|
Name |
Accession |
Description |
Interval |
E-value |
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
8-395 |
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: 569.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 8 FIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETGALT 87
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAG-EGQNPARQAALLAGLPESVPATT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGLDlKLEDTLWAGLTDQHVKLPMGMTAEN 167
Cdd:cd00751 80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLN-TLDGMLDDGLTDPFTGLSMGITAEN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQNLPPVFKKEGTVTA 247
Cdd:cd00751 159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 248 GNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQF 327
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 135762 328 LAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
5-393 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 546.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSdAAYLARHVGLRVGVPTETG 84
Cdd:PRK05790 2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGA-GQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGlDLKLEDTL-WAGLTDQHVKLPMGM 163
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMG-DVELVDTMiHDGLTDAFNGYHMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 164 TAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQNLPPVFKKE 242
Cdd:PRK05790 160 TAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVvDTDEHPRPDTTAESLAKLRPAFDKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 243 GTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEA 322
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 135762 323 FAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLII 393
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIV 390
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
7-395 |
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: 545.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETGAL 86
Cdd:COG0183 4 VVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPESVPAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGtkFGLDLKLEDTL-WAGLTDQHVKLPMGMTA 165
Cdd:COG0183 83 TVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWG--YRMNAKLVDPMiNPGLTDPYTGLSMGETA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQNLPPVFKKEGTV 245
Cdd:COG0183 161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 246 TAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAP 325
Cdd:COG0183 241 TAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 326 QFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:COG0183 321 QVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
9-394 |
2.93e-167 |
|
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: 473.25 E-value: 2.93e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 9 IVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVmQSSSDAAYLARHVGLRVGVPTETGALTL 88
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNV-LQAGEQQNIARQAALLAGLPESVPAYTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 89 NRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV-RNVRFGTKFGlDLKLEDTLWAGLTDQHVKLPMGMTAEN 167
Cdd:TIGR01930 80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVpRSLRWGVKPG-NAELEDARLKDLTDANTGLPMGVTAEN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQNLPPVFKKEGTVTA 247
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 248 GNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQF 327
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 135762 328 LAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
5-394 |
3.10e-164 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 465.97 E-value: 3.10e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETG 84
Cdd:PRK09051 3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQETP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGlDLKLEDTLWAGLTDQHVKLPMGMT 164
Cdd:PRK09051 83 AFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMG-DAKLVDMMVGALHDPFGTIHMGVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 165 AENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQNLPPVFKKE-G 243
Cdd:PRK09051 162 AENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKEnG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 244 TVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAF 323
Cdd:PRK09051 242 TVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAF 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 135762 324 APQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK09051 322 AAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFE 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
4-397 |
9.72e-135 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 391.27 E-value: 9.72e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 4 LRGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGnvmQS--SSDAAYLARHVGLRVGVPT 81
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFG---QGypNGEAPAIGRVAALDAGLPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 82 ETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGlDLKLEDTLWAG-LTDQHVKLP 160
Cdd:PRK06205 78 TVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGG-GVQLHDRLARGrETAGGRRFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 161 M--GM--TAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQNL 235
Cdd:PRK06205 157 VpgGMieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVvDRDEHPRADTTLESLAKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 236 PPVFKK---EGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLK 312
Cdd:PRK06205 237 RPIMGKqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 313 DMDLIDVNEAFAPQFLAVQKSL---DLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGI 389
Cdd:PRK06205 317 DIDLIELNEAFAAQVLAVLKEWgfgADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGL 396
|
....*...
gi 135762 390 SLIIQNTA 397
Cdd:PRK06205 397 AAVFERVN 404
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
4-394 |
1.74e-133 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 388.16 E-value: 1.74e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 4 LRGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSA-GKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTE 82
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 83 TGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRnvRFGTKFGLDLKLEDTL--W----AGLTDQH 156
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMG--KADSAFSRQAEIFDTTigWrfvnPLMKAQY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 157 VKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQT-MQVDEHARPQTTLEQLQNL 235
Cdd:PRK09050 159 GVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVvVDRDEHPRPETTLEALAKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 236 PPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMD 315
Cdd:PRK09050 239 KPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 316 LIDVNEAFAPQFLAVQKSLDL--DPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLII 393
Cdd:PRK09050 319 VIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAI 398
|
.
