YIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTVPGQT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRfgTKLGSDIKLEDSLWVS------LTDQHVQLPM 161
Cdd:PRK08131 85 VNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAE--SAFSRDAKVFDTTIGArfpnpkIVAQYGNDSM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 162 AMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQV--DEHARPQTTLEQLQKLPPVF 239
Cdd:PRK08131 163 PETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLPPKLVaeDEHPRPSSTVEALTKLKPLF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 240 KkDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEV 319
Cdd:PRK08131 243 E-GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEI 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 320 NEAFAPQYLAVERSLDLDI--SKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK08131 322 NEAFASQVLGCLKGLGVDFddPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
7-394 |
8.92e-116 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 342.64 E-value: 8.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 7 VFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKETPAL 86
Cdd:PRK05656 4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQ-NPARQAAIKAGLPHSVPAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGS----DIKLEDSLWVSLTDQHvqlpMA 162
Cdd:PRK05656 83 TLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHaqlvDSMITDGLWDAFNDYH----MG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 163 MTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQ-TMQVDEHARPQTTLEQLQKLPPVFKK 241
Cdd:PRK05656 159 ITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPlAFATDEQPRAGTTAESLAKLKPAFKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 242 DGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNE 321
Cdd:PRK05656 239 DGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167614485 322 AFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK05656 319 AFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
5-394 |
9.02e-113 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 335.01 E-value: 9.02e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 5 RGVFVVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALSAG-KVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKE 82
Cdd:PRK08947 2 EDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPHS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 83 TPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcVRNVRFGTKLGSDIKLEDSLwvsltdqhvqlpMA 162
Cdd:PRK08947 82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPM-NHGVDFHPGLSKNVAKAAGM------------MG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 163 MTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKG-KQTMQVDEHARPQTTLEQLQKLPPVFK- 240
Cdd:PRK08947 149 LTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGvLKLFDYDEVIRPETTVEALAALRPAFDp 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 241 KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVN 320
Cdd:PRK08947 229 VNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELN 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 321 EAFAPQYLAVERSLDLDIS---KTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK08947 309 EAFAAQSLPCLKDLGLLDKmdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
5-395 |
4.41e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 331.98 E-value: 4.41e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSsDAIYLARHVGLRVGIPKETP 84
Cdd:PRK08170 3 RPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSP-DEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRN--VR----------FGTKLGSDIKLEDS----- 147
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEkmVRwlagwyaaksIGQKLAALGKLRPSylapv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 148 --LWVSLTDQHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNdEMAPIevKTKKGKQTMQvDEHARP 225
Cdd:PRK08170 162 igLLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL--FDRDGKFYDH-DDGVRP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 226 QTTLEQLQKLPPVF-KKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGAL 304
Cdd:PRK08170 238 DSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 305 KKAGLSLKDMDLVEVNEAFAPQYLAVERSLD-----------------LDISKTNVNGGAIALGHPLGGSGSRITAHLVH 367
Cdd:PRK08170 318 QRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLHLLH 397
|
410 420
....*....|....*....|....*...
