|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
1-268 |
1.68e-153 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 435.73 E-value: 1.68e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 1 MSLSGMGNPGNISSRLLESEKARDCLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVLD 80
Cdd:PLN02287 164 MTTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVD 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 81 DK-GDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVG 159
Cdd:PLN02287 244 PKtGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVG 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 160 VPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLL 239
Cdd:PLN02287 324 VDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLL 403
|
250 260 270
....*....|....*....|....*....|
gi 1274095745 240 NELKRRGRRA-YGVVSMCIGTGMGAAAVFE 268
Cdd:PLN02287 404 HEMKRRGKDCrFGVVSMCIGTGMGAAAVFE 433
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
1-269 |
1.93e-143 |
|
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: 407.64 E-value: 1.93e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 1 MSLSGMGNPGNISSRLLESEK----------ARDCLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAE 70
Cdd:cd00751 114 MSRAPYLLPKARRGGRLGLNTldgmlddgltDPFTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 71 IVPVTTtvlddKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILG 150
Cdd:cd00751 194 IVPVEV-----PGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 151 VLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCT 230
Cdd:cd00751 269 RIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGAS 348
|
250 260 270
....*....|....*....|....*....|....*....
gi 1274095745 231 GARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFEY 269
Cdd:cd00751 349 GARIVVTLLHELKRRGGR-YGLATMCIGGGQGAAMVIER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
28-268 |
5.97e-135 |
|
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: 386.34 E-value: 5.97e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 28 PMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTtvlddKGDKKTITVSQDEGVRPSTTMQGLAK 107
Cdd:COG0183 155 SMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEV-----PDRKGEVVVDRDEGPRPDTTLEKLAK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 108 LKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDI 187
Cdd:COG0183 230 LKPAFKKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 188 DIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVF 267
Cdd:COG0183 310 DLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGR-YGLATMCIGGGQGIALII 388
|
.
gi 1274095745 268 E 268
Cdd:COG0183 389 E 389
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
1-268 |
9.30e-127 |
|
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: 365.40 E-value: 9.30e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 1 MSLSGMGNPGNISSRLLESEKARD--CLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttv 78
Cdd:TIGR01930 122 RSLRWGVKPGNAELEDARLKDLTDanTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVT--- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 79 ldDKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVV 158
Cdd:TIGR01930 199 --VKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 159 GVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTL 238
Cdd:TIGR01930 277 GVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTL 356
|
250 260 270
....*....|....*....|....*....|
gi 1274095745 239 LNELKRRGRRaYGVVSMCIGTGMGAAAVFE 268
Cdd:TIGR01930 357 LHELKRRGGR-YGLATMCIGGGQGAAVILE 385
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
28-270 |
3.15e-120 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 349.07 E-value: 3.15e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 28 PMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttVLDDKGDkkTITVSQDEGVRPSTTMQGLAK 107
Cdd:PRK05790 156 HMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVT--IKQRKGD--PVVVDTDEHPRPDTTAESLAK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 108 LKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDI 187
Cdd:PRK05790 232 LRPAFDKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 188 DIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVF 267
Cdd:PRK05790 312 DLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAK-KGLATLCIGGGQGVALIV 390
|
...
gi 1274095745 268 EYP 270
Cdd:PRK05790 391 ERP 393
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
29-268 |
1.68e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 324.40 E-value: 1.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVL----DDKGDKKTITVSQDEGVRPSTTMQG 104
Cdd:PRK07661 147 MGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRtvgeNNKLQEETITFSQDEGVRADTTLEI 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 105 LAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTV 184
Cdd:PRK07661 227 LGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLEL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 185 NDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAA 264
Cdd:PRK07661 307 SDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQ-FGIVTMCIGGGMGAA 385
|
....
gi 1274095745 265 AVFE 268
Cdd:PRK07661 386 GVFE 389
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
6-268 |
7.21e-106 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 312.71 E-value: 7.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 6 MGNPGNISSRLLESEKARDCLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVP--VTTTVLDDKG 83
Cdd:PRK09052 131 MGNKPSMSPAIFARDENVGIAYGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPyeITERFPDLAT 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 84 ---DKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGV 160
Cdd:PRK09052 211 gevDVKTRTVDLDEGPRADTSLEGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 161 PPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLN 240
Cdd:PRK09052 291 PPEIMGIGPIEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVH 370
|
250 260
....*....|....*....|....*...