gi 135762 394 Q 394
Cdd:PRK09050 399 E 399
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
5-394 |
1.46e-127 |
|
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: 372.96 E-value: 1.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAG-KVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTET 83
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 84 GALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRnvRFGTKFGLDLKLEDTL--WAGLTDQHVKL-- 159
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMG--KADSAFSRSAKIEDTTigWRFINPLMKALyg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 160 --PMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQT-MQVDEHARPQTTLEQLQNLP 236
Cdd:TIGR02430 159 vdSMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTvVDQDEHPRPETTLEGLAKLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 237 PVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDL 316
Cdd:TIGR02430 239 PVVRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 317 IDVNEAFAPQFLAVQKSLDL--DPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:TIGR02430 319 IELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIE 398
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
9-394 |
8.22e-123 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 360.57 E-value: 8.22e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 9 IVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSD---AAYLARHVGLRVGVPTETga 85
Cdd:PRK08235 6 IVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGqipSRQAARAAGIPWEVQTET-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 86 ltLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFG----LDLKLEDTLWAGLTDQHvklpM 161
Cdd:PRK08235 84 --VNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGdnevIDLMVADGLTCAFSGVH----M 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 162 GMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQ-TMQVDEHARPQTTLEQLQNLPPVFK 240
Cdd:PRK08235 158 GVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPiVVAKDEAPRKDTTIEKLAKLKPVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 241 KEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVN 320
Cdd:PRK08235 238 KTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEIN 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 135762 321 EAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK08235 318 EAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
7-394 |
1.48e-122 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 360.09 E-value: 1.48e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 7 VFIVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSagKVP---PETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTE 82
Cdd:PRK09052 8 AYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVA--QVPgldPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPNS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 83 TGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSvrnvrfGTKFGLDLKLEDTlwagltDQHVKLP-- 160
Cdd:PRK09052 86 VGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMM------GNKPSMSPAIFAR------DENVGIAyg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 161 MGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKK----------GKQTMQVDEHARPQTTLE 230
Cdd:PRK09052 154 MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatgevdvKTRTVDLDEGPRADTSLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 231 QLQNLPPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLS 310
Cdd:PRK09052 234 GLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 311 LKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIS 390
Cdd:PRK09052 314 QDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAA 393
|
....
gi 135762 391 LIIQ 394
Cdd:PRK09052 394 GIFE 397
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
3-394 |
4.84e-117 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 345.86 E-value: 4.84e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 3 LLRGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAyLARHVGLRVGVPTE 82
Cdd:PRK06633 1 MTKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQN-PARQTLIHAGIPKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 83 TGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSvRNVRFGTKFGlDLKLEDTL-WAGLTDQHVKLPM 161
Cdd:PRK06633 80 VPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHG-SYIRAGAKFG-DIKMVDLMqYDGLTDVFSGVFM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 162 GMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQNLPPVFKK 241
Cdd:PRK06633 158 GITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 242 EGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNE 321
Cdd:PRK06633 238 NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 135762 322 AFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06633 318 AFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
8-395 |
1.88e-116 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 344.84 E-value: 1.88e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 8 FIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALT 87
Cdd:PRK08131 5 YIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTVPGQT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRfgTKFGLDLKLEDTLWAG------LTDQHVKLPM 161
Cdd:PRK08131 85 VNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAE--SAFSRDAKVFDTTIGArfpnpkIVAQYGNDSM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 162 GMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQV--DEHARPQTTLEQLQNLPPVF 239
Cdd:PRK08131 163 PETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLPPKLVaeDEHPRPSSTVEALTKLKPLF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 240 KkEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDV 319
Cdd:PRK08131 243 E-GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEI 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 135762 320 NEAFAPQFLAVQKSLDL--DPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:PRK08131 322 NEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIER 399
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
7-394 |
1.34e-113 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 337.25 E-value: 1.34e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSdAAYLARHVGLRVGVPTETGAL 86
Cdd:PRK05656 4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLPHSVPAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFG----LDLKLEDTLWAGLTDQHvklpMG 162
Cdd:PRK05656 83 TLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGhaqlVDSMITDGLWDAFNDYH----MG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 163 MTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQ-TMQVDEHARPQTTLEQLQNLPPVFKK 241
Cdd:PRK05656 159 ITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPlAFATDEQPRAGTTAESLAKLKPAFKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 242 EGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNE 321
Cdd:PRK05656 239 DGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 135762 322 AFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK05656 319 AFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
5-395 |
3.13e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 335.06 E-value: 3.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETG 84
Cdd:PRK08170 3 RPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSP-DEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSP--YSVRNVR----------FGTKFGLDLKLEDTLWA-- 150
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPllFSEKMVRwlagwyaaksIGQKLAALGKLRPSYLApv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 151 -----GLTDQHVKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEeMAPIevKTKKGKQTMQvDEHARP 225
Cdd:PRK08170 162 igllrGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKE-VVPL--FDRDGKFYDH-DDGVRP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 226 QTTLEQLQNLPPVF-KKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGAL 304
Cdd:PRK08170 238 DSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 305 KKAGLSLKDMDLIDVNEAFAPQFLAVQKSLD-----------------LDPSKTNVSGGAIALGHPLGGSGSRITAHLVH 367
Cdd:PRK08170 318 QRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLHLLH 397
|
410 420
....*....|....*....|....*...
gi 135762 368 ELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:PRK08170 398 ALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
4-395 |
2.19e-109 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 326.68 E-value: 2.19e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 4 LRGVFIVAAKRTPFGAYGGllKD-----FTATDLTEFAA---RAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGL 75
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRP--KDpqkdvFNNIRPEELAAmliNRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 76 RVGVPTETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSP-YSVRNVRFGTKFGLDLKLEDTlwagltD 154
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPmGDNPHIEPNPKLLTDPKYIEY------D 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 155 QHVKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQN 234
Cdd:PRK06445 153 LTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 235 LPPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDM 314
Cdd:PRK06445 233 LPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 315 DLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06445 313 DLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLE 392
|
.