gi 167614485 368 ELRRRGGKYAVGSACIGGGQGIAVIIQS 395
Cdd:PRK08170 398 ALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
4-394 |
3.85e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 328.60 E-value: 3.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 4 LRGVFVVAAKRTPFGAYGGllKD-----FTATDLSEFAA---KAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGL 75
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRP--KDpqkdvFNNIRPEELAAmliNRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 76 RVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAP-YCVRNVRFGTKLGSDIKLEDslwvslTD 154
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPmGDNPHIEPNPKLLTDPKYIE------YD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 155 QHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQK 234
Cdd:PRK06445 153 LTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 235 LPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDM 314
Cdd:PRK06445 233 LPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 315 DLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK06445 313 DLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLE 392
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
5-397 |
6.13e-109 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 325.51 E-value: 6.13e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLqSSSDAIYLARHVGLRVGIPKETP 84
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVL-SANLGQAPARQAALGAGLPPSTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGS----DIKLEDSLWVSLTDQHvqlp 160
Cdd:PLN02644 80 CTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHdtvvDGMLKDGLWDVYNDFG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 MAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARP-QTTLEQLQKLPPVF 239
Cdd:PLN02644 156 MGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIVDKDEGLgKFDPAKLRKLRPSF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 240 KKD-GTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVE 318
Cdd:PLN02644 236 KEDgGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614485 319 VNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA 397
Cdd:PLN02644 316 INEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELMQ 394
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
4-390 |
8.91e-109 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 324.78 E-value: 8.91e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 4 LRGVFVVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKE 82
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 83 TPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcvrnvrfgtkLGSDIKLEdslwVSLTDQHVQLPMA 162
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPM----------MGHVVRPN----PRLVEAAPEYYMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 163 M--TAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEV---------KTKKGKQTMQVDEHARPQTTLEQ 231
Cdd:PRK07661 147 MghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVtlrtvgennKLQEETITFSQDEGVRADTTLEI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 232 LQKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSL 311
Cdd:PRK07661 227 LGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLEL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614485 312 KDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIA 390
Cdd:PRK07661 307 SDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAA 385
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
8-394 |
2.52e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 315.88 E-value: 2.52e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 8 FVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALT 87
Cdd:PRK07801 5 YIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEVPGVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCvRNVRFGTKLG-SDIKLEDSLWVS-LTDQHVQLPMAmtA 165
Cdd:PRK07801 85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPIS-SAMTAGEQLGfTSPFAESKGWLHrYGDQEVSQFRG--A 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 166 ENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTkkgkqtmqVDEHARpQTTLEQLQKLPPVFKkDGTV 245
Cdd:PRK07801 162 ELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGGVT--------VDEGPR-ETSLEKMAGLKPLVE-GGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 246 TAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAP 325
Cdd:PRK07801 232 TAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAP 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614485 326 QYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK07801 312 VVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
7-394 |
2.92e-102 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 310.16 E-value: 2.92e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 7 VFVVAAKRTPF-GAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPA 85
Cdd:PLN02287 48 VVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 86 LTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcVRNVRFGTKLGSDIKLEDSLwvsltdqhvqLPMAMTA 165
Cdd:PLN02287 128 RTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPM-AWEGGVNPRVESFSQAQDCL----------LPMGITS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 166 ENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQ------TMQVDEHARPQTTLEQLQKLPPVF 239
Cdd:PLN02287 197 ENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDPKTgeekpiVISVDDGIRPNTTLADLAKLKPVF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 240 KKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEV 319
Cdd:PLN02287 277 KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEI 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 320 NEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRG--GKYAVGSACIGGGQGIAVIIQ 394
Cdd:PLN02287 357 NEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFE 433
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
9-394 |
3.40e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 298.46 E-value: 3.40e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 9 VVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALSagKV---SPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPkETP 84
Cdd:PRK07851 6 IVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALD--KVpalDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD-FLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYC-------VRNVRFGTKLGSDIKLEDSLWVSLTDQH- 156
Cdd:PRK07851 83 GTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGnsdslpdTKNPLFAEAQARTAARAEGGAEAWHDPRe 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 157 ------VQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPieVKTKKGKqTMQVDEHARPQTTLE 230
Cdd:PRK07851 163 dgllpdVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITP--VTLPDGT-VVSTDDGPRAGTTYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 231 QLQKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLS 310
Cdd:PRK07851 240 KVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAGMS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 311 LKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIA 390
Cdd:PRK07851 320 IDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGGGQGMA 399
|
....