gi 1274095745 241 ELKRRGRRaYGVVSMCIGTGMGAAAVFE 268
Cdd:PRK09052 371 GLRRTNLK-YGMVTMCVGTGMGAAGIFE 397
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
28-268 |
5.63e-95 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 284.93 E-value: 5.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 28 PMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTtvlddKGDKKTITVSQDEGVRPSTTMQGLAK 107
Cdd:PRK09051 157 HMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEI-----KTRKGEVVFDTDEHVRADTTLEDLAK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 108 LKPAF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVND 186
Cdd:PRK09051 232 LKPVFkKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVAD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 187 IDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAV 266
Cdd:PRK09051 312 LDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGR-YALVTMCIGGGQGIAAI 390
|
..
gi 1274095745 267 FE 268
Cdd:PRK09051 391 FE 392
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
29-268 |
1.90e-93 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 281.07 E-value: 1.90e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVttTVLDDKGDkkTITVSQDEGVRPSTTMQGLAKL 108
Cdd:PRK09050 163 MPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPV--TIPQKKGD--PVVVDRDEHPRPETTLEALAKL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGL-PILGVLrSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDI 187
Cdd:PRK09050 239 KPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLtPRARIL-GMATAGVEPRIMGIGPAPATRKLLARLGLTIDQF 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 188 DIFEINEAFASQAVYCVEKLGIP--AEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAA 265
Cdd:PRK09050 318 DVIELNEAFAAQGLAVLRQLGLAddDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGR-YALCTMCIGVGQGIAL 396
|
...
gi 1274095745 266 VFE 268
Cdd:PRK09050 397 AIE 399
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
28-268 |
2.96e-92 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 277.81 E-value: 2.96e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 28 PMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTV-LDDKGD----KKTITVSQDEGVRPSTTM 102
Cdd:PRK07108 147 SMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAgVADKATgrlfTKEVTVSADEGIRPDTTL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 103 QGLAKLKPAFKdGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGL 182
Cdd:PRK07108 227 EGVSKIRSALP-GGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 183 TVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMG 262
Cdd:PRK07108 306 KVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAK-YVVVTMCIGGGQG 384
|
....*.
gi 1274095745 263 AAAVFE 268
Cdd:PRK07108 385 AAGLFE 390
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
29-268 |
1.79e-89 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 270.30 E-value: 1.79e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTvlDDKGDKKTITVsqDEGVRPSTTMQGLAKL 108
Cdd:PRK08947 147 MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGH--DADGVLKLFDY--DEVIRPETTVEALAAL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAFKD-GGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDI 187
Cdd:PRK08947 223 RPAFDPvNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDI 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 188 DIFEINEAFASQAVYCVEKLGI---PAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAA 264
Cdd:PRK08947 303 DVFELNEAFAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQ-FGLATMCIGLGQGIA 381
|
....
gi 1274095745 265 AVFE 268
Cdd:PRK08947 382 TVFE 385
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
28-268 |
2.59e-88 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 268.01 E-value: 2.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 28 PMGM--TSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttVLDDKGDkkTITVSQDEGVRPSTTMQGL 105
Cdd:PRK06205 158 PGGMieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVT--VPQRKGD--PTVVDRDEHPRADTTLESL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 106 AKLKP--AFKDGGST-TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGL 182
Cdd:PRK06205 234 AKLRPimGKQDPEATvTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 183 TVNDIDIFEINEAFASQAVYCVEKLGIPA---EKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGT 259
Cdd:PRK06205 314 TLDDIDLIELNEAFAAQVLAVLKEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQAR-YGLETMCIGG 392
|
....*....
gi 1274095745 260 GMGAAAVFE 268
Cdd:PRK06205 393 GQGLAAVFE 401
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
29-268 |
3.03e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 257.34 E-value: 3.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVlddkgDKKTITVSQDEGVRPSTTMQGLAKL 108
Cdd:PRK06445 159 MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEV-----EGKKKVVDVDQSVRPDTSLEKLAKL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDID 188
Cdd:PRK06445 234 PPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDID 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 189 IFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 268
Cdd:PRK06445 314 LWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKD-YGVATLCVGGGQGGAVVLE 392
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
24-268 |
2.65e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 247.61 E-value: 2.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 24 DCLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTT---TVlddkgdkktitVSQDEGVRPST 100
Cdd:PRK07851 168 DVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLpdgTV-----------VSTDDGPRAGT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 101 TMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKA 180
Cdd:PRK07851 237 TYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 181 GLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTG 260
Cdd:PRK07851 317 GMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKT-FGLETMCVGGG 395
|
....*...
gi 1274095745 261 MGAAAVFE 268
Cdd:PRK07851 396 QGMAMVLE 403
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
29-270 |
6.64e-77 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 238.46 E-value: 6.64e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttVLDDKGDkkTITVSQDEGVRPSTTMQGLAKL 108
Cdd:PRK08235 157 MGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVT--IPQRKGD--PIVVAKDEAPRKDTTIEKLAKL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDID 188
Cdd:PRK08235 233 KPVFDKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDID 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 189 IFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGrRAYGVVSMCIGTGMGAAAVFE 268
Cdd:PRK08235 313 LFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRG-GGIGIAAICSGGGQGDAVLIE 391
|
..