gi 135762 395 N 395
Cdd:PRK06445 393 R 393
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
7-266 |
8.15e-109 |
|
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: 320.02 E-value: 8.15e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAyLARHVGLRVGVPTETGAL 86
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQN-PARQAALKAGIPDSAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV-RNVRFGTKFGLDLKLEDTLWAGLTDQHVKLPMGMTA 165
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQNLPPVFKKEGTV 245
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
|
250 260
....*....|....*....|.
gi 135762 246 TAGNASGMSDGAGVVIIASED 266
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
5-394 |
2.19e-107 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 321.14 E-value: 2.19e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 5 RGVFIVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSAG-KVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTE 82
Cdd:PRK08947 2 EDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPHS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 83 TGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSvrnvrFGTKFGLDLKLEDTLWAGLtdqhvklpMG 162
Cdd:PRK08947 82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMN-----HGVDFHPGLSKNVAKAAGM--------MG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 163 MTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKG-KQTMQVDEHARPQTTLEQLQNLPPVFK- 240
Cdd:PRK08947 149 LTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGvLKLFDYDEVIRPETTVEALAALRPAFDp 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 241 KEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVN 320
Cdd:PRK08947 229 VNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELN 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 135762 321 EAFAPQFLAVQKSLDLDPS---KTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK08947 309 EAFAAQSLPCLKDLGLLDKmdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
8-394 |
1.12e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 316.65 E-value: 1.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 8 FIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALT 87
Cdd:PRK07801 5 YIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEVPGVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSvRNVRFGTKFGLDLKL-EDTLW-AGLTDQHVKLPMGmtA 165
Cdd:PRK07801 85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPIS-SAMTAGEQLGFTSPFaESKGWlHRYGDQEVSQFRG--A 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTkkgkqtmqVDEHARpQTTLEQLQNLPPVFKkEGTV 245
Cdd:PRK07801 162 ELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGGVT--------VDEGPR-ETSLEKMAGLKPLVE-GGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 246 TAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAP 325
Cdd:PRK07801 232 TAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAP 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 135762 326 QFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK07801 312 VVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
4-388 |
2.68e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 315.92 E-value: 2.68e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 4 LRGVFIVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTE 82
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 83 TGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKfgldlkledtlwagLTDQHVKLPMG 162
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVRPNPR--------------LVEAAPEYYMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 163 M--TAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEV---------KTKKGKQTMQVDEHARPQTTLEQ 231
Cdd:PRK07661 147 MghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVtlrtvgennKLQEETITFSQDEGVRADTTLEI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 232 LQNLPPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSL 311
Cdd:PRK07661 227 LGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLEL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 135762 312 KDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQG 388
Cdd:PRK07661 307 SDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMG 383
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
5-394 |
5.87e-105 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 315.11 E-value: 5.87e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAyLARHVGLRVGVPTETG 84
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQA-PARQAALGAGLPPSTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFG----LDLKLEDTLWAGLTDQHvklp 160
Cdd:PLN02644 80 CTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGhdtvVDGMLKDGLWDVYNDFG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 161 MGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARP-QTTLEQLQNLPPVF 239
Cdd:PLN02644 156 MGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIVDKDEGLgKFDPAKLRKLRPSF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 240 KKE-GTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLID 318
Cdd:PLN02644 236 KEDgGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 135762 319 VNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PLN02644 316 INEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVE 391
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
7-388 |
1.33e-99 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 303.61 E-value: 1.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 7 VFIVAAKRTPF-GAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGA 85
Cdd:PLN02287 48 VVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 86 LTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNvRFGTKFGLDLKLEDTLwagltdqhvkLPMGMTA 165
Cdd:PLN02287 128 RTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEG-GVNPRVESFSQAQDCL----------LPMGITS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQ------TMQVDEHARPQTTLEQLQNLPPVF 239
Cdd:PLN02287 197 ENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDPKTgeekpiVISVDDGIRPNTTLADLAKLKPVF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 240 KKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDV 319
Cdd:PLN02287 277 KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEI 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 135762 320 NEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRG--GKYAVGSACIGGGQG 388
Cdd:PLN02287 357 NEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMG 427
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
9-394 |
2.87e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 293.45 E-value: 2.87e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 9 IVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSagKVP---PETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETG 84
Cdd:PRK07851 6 IVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALD--KVPaldPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYDFLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 85 AlTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQ-------SPYSVRNVRFGTKFGLDLKLEDTLWAGLTDQH- 156
Cdd:PRK07851 84 T-TVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRfakgnsdSLPDTKNPLFAEAQARTAARAEGGAEAWHDPRe 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 157 ------VKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPieVKTKKGKqTMQVDEHARPQTTLE 230
Cdd:PRK07851 163 dgllpdVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITP--VTLPDGT-VVSTDDGPRAGTTYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 231 QLQNLPPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLS 310
Cdd:PRK07851 240 KVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAGMS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 311 LKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIS 390
Cdd:PRK07851 320 IDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGGGQGMA 399
|
....