gi 167614485 391 VIIQ 394
Cdd:PRK07851 400 MVLE 403
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
9-390 |
4.82e-98 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 297.45 E-value: 4.82e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 9 VVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALT 87
Cdd:PRK07108 6 IVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVTVPGMT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSqapyCVRNvrfgtklGSDIKLEDSLWVSLTDQHVQLPMAMTAEN 167
Cdd:PRK07108 86 VNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIS----CVQN-------EMNRHMLREGWLVEHKPEIYWSMLQTAEN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQ----------TMQVDEHARPQTTLEQLQKLPP 237
Cdd:PRK07108 155 VAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKatgrlftkevTVSADEGIRPDTTLEGVSKIRS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 238 VFKkDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLV 317
Cdd:PRK07108 235 ALP-GGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLW 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167614485 318 EVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIA 390
Cdd:PRK07108 314 ELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
7-394 |
4.17e-96 |
|
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: 292.23 E-value: 4.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 7 VFVVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALSAG-KVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETP 84
Cdd:TIGR02445 2 VVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARNpKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPycvrnvrfgTKLGSDIKLEDSLWVSLTDQHvqlpMAMT 164
Cdd:TIGR02445 82 AVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP---------MMHGVDFHPGMSLHVAKAAGM----MGLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 165 AENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGK-QTMQVDEHARPQTTLEQLQKLPPVFK-KD 242
Cdd:TIGR02445 149 AEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFlKQFDYDEVIRPETTVESLAALRPAFDpKN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 243 GTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEA 322
Cdd:TIGR02445 229 GTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167614485 323 FAPQYLAVERSL---DLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:TIGR02445 309 FAAQALPCLKDLgllDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
8-394 |
4.68e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 292.56 E-value: 4.68e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 8 FVVAAKRTPFG--AYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPA 85
Cdd:PRK08242 5 YIYDAVRTPRGkgKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPETVPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 86 LTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPycvrnvrfgtkLGSDikleDSLWVslTDQHVQL-----P 160
Cdd:PRK08242 85 VQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP-----------MGSD----GGAWA--MDPSTNFptyfvP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 MAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPieVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK 240
Cdd:PRK08242 148 QGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVP--VKDQNGLTILDHDEHMRPGTTMESLAKLKPSFA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 241 KDGTV---------------------TAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPA 299
Cdd:PRK08242 226 MMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 300 ISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVG 379
Cdd:PRK08242 306 TRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALI 385
|
410
....*....|....*
gi 167614485 380 SACIGGGQGIAVIIQ 394
Cdd:PRK08242 386 TLCVGGGMGIATIIE 400
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
8-394 |
5.08e-93 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 284.70 E-value: 5.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 8 FVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALT 87
Cdd:PRK06504 5 YIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPESVPGTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVrNVRFGTKLGSDIKLEDSLWVSLTDqhVQLPMAMTAEN 167
Cdd:PRK06504 85 IDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGS-PSTLPAKNGLGHYKSPGMEERYPG--IQFSQFTGAEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKLPPVfKKDGTVT 246
Cdd:PRK06504 162 MAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMhTVDEGIRFDATLEGIAGVKLI-AEGGRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 247 AGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQ 326
Cdd:PRK06504 241 AATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167614485 327 YLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK06504 321 PLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
4-388 |
1.81e-91 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 280.36 E-value: 1.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 4 LRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQS---SSDAIYLARHVGLRVGIP 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAgvgQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 81 KetpaLTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV-RNVRFGTK--LGSDIKLEDSLWVS-LTDQH 156
Cdd:PRK06366 81 K----YTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPKhlLHKNYKIDDAMLVDgLIDAF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 157 VQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEvktkkgkqTMQVDEHARpQTTLEQLQKLP 236
Cdd:PRK06366 157 YFEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIR-KTTMEDLAKLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 237 PVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDL 316
Cdd:PRK06366 228 PAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167614485 317 VEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQG 388
Cdd:PRK06366 308 VEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGA 379
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
7-394 |