gi 1274095745 269 YP 270
Cdd:PRK08235 392 VH 393
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
29-268 |
9.34e-77 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 238.52 E-value: 9.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttvLDDKGDKKTITVSQDEGVRPSTTMQGLAKL 108
Cdd:PRK08131 162 MPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIE---VPQGRKLPPKLVAEDEHPRPSSTVEALTKL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAFkDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDID 188
Cdd:PRK08131 239 KPLF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMD 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 189 IFEINEAFASQAVYCVEKLGIPAE--KVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAV 266
Cdd:PRK08131 318 IIEINEAFASQVLGCLKGLGVDFDdpRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKR-YAVVSLCIGVGQGLAMV 396
|
..
gi 1274095745 267 FE 268
Cdd:PRK08131 397 IE 398
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
29-270 |
1.22e-74 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 232.86 E-value: 1.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttVLDDKGDKktITVSQDEGVRPSTTMQGLAKL 108
Cdd:PRK05656 157 MGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIL--IPQRKGEP--LAFATDEQPRAGTTAESLAKL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDID 188
Cdd:PRK05656 233 KPAFKKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 189 IFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAyGVVSMCIGTGMGAAAVFE 268
Cdd:PRK05656 313 LIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKK-GLATLCIGGGQGVALAIE 391
|
..
gi 1274095745 269 YP 270
Cdd:PRK05656 392 RD 393
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
26-268 |
1.80e-74 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 232.47 E-value: 1.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 26 LTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTT----TVLDdkgdkktitvsQDEGVRPSTT 101
Cdd:PRK08242 145 FVPQGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDqnglTILD-----------HDEHMRPGTT 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 102 MQGLAKLKPAFKDGGST---------------------TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGV 160
Cdd:PRK08242 214 MESLAKLKPSFAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGS 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 161 PPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLN 240
Cdd:PRK08242 294 DPTIMLTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLD 373
|
250 260
....*....|....*....|....*...
gi 1274095745 241 ELKRRGRRaYGVVSMCIGTGMGAAAVFE 268
Cdd:PRK08242 374 ELERRGKR-TALITLCVGGGMGIATIIE 400
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
29-268 |
3.57e-74 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 231.46 E-value: 3.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVlddkgDKKTITVSQDEGVRPSTTMQGLAKL 108
Cdd:PRK06633 157 MGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTI-----KKTTSLFDHDETVRPDTSLEILSKL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDID 188
Cdd:PRK06633 232 RPAFDKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 189 IFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELkRRGRRAYGVVSMCIGTGMGAAAVFE 268
Cdd:PRK06633 312 VIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGL-RRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
28-268 |
9.93e-74 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 230.36 E-value: 9.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 28 PMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttVLDDKGDKKTItVSQDEGVRpSTTMQGLAK 107
Cdd:PLN02644 155 GMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVE--VPGGRGRPSVI-VDKDEGLG-KFDPAKLRK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 108 LKPAFK-DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVND 186
Cdd:PLN02644 231 LRPSFKeDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 187 IDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAV 266
Cdd:PLN02644 311 VDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGK-YGVAGICNGGGGASAIV 389
|
..
gi 1274095745 267 FE 268
Cdd:PLN02644 390 VE 391
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
29-268 |
2.96e-73 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 230.29 E-value: 2.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGcFRAEIVPVtttvLDDKGDkktiTVSQDEGVRPSTTMQGLAKL 108
Cdd:PRK08170 177 MGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEG-RLKEVVPL----FDRDGK----FYDHDDGVRPDSSMEKLAKL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDI 187
Cdd:PRK08170 248 KPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 188 DIFEINEAFASQAV----------YCVEKLGIPA-------EKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaY 250
Cdd:PRK08170 328 DLWEINEAFAAQVLaclaawadeeYCREQLGLDGalgeldrERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGTK-R 406
|
250
....*....|....*...
gi 1274095745 251 GVVSMCIGTGMGAAAVFE 268
Cdd:PRK08170 407 GIAAICIGGGQGGAMLLE 424
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
29-268 |
1.51e-70 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 223.32 E-value: 1.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEivpVTTTVLDDKGDkktiTVSQDEGVRPSTTMQGLAKL 108
Cdd:PRK08963 176 MGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDE---VMTAHVPPYKQ----PLEEDNNIRGDSTLEDYAKL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPP-DVMGIGPAYAIPAALQKAGLTVND 186
Cdd:PRK08963 249 RPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLALERAGLTLAD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 187 IDIFEINEAFASQAV----------YCVEKLG-------IPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGrRA 249
Cdd:PRK08963 329 LTLIDMHEAFAAQTLanlqmfaserFAREKLGrsqaigeVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRRG-GG 407
|
250
....*....|....*....