gi 135762 391 LIIQ 394
Cdd:PRK07851 400 MVLE 403
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
7-394 |
7.02e-95 |
|
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: 289.15 E-value: 7.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 7 VFIVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSAG-KVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETG 84
Cdd:TIGR02445 2 VVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARNpKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSvrnvrFGTKFGLDLKLEDTLWAGLtdqhvklpMGMT 164
Cdd:TIGR02445 82 AVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMM-----HGVDFHPGMSLHVAKAAGM--------MGLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 165 AENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGK-QTMQVDEHARPQTTLEQLQNLPPVFK-KE 242
Cdd:TIGR02445 149 AEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFlKQFDYDEVIRPETTVESLAALRPAFDpKN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 243 GTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEA 322
Cdd:TIGR02445 229 GTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 135762 323 FAPQFLAVQKSL---DLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:TIGR02445 309 FAAQALPCLKDLgllDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
8-394 |
6.28e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 287.16 E-value: 6.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 8 FIVAAKRTPFG--AYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGA 85
Cdd:PRK08242 5 YIYDAVRTPRGkgKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPETVPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 86 LTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPysvrnvrFGTKFGLdlkledtlWAglTDQHVKL-----P 160
Cdd:PRK08242 85 VQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP-------MGSDGGA--------WA--MDPSTNFptyfvP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 161 MGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPieVKTKKGKQTMQVDEHARPQTTLEQLQNLPPVFK 240
Cdd:PRK08242 148 QGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVP--VKDQNGLTILDHDEHMRPGTTMESLAKLKPSFA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 241 KEGTV---------------------TAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPA 299
Cdd:PRK08242 226 MMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 300 ITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVG 379
Cdd:PRK08242 306 TRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALI 385
|
410
....*....|....*
gi 135762 380 SACIGGGQGISLIIQ 394
Cdd:PRK08242 386 TLCVGGGMGIATIIE 400
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
9-388 |
7.67e-93 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 283.97 E-value: 7.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 9 IVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALT 87
Cdd:PRK07108 6 IVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVTVPGMT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSqspySVRNvrfgtkfGLDLKLEDTLWAGLTDQHVKLPMGMTAEN 167
Cdd:PRK07108 86 VNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIS----CVQN-------EMNRHMLREGWLVEHKPEIYWSMLQTAEN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQ----------TMQVDEHARPQTTLEQLQNLPP 237
Cdd:PRK07108 155 VAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKatgrlftkevTVSADEGIRPDTTLEGVSKIRS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 238 VFKKeGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLI 317
Cdd:PRK07108 235 ALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLW 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 135762 318 DVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQG 388
Cdd:PRK07108 314 ELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQG 384
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
8-394 |
1.50e-91 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 280.85 E-value: 1.50e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 8 FIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALT 87
Cdd:PRK06504 5 YIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPESVPGTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVrNVRFGTKFGLDLKLEDTLWAGLTDqhVKLPMGMTAEN 167
Cdd:PRK06504 85 IDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGS-PSTLPAKNGLGHYKSPGMEERYPG--IQFSQFTGAEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQNLPPVfKKEGTVT 246
Cdd:PRK06504 162 MAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMhTVDEGIRFDATLEGIAGVKLI-AEGGRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 247 AGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQ 326
Cdd:PRK06504 241 AATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 135762 327 FLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06504 321 PLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
4-394 |
1.17e-89 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 275.74 E-value: 1.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 4 LRGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQS---SSDAAYLARHVGLrvgvP 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAgvgQNPAGQAAYHAGL----P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 81 TETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV-RNVRFGTKFGL--DLKLEDTLWA-GLTDQH 156
Cdd:PRK06366 77 FGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPKHLLhkNYKIDDAMLVdGLIDAF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 157 VKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEvktkkgkqTMQVDEHARpQTTLEQLQNLP 236
Cdd:PRK06366 157 YFEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIR-KTTMEDLAKLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 237 PVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDL 316
Cdd:PRK06366 228 PAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 135762 317 IDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06366 308 VEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
7-394 |
1.05e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 271.00 E-value: 1.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAyLARHVGLRVGVPTETGAL 86
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQA-PARQAALGAGLPLSVGCT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGLDLKLEDTLWAGLTDQHVK-LPMGMTA 165
Cdd:PRK06954 88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKgRLMGTFA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARpQTTLEQLQNLPPVFKKEGTV 245
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPF-KANPEKIPTLKPAFSKTGTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 246 TAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAP 325
Cdd:PRK06954 247 TAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 135762 326 QFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06954 327 VTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
9-394 |
1.30e-79 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 249.30 E-value: 1.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 9 IVAAKRTPFGAYGGLLKDFTATDLTEFAARAaLSAGKvpPETIDSVIVGNVMQSSSDaayLARHVGLRVGVPTETGALTL 88
Cdd:PRK06690 5 IVEAKRTPIGKKNGMLKDYEVQQLAAPLLTF-LSKGM--EREIDDVILGNVVGPGGN---VARLSALEAGLGLHIPGVTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 89 NRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRnVRFGTKfgldlkledtlWAGLTDqhvklpMGMTAENL 168
Cdd:PRK06690 79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNR-ARFSPE-----------TIGDPD------MGVAAEYV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 169 AAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEvktkkgkqtMQVDEHARPQTTLEQL-QNLPPVFKKEGTVTA 247
Cdd:PRK06690 141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN---------GLLDESIKKEMNYERIiKRTKPAFLHNGTVTA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 248 GNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQF 327
Cdd:PRK06690 212 GNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKV 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 135762 328 LAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06690 292 VACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
7-394 |
1.13e-77 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 246.05 E-value: 1.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETGAL 86
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMP-EAPNIAREIVLGTGMNVHTDAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV--------RNVRFGTKFGLDLKLEDTLWA-------- 150
Cdd:PRK08963 86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVskklaralVDLNKARTLGQRLKLFSRLRLrdllpvpp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 151 GLTDQHVKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMapIEVKTKKGKQTMQVDEHARPQTTLE 230
Cdd:PRK08963 166 AVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEV--MTAHVPPYKQPLEEDNNIRGDSTLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 231 QLQNLPPVF-KKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAI-MGIGPVPAITGALKKAG 308
Cdd:PRK08963 244 DYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQdMLLGPAYATPLALERAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 309 LSLKDMDLIDVNEAFAPQFLAVQKSL-----------------DLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRR 371
Cdd:PRK08963 324 LTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRR 403
|
410 420
....*....|....*....|...