1.36e-85 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 265.60 E-value: 1.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 7 VFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIyLARHVGLRVGIPKETPAL 86
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQA-PARQAALGAGLPLSVGCT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQ-LPMAMTA 165
Cdd:PRK06954 88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKgRLMGTFA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 166 ENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARpQTTLEQLQKLPPVFKKDGTV 245
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPF-KANPEKIPTLKPAFSKTGTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 246 TAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAP 325
Cdd:PRK06954 247 TAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614485 326 QYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK06954 327 VTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
7-396 |
1.87e-81 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 256.06 E-value: 1.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 7 VFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSsDAIYLARHVGLRVGIPKETPAL 86
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMP-EAPNIAREIVLGTGMNVHTDAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV--------------RNVRFGTKLGSDIKLEDSLWV-- 150
Cdd:PRK08963 86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVskklaralvdlnkaRTLGQRLKLFSRLRLRDLLPVpp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 151 SLTDQHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMapIEVKTKKGKQTMQVDEHARPQTTLE 230
Cdd:PRK08963 166 AVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEV--MTAHVPPYKQPLEEDNNIRGDSTLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 231 QLQKLPPVF-KKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDP-SIMGIGPVPAISGALKKAG 308
Cdd:PRK08963 244 DYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLALERAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 309 LSLKDMDLVEVNEAFAPQYLA----------VERSL-------DLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRR 371
Cdd:PRK08963 324 LTLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRR 403
|
410 420
....*....|....*....|....*
gi 167614485 372 RGGKYAVGSACIGGGQGIAVIIQST 396
Cdd:PRK08963 404 RGGGLGLTTACAAGGLGAAMVLEVE 428
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
9-394 |
2.14e-79 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 249.25 E-value: 2.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 9 VVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALTI 88
Cdd:PRK07850 6 IVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYHVGATTI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 89 NRLCGSGFQS--IVNGCqeICVKEAEVVLCGGTESMSQAPycvrnvrFGTKLGSDIKL--EDSLWVSLTDQHVqlpmamT 164
Cdd:PRK07850 86 DCQCGSAQQAnhLVAGL--IAAGAIDVGIACGVEAMSRVP-------LGANAGPGRGLprPDSWDIDMPNQFE------A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 165 AENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIE--VKTKKGKQTMQVDEHARPQ----TTLEQLQKLPPV 238
Cdd:PRK07850 151 AERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapVLDEEGQPTGETRLVTRDQglrdTTMEGLAGLKPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 239 FKkDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVE 318
Cdd:PRK07850 231 LE-GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167614485 319 VNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK07850 310 INEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
9-394 |
3.64e-79 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 248.14 E-value: 3.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 9 VVAAKRTPFGAYGGLLKDFTATDLsefAAKAALSAGKVSPETVDSVIMGNVLQSSSDaiyLARHVGLRVGIPKETPALTI 88
Cdd:PRK06690 5 IVEAKRTPIGKKNGMLKDYEVQQL---AAPLLTFLSKGMEREIDDVILGNVVGPGGN---VARLSALEAGLGLHIPGVTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 89 NRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRnVRFGTKlgsdikledslWVSLTDqhvqlpMAMTAENL 168
Cdd:PRK06690 79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNR-ARFSPE-----------TIGDPD------MGVAAEYV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 169 AVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEvktkkgkqtMQVDEHARPQTTLEQL-QKLPPVFKKDGTVTA 247
Cdd:PRK06690 141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN---------GLLDESIKKEMNYERIiKRTKPAFLHNGTVTA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 248 GNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:PRK06690 212 GNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKV 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 328 LAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK06690 292 VACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
8-394 |
1.57e-71 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 230.05 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 8 FVVAAKRTPFG---AYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETP 84
Cdd:PRK06025 5 YIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYDIKAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSqapYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMT 164
Cdd:PRK06025 85 GVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMS---YTAAMAAEDMAAGKPPLGMGSGNLRLRALHPQSHQGVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 165 AENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPieVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKK--- 241
Cdd:PRK06025 162 GDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVP--VYRDDGSVALDHEEFPRPQTTAEGLAALKPAFTAiad 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 242 ----DGTVT-------------------AGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVP 298
Cdd:PRK06025 240 ypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 299 AISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAV 378
Cdd:PRK06025 320 AAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGL 399
|
410
....*....|....*.