gi 135762 372 RGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK08963 404 RGGGLGLTTACAAGGLGAAMVLE 426
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
9-394 |
1.83e-75 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 239.24 E-value: 1.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 9 IVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALTL 88
Cdd:PRK07850 6 IVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYHVGATTI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 89 NRLCGSGFQS--IVSGCqeICSKDAEVVLCGGTESMSQSPysvrnvrFGTKFGLDLkleDTLWAGltDQHVKLPMGMT-A 165
Cdd:PRK07850 86 DCQCGSAQQAnhLVAGL--IAAGAIDVGIACGVEAMSRVP-------LGANAGPGR---GLPRPD--SWDIDMPNQFEaA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIE--VKTKKGKQTMQVDEHARPQ----TTLEQLQNLPPVF 239
Cdd:PRK07850 152 ERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapVLDEEGQPTGETRLVTRDQglrdTTMEGLAGLKPVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 240 KkEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDV 319
Cdd:PRK07850 232 E-GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEI 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 135762 320 NEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK07850 311 NEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
8-394 |
4.59e-70 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 226.20 E-value: 4.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 8 FIVAAKRTPFG---AYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETG 84
Cdd:PRK06025 5 YIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYDIKAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSqspYSVRNVRFGTKFGLDLKLEDTLWAGLTDQHVKLPMGMT 164
Cdd:PRK06025 85 GVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMS---YTAAMAAEDMAAGKPPLGMGSGNLRLRALHPQSHQGVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 165 AENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPieVKTKKGKQTMQVDEHARPQTTLEQLQNLPPVFKK--- 241
Cdd:PRK06025 162 GDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVP--VYRDDGSVALDHEEFPRPQTTAEGLAALKPAFTAiad 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 242 ----EGTVT-------------------AGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVP 298
Cdd:PRK06025 240 ypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 299 AITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAV 378
Cdd:PRK06025 320 AAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGL 399
|
410
....*....|....*.
gi 135762 379 GSACIGGGQGISLIIQ 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 |
1.61e-64 |
|
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: 201.72 E-value: 1.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 273 FTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGH 352
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 135762 353 PLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
10-394 |
3.67e-63 |
|
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: 207.73 E-value: 3.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 10 VAAKRTPFGAYGGLLKDFtATDLTEFAARAALSAGKVP----PETIDSVIVGNVMqSSSDAAYLARHVGLRVGVPTETGA 85
Cdd:cd00826 1 AGAAMTAFGKFGGENGAD-ANDLAHEAGAKAIAAALEPagvaAGAVEEACLGQVL-GAGEGQNCAQQAAMHAGGLQEAPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 86 LTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSqspYSVRNVrfgtkfgldlkledtlwagltdqhvklPMGMTA 165
Cdd:cd00826 79 IGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME---TSAENN---------------------------AKEKHI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 166 ENLAAKYNiSREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQT--TLEQLQNLPPVFKKEG 243
Cdd:cd00826 129 DVLINKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGDeaSLDEIAKLRPAFDKED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 244 TVTAGNASGMSDGAGVVIIASEDAVKKHNFT-------PLARVVGYFVSGCDPA----IMGIGPVPAITGALKKAGLSLK 312
Cdd:cd00826 208 FLTAGNACGLNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 313 DMDLIDVNEAFAPQFLAVQKSLDLDP------------------SKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGG 374
Cdd:cd00826 288 DLDLIEAHDAFAANACATNEALGLCPegqggalvdrgdntyggkSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAG 367
|
410 420
....*....|....*....|....*
gi 135762 375 KYAVGSA-----CIGGGQGISLIIQ 394
Cdd:cd00826 368 KRQGAGAglallCIGGGGGAAMCIE 392
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-394 |
6.69e-58 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 194.73 E-value: 6.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 1 MALLRGVFIVAAKRTPFGAYGGLLKD------FTATdLTEFAARAALsAGkvppETIDSVIVGNVMQSSSDAAyLARHVG 74
Cdd:PRK09268 3 MPTVRRVAILGGNRIPFARSNGAYADasnqdmLTAA-LDGLVDRFGL-QG----ERLGEVVAGAVLKHSRDFN-LTRECV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 75 LRVGVPTETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV-RNVRfgtKFGLDLKLEDT------ 147