gi 167614485 379 GSACIGGGQGIAVIIQ 394
Cdd:PRK06025 400 VTMCAAGGMAPAIIIE 415
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
273-394 |
4.33e-67 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 208.65 E-value: 4.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 273 FTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGH 352
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 167614485 353 PLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
10-395 |
8.01e-64 |
|
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: 209.27 E-value: 8.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 10 VAAKRTPFGAYGGLLKDFTATDLSEFAAKA---ALSAGKVSPETVDSVIMGNVLQSSSDAIyLARHVGLRVGIPKETPAL 86
Cdd:cd00826 1 AGAAMTAFGKFGGENGADANDLAHEAGAKAiaaALEPAGVAAGAVEEACLGQVLGAGEGQN-CAQQAAMHAGGLQEAPAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSqapYCVRNVRFGTKLgsdikledslwvsltdqhvqlpmamtae 166
Cdd:cd00826 80 GMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME---TSAENNAKEKHI---------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 167 NLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQT--TLEQLQKLPPVFKKDGT 244
Cdd:cd00826 129 DVLINKYGMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGDeaSLDEIAKLRPAFDKEDF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 245 VTAGNASGVADGAGAVIIASEDAVKKHNFT-------PLARIVGYFVSGCDPS----IMGIGPVPAISGALKKAGLSLKD 313
Cdd:cd00826 209 LTAGNACGLNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 314 MDLVEVNEAFAPQYLAVERSLDLD------------------ISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGK 375
Cdd:cd00826 289 LDLIEAHDAFAANACATNEALGLCpegqggalvdrgdntyggKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGK 368
|
410 420
....*....|....*....|....*
gi 167614485 376 YAVGSA-----CIGGGQGIAVIIQS 395
Cdd:cd00826 369 RQGAGAglallCIGGGGGAAMCIES 393
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-395 |
3.77e-62 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 205.90 E-value: 3.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 1 MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDaIYLARHVGLRVGIP 80
Cdd:PRK09268 3 MPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRD-FNLTRECVLGSALS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 81 KETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV------------RNVRFGTKLGSDIKLEDSL 148
Cdd:PRK09268 82 PYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVneglrkillelnRAKTTGDRLKALGKLRPKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 149 WVSLTDQHVQ----LPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKkgkqtmqvDEHAR 224
Cdd:PRK09268 162 LAPEIPRNGEprtgLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR--------DNNLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 225 PQTTLEQLQKLPPVFKK--DGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGY------FVSGCDPSIMGigP 296
Cdd:PRK09268 234 PDSSLEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetaavdFVHGKEGLLMA--P 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 297 VPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAV-----------ER-SLD-----LDISKTNVNGGAIALGHPLGGSGS 359
Cdd:PRK09268 312 AYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATlkawedeeycrERlGLDaplgsIDRSKLNVNGSSLAAGHPFAATGG 391
|
410 420 430
....*....|....*....|....*....|....*.
gi 167614485 360 RITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQS 395
Cdd:PRK09268 392 RIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
15-393 |
1.77e-23 |
|
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: 100.42 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 15 TPFGAYGGLlkdfTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSD---AIYLARHVGLRVGipketPALTINRL 91
Cdd:cd00829 6 TPFGRRSDR----SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQsfpGALIAEYLGLLGK-----PATRVEAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 92 CGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcvrNVRFGTKLGSdikLEDSLWVSLTDQHVQLPMAMTAENLAVK 171
Cdd:cd00829 77 GASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPT---GDEAGGRASD---LEWEGPEPPGGLTPPALYALAARRYMHR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 172 HKISREECDKYALQsQQRWKAANDAGYFNDEMapievktkkgkqtmqvdeharpqtTLEQLQKLPPVFkkdGTVTAGNAS 251
Cdd:cd00829 151 YGTTREDLAKVAVK-NHRNAARNPYAQFRKPI------------------------TVEDVLNSRMIA---DPLRLLDCC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 252 GVADGAGAVIIASEDAVKKHnFTPLARIVG-------YFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFA 324
Cdd:cd00829 203 PVSDGAAAVVLASEERAREL-TDRPVWILGvgaasdtPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 325 PQ-YLAVE--------------RSLDLDIS---KTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIG-- 384
Cdd:cd00829 282 IAeLLALEdlgfcekgeggklvREGDTAIGgdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGla 361
|
410
....*....|..