Cdd:PRK09268 76 LGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVnEGLR---KILLELNRAKTtgdrlk 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 148 LWAGLTDQHVK------------LPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKkgkq 215
Cdd:PRK09268 153 ALGKLRPKHLApeiprngeprtgLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 216 tmqvDEHARPQTTLEQLQNLPPVFKK--EGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGY------FVSGC 287
Cdd:PRK09268 229 ----DNNLRPDSSLEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetaavdFVHGK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 288 DPAIMGigPVPAITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKS------------LD-----LDPSKTNVSGGAIAL 350
Cdd:PRK09268 305 EGLLMA--PAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAwedeeycrerlgLDaplgsIDRSKLNVNGSSLAA 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 135762 351 GHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK09268 383 GHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILE 426
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
15-392 |
2.79e-25 |
|
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: 105.81 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 15 TPFGAYGGLlkdfTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSD---AAYLARHVGLRVGVPTETGALtlnrl 91
Cdd:cd00829 6 TPFGRRSDR----SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQsfpGALIAEYLGLLGKPATRVEAA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 92 CGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVrnvrfgTKFGLDLKLEDTLWAGLTDQHVKLPMGMTAENLAAK 171
Cdd:cd00829 77 GASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGD------EAGGRASDLEWEGPEPPGGLTPPALYALAARRYMHR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 172 YNISREDCDRYALQsQQRWKAANEAGYFNEEMapievktkkgkqtmqvdeharpqtTLEQLQNLPPVFkkeGTVTAGNAS 251
Cdd:cd00829 151 YGTTREDLAKVAVK-NHRNAARNPYAQFRKPI------------------------TVEDVLNSRMIA---DPLRLLDCC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 252 GMSDGAGVVIIASEDAVKKHnFTPLARVVG-------YFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFA 324
Cdd:cd00829 203 PVSDGAAAVVLASEERAREL-TDRPVWILGvgaasdtPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 325 P---------QFLAVQKSLDLDPS---------KTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGG 386
Cdd:cd00829 282 IaellaledlGFCEKGEGGKLVREgdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLA 361
|
....*.
gi 135762 387 QGISLI 392
Cdd:cd00829 362 HNIGGT 367
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
247-393 |
1.87e-21 |
|
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: 92.51 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 247 AGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCD----PAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEA 322
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 323 FAPQFLAVQKSLDLDPSK---TNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKY-------AVGSACIGGGQGISLI 392
Cdd:cd00327 174 GTPIGDAVELALGLDPDGvrsPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtpreprtVLLLGFGLGGTNAAVV 253
|
.
gi 135762 393 I 393
Cdd:cd00327 254 L 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
4-388 |
2.84e-16 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 79.56 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 4 LRGVFIVAAKRTPFGAygglLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNV---MQSSSD--AAYLARHVGLRvG 78
Cdd:PRK06064 1 MRDVAIIGVGQTKFGE----LWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMsagLFVSQEhiAALIADYAGLA-P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 79 VPTetgaltlNRL---CGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVrNVRFGTKFGldlkleDTLWAGLtdq 155
Cdd:PRK06064 76 IPA-------TRVeaaCASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPD-ATEAIARAG------DYEWEEF--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 156 hvklpMGMTAENLAAKynISREDCDRYalqsqqrwkaaneaGYFNEEMAPIEVKTKKgKQTMQVDEHARPQTTLEQLQNL 235
Cdd:PRK06064 139 -----FGATFPGLYAL--IARRYMHKY--------------GTTEEDLALVAVKNHY-NGSKNPYAQFQKEITVEQVLNS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 236 PPVfkkEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPL-----ARVVGYFVSGCDPAIMGIGP-VPAITGALKKAGL 309
Cdd:PRK06064 197 PPV---ADPLKLLDCSPITDGAAAVILASEEKAKEYTDTPVwikasGQASDTIALHDRKDFTTLDAaVVAAEKAYKMAGI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 310 SLKDMDLIDVNEAFA-PQFLAVQkslDLDPSK--------------------TNVSGGAIALGHPLGGSGSRITAHLVHE 368
Cdd:PRK06064 274 EPKDIDVAEVHDCFTiAEILAYE---DLGFAKkgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQ 350
|
410 420
....*....|....*....|....*..
gi 135762 369 LRRR--GGKYAVGSACIG-----GGQG 388
Cdd:PRK06064 351 LRGEaeKGRQQVIGAGYGlthnvGGTG 377
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
31-381 |
7.77e-12 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 66.25 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 31 DLTEFAARAALSAGKVPPETIDSVIVGNVmqsssdAAYLARHVGLRVGVPTE-------TGALTLNRLCGSGFQSIVSGC 103
Cdd:PRK06289 28 DLTREVVDGTLAAAGVDADDIEVVHVGNF------FGELFAGQGHLGAMPATvhpalwgVPASRHEAACASGSVATLAAM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 104 QEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTkfgldlkledTLWAGLTDQHVKLPMGMTAENLAAKYNisredcDRYA 183
Cdd:PRK06289 102 ADLRAGRYDVALVVGVELMKTVPGDVAAEHLGA----------AAWTGHEGQDARFPWPSMFARVADEYD------RRYG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 184 LQSQqRWKAANEAGYFNEEMAPievktkkGKQTMQ---VDEHARPQTTLEqlqnlPPVfkkEGTVTAGNASGMSDGAGVV 260
Cdd:PRK06289 166 LDEE-HLRAIAEINFANARRNP-------NAQTRGwafPDEATNDDDATN-----PVV---EGRLRRQDCSQVTDGGAGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 261 IIASEDAVKKH-NFTPLARVVGYfvsGCDPAIMGIGP-----------VP----AITGALKKAGLSLKDMDLIDVNEAFA 324
Cdd:PRK06289 230 VLASDAYLRDYaDARPIPRIKGW---GHRTAPLGLEQkldrsagdpyvLPhvrqAVLDAYRRAGVGLDDLDGFEVHDCFT 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 135762 325 P-QFLAVQK----------------SLDLDPSK-TNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSA 381
Cdd:PRK06289 307 PsEYLAIDHigltgpgeswkaiengEIAIGGRLpINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGDYQVEGA 381
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
253-358 |
5.96e-10 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 60.57 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 253 MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSgCD------PAIMGIGPVPAITGALKKAGLSLKDMDLI--------- 317
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMT-GDayhmtaPAPDGEGAARAMKLALKDAGINPEDIDYInahgtstpa 308
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 135762 318 -DVNEAfapqfLAVQKSLDLDPSKTNVSGGAIALGHPLGGSG 358
Cdd:PRK07314 309 gDKAET-----QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAG 345
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
253-359 |
1.08e-08 |
|
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: 56.64 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 253 MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSgCD------PAIMGIGPVPAITGALKKAGLSLKDMDLI--------- 317
Cdd:COG0304 229 LGEGAGVLVLEELEHAKARGAKIYAEVVGYGAS-SDayhitaPAPDGEGAARAMRAALKDAGLSPEDIDYInahgtstpl 307
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 135762 318 -DVNEAfapqfLAVQKSLDLDPSKTNVSggAI--ALGHPLGGSGS 359
Cdd:COG0304 308 gDAAET-----KAIKRVFGDHAYKVPVS--STksMTGHLLGAAGA 345
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
253-359 |
2.13e-07 |
|
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: 52.54 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 253 MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSgCD------PAIMGIGPVPAITGALKKAGLSLKDMDLI--------- 317
Cdd:cd00834 229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGAS-SDayhitaPDPDGEGAARAMRAALADAGLSPEDIDYInahgtstpl 307
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 135762 318 -DVNEAfapqfLAVQKSLDLDPSKTNVSG--GAIalGHPLGGSGS 359
Cdd:cd00834 308 nDAAES-----KAIKRVFGEHAKKVPVSStkSMT--GHLLGAAGA 345
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
224-381 |
5.71e-07 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 51.05 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 224 RPQTTLEQLQNLPPVFkkeGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGY-----FVSGCDP--AIMGIG- 295
Cdd:PRK08256 187 RDEYTLEDVLASPMIW---GPLTRLQCCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQamttdTPSTFDGrsMIDLVGy 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 296 --PVPAITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPSK------------------TNVSGGAIALGHPLG 355
Cdd:PRK08256 264 dmTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGeaekfiddgdntyggrwvVNPSGGLLSKGHPLG 343
|
170 180
....*....|....*....|....*.