gi 167614485 385 ---GGQGIAVII 393
Cdd:cd00829 362 hniGGTGSAAVV 373
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
247-393 |
3.64e-23 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 97.51 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 247 AGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPS----IMGIGPVPAISGALKKAGLSLKDMDLVEVNEA 322
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 323 FAPQYLAVERSLDLDISK---TNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKY-------AVGSACIGGGQGIAVI 392
Cdd:cd00327 174 GTPIGDAVELALGLDPDGvrsPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtpreprtVLLLGFGLGGTNAAVV 253
|
.
gi 167614485 393 I 393
Cdd:cd00327 254 L 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
4-388 |
5.60e-14 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 72.62 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 4 LRGVFVVAAKRTPFGAygglLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL------QSSSdAIYLARHVGLRv 77
Cdd:PRK06064 1 MRDVAIIGVGQTKFGE----LWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSaglfvsQEHI-AALIADYAGLA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 78 gipkETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLgsdikleDSLWVSLtdQHV 157
Cdd:PRK06064 75 ----PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAG-------DYEWEEF--FGA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 158 QLP--MAMTAenlavkhkisREECDKYalqsqqrwkaandaGYFNDEMAPIEVKTKKgKQTMQVDEHARPQTTLEQLQKL 235
Cdd:PRK06064 142 TFPglYALIA----------RRYMHKY--------------GTTEEDLALVAVKNHY-NGSKNPYAQFQKEITVEQVLNS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 236 PPVFKKdgtVTAGNASGVADGAGAVIIASEDAVKKHNFTPL-----ARIVGYFVSGCDPSIMGIGP-VPAISGALKKAGL 309
Cdd:PRK06064 197 PPVADP---LKLLDCSPITDGAAAVILASEEKAKEYTDTPVwikasGQASDTIALHDRKDFTTLDAaVVAAEKAYKMAGI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 310 SLKDMDLVEVNEAFA-PQYLAVErslDLDISK--------------------TNVNGGAIALGHPLGGSGSRITAHLVHE 368
Cdd:PRK06064 274 EPKDIDVAEVHDCFTiAEILAYE---DLGFAKkgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQ 350
|
410 420
....*....|....*....|....*..
gi 167614485 369 LRRR--GGKYAVGSACIG-----GGQG 388
Cdd:PRK06064 351 LRGEaeKGRQQVIGAGYGlthnvGGTG 377
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
236-381 |
5.05e-10 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 60.86 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 236 PPVFKKDGT---VTAG-----NASGVADGAGAVIIASEDAVKKH-NFTPLARIVGY-------------FVSGCDPSIMg 293
Cdd:PRK06289 197 DEATNDDDAtnpVVEGrlrrqDCSQVTDGGAGVVLASDAYLRDYaDARPIPRIKGWghrtaplgleqklDRSAGDPYVL- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 294 igpvP----AISGALKKAGLSLKDMDLVEVNEAFAP-QYLAVE--------------RSLDLDISKT---NVNGGAIALG 351
Cdd:PRK06289 276 ----PhvrqAVLDAYRRAGVGLDDLDGFEVHDCFTPsEYLAIDhigltgpgeswkaiENGEIAIGGRlpiNPSGGLIGGG 351
|
170 180 190
....*....|....*....|....*....|
gi 167614485 352 HPLGGSGSRITAHLVHELRRRGGKYAVGSA 381
Cdd:PRK06289 352 HPVGASGVRMLLDAAKQVTGTAGDYQVEGA 381
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
255-358 |
4.13e-07 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 51.71 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 255 DGAGAVIIASEDAVKKHNFTPLARIVGYFVSgCD------PSIMGIGPVPAISGALKKAGLSLKDMDLV----------E 318
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGMT-GDayhmtaPAPDGEGAARAMKLALKDAGINPEDIDYInahgtstpagD 310
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 167614485 319 VNEAfapqyLAVERSLDLDISKTNVNGGAIALGHPLGGSG 358
Cdd:PRK07314 311 KAET-----QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAG 345
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
7-358 |
9.53e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 47.25 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 7 VFVVAAKRTPFGAygglLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGN-----VLQSSSDAIYLARHVGLRVgipk 81
Cdd:PRK07516 4 ASIVGWAHTPFGK----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHfnagfSPQDFPASLVLQADPALRF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 82 eTPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPycvrNVRFGTKL-GSDIKLEDSlwvsltdqhvQLP 160
Cdd:PRK07516 76 -KPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP----TAEVGDILlGASYLKEEG----------DTP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 MAMTAenlaVKHKISREECDKYALQSqqrwkaandagyfnDEMAPIEVKTKKgkqtmqvDEHARPqttLEQLQK-LPPVF 239
Cdd:PRK07516 141 GGFAG----VFGRIAQAYFQRYGDQS--------------DALAMIAAKNHA-------NGVANP---YAQMRKdLGFEF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 240 KKdgTVTAGN-----------ASGVADGAGAVIIASEDAVKK-------------HNFTPLARIvgyfvsgcDPSIMGiG 295
Cdd:PRK07516 193 CR--TVSEKNplvagplrrtdCSLVSDGAAALVLADAETARAlqravrfrarahvNDFLPLSRR--------DPLAFE-G 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 296 PVPAISGALKKAGLSLKDMDLVEVNEAF-------------APQ---YLAVERSLDLDISKTNVN--GGAIALGHPLGGS 357
Cdd:PRK07516 262 PRRAWQRALAQAGVTLDDLSFVETHDCFtiaelieyeamglAPPgqgARAIREGWTAKDGKLPVNpsGGLKAKGHPIGAT 341
|
.
gi 167614485 358 G 358
Cdd:PRK07516 342 G 342
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
242-359 |
1.59e-05 |
|
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: 46.63 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 242 DGTVtagnasgVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSgCD------PSIMGIGPVPAISGALKKAGLSLKDMD 315
Cdd:COG0304 225 DGFV-------LGEGAGVLVLEELEHAKARGAKIYAEVVGYGAS-SDayhitaPAPDGEGAARAMRAALKDAGLSPEDID 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 167614485 316 LV----------EVNEAfapqyLAVERSLDLDISKTNVNggAI--ALGHPLGGSGS 359
Cdd:COG0304 297 YInahgtstplgDAAET-----KAIKRVFGDHAYKVPVS--STksMTGHLLGAAGA 345
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
254-369 |
3.98e-05 |
|
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: 45.32 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 254 ADGAGAVIIASEDAVKKHNFTPLARIVGYfVSGCDPSIMGI------GPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:cd00825 160 GDGAGALVVEELEHALARGAHIYAEIVGT-AATIDGAGMGAfapsaeGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIG 238
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 167614485 328 LAVERSLDLDISKtnvnGGAIALGHPLGGSGSRITAHLVHEL 369
Cdd:cd00825 239 DVKELKLLRSEFG----DKSPAVSATKAMTGNLSSAAVVLAV 276
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
253-359 |
6.49e-05 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 44.78 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 253 VADGAGAVIIASEDAVKKHNFTPLARIVGYFVSG-----CDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:PLN02836 253 IGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGdahhiTQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAHATSTPLG 332
|
90 100 110
....*....|....*....|....*....|....*....