gi 135762 356 GSGSRITAHLVHELRRRGGKYAVGSA 381
Cdd:PRK08256 344 ATGLAQCAELTWQLRGTAGARQVEGA 369
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
197-379 |
5.37e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 48.21 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 197 GYFNEEMAPIEVKTKKGKQTMQVDEHARPqTTLEQLQNLPPVFKKegtVTAGNASGMSDGAGVVIIASEDAVKKHNFTPL 276
Cdd:PRK06066 158 GITREDLALVVEKNKKAGLSNPRASYASN-ISLEDVLSSEYVVYP---LTELDIAPFVDGAIVVVLASEEVAKKLTDDPV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 277 -ARVVGYFVSGCDPAIMGIGPVP----AITGALKKAGLS--LKDMDLIDVNEAF-------------APQFLAVQ--KSL 334
Cdd:PRK06066 234 wIKGIGWSTESSNLETAELGKANymriAADMAYKMAGIEspRKEVDAAEVDDRYsykelqhiealrlSEEPEKDSllREG 313
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 135762 335 DLDPS---KTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVG 379
Cdd:PRK06066 314 NFDPQgelPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGARQGK 361
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
7-358 |
3.75e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 45.32 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 7 VFIVAAKRTPFGAygglLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNV---MQSSSDAAYLARHV--GLRvGVPt 81
Cdd:PRK07516 4 ASIVGWAHTPFGK----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFnagFSPQDFPASLVLQAdpALR-FKP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 82 etgALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPysvrnvrfGTKFGLDLkledtLWAGLTDQHVKLPM 161
Cdd:PRK07516 78 ---ATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP--------TAEVGDIL-----LGASYLKEEGDTPG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 162 GMTA--ENLAAKYNisredcDRYALQSqqrwkaaneagyfnEEMAPIEVKTKKGK-----QTMQVD---EHARpqttleq 231
Cdd:PRK07516 142 GFAGvfGRIAQAYF------QRYGDQS--------------DALAMIAAKNHANGvanpyAQMRKDlgfEFCR------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 232 lqnlppvfkkegTVTAGN-----------ASGMSDGAGVVIIASED----AVKKHNFTPLARVVGYF-VSGCDPAIMGiG 295
Cdd:PRK07516 195 ------------TVSEKNplvagplrrtdCSLVSDGAAALVLADAEtaraLQRAVRFRARAHVNDFLpLSRRDPLAFE-G 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 296 PVPAITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPS------------------KTNVSGGAIALGHPLGGS 357
Cdd:PRK07516 262 PRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGAT 341
|
.
gi 135762 358 G 358
Cdd:PRK07516 342 G 342
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
253-358 |
1.69e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 43.45 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 253 MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSgCD------PAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAP- 325
Cdd:PRK06333 242 MGEGAGILVIETLEHALARGAPPLAELVGYGTS-ADayhmtaGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPv 320
|
90 100 110
....*....|....*....|....*....|....*..
gi 135762 326 ----QFLAVqKSLDLDPSKTNVSGGAIALGHPLGGSG 358
Cdd:PRK06333 321 gdlgEVAAI-KKVFGHVSGLAVSSTKSATGHLLGAAG 356
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
25-124 |
3.00e-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: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 25 KDFTATDLTEFAARAALSAGKVPPETIDSVIVGNV---MQSSSDAAYLARHVGLRvgvptETGALTLNRLCgSGF-QSIV 100
Cdd:COG0332 47 PDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVtpdYLFPSTACLVQHKLGAK-----NAAAFDINAAC-SGFvYALS 120
|
90 100
....*....|....*....|....
gi 135762 101 SGCQEICSKDAEVVLCGGTESMSQ 124
Cdd:COG0332 121 VAAALIRSGQAKNVLVVGAETLSR 144
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
251-395 |
5.58e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 41.80 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 251 SGMSDGAGVVIIASEDAVKKHNFTP----------LARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVN 320
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsrlveiksLACASGNLYEDPPDATRMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 321 EAFAPQFLAVQKSLDL-DPSKT-----------------NVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKY------ 376
Cdd:PTZ00455 336 DCFTIAELLMYEALGIaEYGHAkdlirngatalegripvNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYqmknip 415
|
170 180
....*....|....*....|..
gi 135762 377 AVGSACIGGGQ---GISLIIQN 395
Cdd:PTZ00455 416 ALGATLNMGGDdktAVSTVLQN 437
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
246-366 |
4.36e-03 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 38.96 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 246 TAGNASG--MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGcDPAIMGI-----GPVPAITGALKKAGLSLKDMDLI- 317
Cdd:cd00828 220 FDETRDGfvEAEGAGVLVLERAELALARGAPIYGRVAGTASTT-DGAGRSVpaggkGIARAIRTALAKAGLSLDDLDVIs 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 318 ---------DVNEAFApqFLAVQKSLDLDPSKTNVSGGaiaLGHPLGGSG--SRITAHLV 366
Cdd:cd00828 299 ahgtstpanDVAESRA--IAEVAGALGAPLPVTAQKAL---FGHSKGAAGalQLIGALQS 353
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
253-359 |
6.88e-03 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 38.52 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 253 MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSgCD------PAIMGIGPVPAITGALKKAG-LSLKDMDLIDVNEAFAP 325
Cdd:PTZ00050 237 MGEGAGILVLEELEHALRRGAKIYAEIRGYGSS-SDahhitaPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTP 315
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 135762 326 -----QFLAVQKSL-DLDPSKTNVSGGAIALGHPLGGSGS 359
Cdd:PTZ00050 316 igdkiELKAIKKVFgDSGAPKLYVSSTKGGLGHLLGAAGA 355
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
255-370 |
7.22e-03 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 38.00 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135762 255 DGAGVVIIASEDAVKKHNFTPLARVVGYfVSGCDPAIMGI------GPVPAITGALKKAGLSLKDMDLIDVNEAFAPQFL 328
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGT-AATIDGAGMGAfapsaeGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 135762 329 AVQKSLDLD---PSKTNVSGGAIALGHPLGGSGSRITAHLVHELR 370
Cdd:cd00825 240 VKELKLLRSefgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
|
|
| |