gi 167614485 328 LAVERSLDLDISKTNVNGGAIAL-------GHPLGGSGS 359
Cdd:PLN02836 333 DAVEARAIKTVFSEHATSGGLAFsstkgatGHLLGAAGA 371
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
254-359 |
6.84e-05 |
|
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: 44.84 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 254 ADGAGAVIIASEDAVKKHNFTPLARIVGYFVSgCD------PSIMGIGPVPAISGALKKAGLSLKDMDLV---------- 317
Cdd:cd00834 230 GEGAGVLVLESLEHAKARGAKIYAEILGYGAS-SDayhitaPDPDGEGAARAMRAALADAGLSPEDIDYInahgtstpln 308
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 167614485 318 EVNEAfapqyLAVERSLDLDISKTNVNG--GAIalGHPLGGSGS 359
Cdd:cd00834 309 DAAES-----KAIKRVFGEHAKKVPVSStkSMT--GHLLGAAGA 345
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
7-387 |
1.90e-04 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 43.09 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 7 VFVVAAKRTPFGAYGgllkDFTATDLSEFAAKAALSAGKVSPETVDSVIMG---NVLQSSSDAIYLARHVGLrvgipKET 83
Cdd:PRK06157 9 VAILGMGCTKFGERW----DAGAEDLMVEAFLEALADAGIEPKDIDAAWFGthyDEIGSGKSGTPLSRALRL-----PNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 84 PALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVR-FGTklgsdikLEDSLWVSLTDqhvqlP-- 160
Cdd:PRK06157 80 PVTRVENFCATGSEAFRGAVYAVASGAYDIALALGVEKLKDTGYGGLPVAnPGT-------LADMTMPNVTA-----Pgn 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 MAMTAENLAVKHKISREECdkyalqsqqrwKAAndagyfndeMAPIEVKTKKGKqTMQVDEHARPQTTLEQLQKLPPVFK 240
Cdd:PRK06157 148 FAQLASAYAAKYGVSREDL-----------KRA---------MAHVSVKSHANG-ARNPKAHLRKAVTEEQVLKAPMIAG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 241 KDGTVtagNASGVADGAGAVIIASEDAVKKHNFTPLARI------VGYFVSGCDPSIMGIgPVPAISGALKKA----GLS 310
Cdd:PRK06157 207 PLGLF---DCCGVSDGAAAAIVTTPEIARALGKKDPVYVkalqlaVSNGWELQYNGWDGS-YFPTTRIAARKAyreaGIT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 311 --LKDMDLVEVNEAFAPQYLAVERslDLDISK--------------------TNVNGGAIALGHPLGGSGSRITAHLVHE 368
Cdd:PRK06157 283 dpREELSMAEVHDCFSITELVTME--DLGLSErgqawrdvldgffdadgglpCQIDGGLKCFGHPIGASGLRMLYEMYLQ 360
|
410 420
....*....|....*....|....
gi 167614485 369 LRRRGGKYAVGSACIG-----GGQ 387
Cdd:PRK06157 361 LLGRAGERQLKNPRLAlthnlGGA 384
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
251-376 |
4.21e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 42.19 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 251 SGVADGAGAVIIASEDAVKKHNFTPL-ARIVGYFVSGC----------DPSIMgIGPVPAISGALKKAGLSLKDMDLVEV 319
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEIKSLACasgnlyedppDATRM-FTSRAAAQKALSMAGVKPSDLQVAEV 334
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 320 NEAFAPQYLAVERSLDldISK--------------------TNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKY 376
Cdd:PTZ00455 335 HDCFTIAELLMYEALG--IAEyghakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEY 409
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
256-317 |
7.97e-04 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 41.17 E-value: 7.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 256 GAGAVIIASEDAVKKHNFTPLARIVGYFV-----SGCDPSImgIGPVPAISGALKKAGLSLKDMDLV 317
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMrldanRGPDPSL--EGEMRVIRAALRRAGLGPEDIDYV 304
|
|
|