gi 1274095745 250 YGVVSMCIGTGMGAAAVFE 268
Cdd:PRK08963 408 LGLTTACAAGGLGAAMVLE 426
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
33-268 |
3.37e-69 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 218.44 E-value: 3.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 33 SENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVLDDKGDK--KTITVSQDEGVRpSTTMQGLAKLKP 110
Cdd:PRK07850 151 AERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEGQPtgETRLVTRDQGLR-DTTMEGLAGLKP 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 111 AFkDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIF 190
Cdd:PRK07850 230 VL-EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLV 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095745 191 EINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 268
Cdd:PRK07850 309 EINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKS-TALITMCAGGALSTGTIIE 385
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
146-269 |
6.88e-68 |
|
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: 206.34 E-value: 6.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 146 LPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGH 225
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1274095745 226 PLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFEY 269
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGK-YGLASLCIGGGQGVAMIIER 123
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
33-268 |
1.40e-61 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 198.78 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 33 SENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVtttvlddkGDkktitVSQDEGVRpSTTMQGLAKLKPaF 112
Cdd:PRK07801 161 AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV--------GG-----VTVDEGPR-ETSLEKMAGLKP-L 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 113 KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEI 192
Cdd:PRK07801 226 VEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEI 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095745 193 NEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 268
Cdd:PRK07801 306 NEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGR-YGLQTMCEGGGTANVTIIE 380
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
29-268 |
3.93e-61 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 196.91 E-value: 3.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTtvLDDKGDKKTitvsqdegvRPSTTMqgLAKL 108
Cdd:PRK06690 133 MGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNG--LLDESIKKE---------MNYERI--IKRT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGL-PILGVLRSyAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDI 187
Cdd:PRK06690 200 KPAFLHNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 188 DIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVF 267
Cdd:PRK06690 279 DYFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMK-YGIATLGIGGGIGLALLF 357
|
.
gi 1274095745 268 E 268
Cdd:PRK06690 358 E 358
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
19-268 |
1.75e-58 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 191.91 E-value: 1.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 19 SEKARDCLTPMGMTSEN------------------VAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVtttvLD 80
Cdd:PRK06025 130 AEDMAAGKPPLGMGSGNlrlralhpqshqgvcgdaIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV----YR 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 81 DKGdkkTITVSQDEGVRPSTTMQGLAKLKPAFK--------DGGST------------------TAGNSSQVSDGAAAVL 134
Cdd:PRK06025 206 DDG---SVALDHEEFPRPQTTAEGLAALKPAFTaiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 135 LARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKV 214
Cdd:PRK06025 283 LASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKV 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1274095745 215 NPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 268
Cdd:PRK06025 363 NVNGGAIALGHPIGATGSILIGTVLDELERRGLK-RGLVTMCAAGGMAPAIIIE 415
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
31-268 |
6.85e-58 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 189.55 E-value: 6.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 31 MTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVLDDKGDKKTItvsqDEGVRPSTTMQGLAKLKP 110
Cdd:PRK06504 157 TGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTV----DEGIRFDATLEGIAGVKL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 111 aFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIF 190
Cdd:PRK06504 233 -IAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLY 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095745 191 EINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 268
Cdd:PRK06504 312 EVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKR-YGLQTMCEGGGMANVTIVE 388
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
29-268 |
1.29e-54 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 182.02 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVtttvlddKGdkktitVSQDEGVRPSTTMQGLAKL 108
Cdd:PRK09268 178 MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-------LG------LTRDNNLRPDSSLEKLAKL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAF--KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVP----PDVMGIGPAYAIPAALQKAGL 182
Cdd:PRK09268 245 KPVFgkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhgKEGLLMAPAYAVPRLLARNGL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 183 TVNDIDIFEINEAFASQ----------AVYCVEKLGIPA-------EKVNPLGGAIALGHPLGCTGARQVVTLLNELKRR 245
Cdd:PRK09268 325 TLQDFDFYEIHEAFASQvlatlkawedEEYCRERLGLDAplgsidrSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEK 404
|
250 260
....*....|....*....|...
gi 1274095745 246 GrRAYGVVSMCIGTGMGAAAVFE 268
Cdd:PRK09268 405 G-SGRGLISICAAGGQGVTAILE 426
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
20-268 |
2.19e-51 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 172.77 E-value: 2.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 20 EKARDCLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTvlddkGDKKTITVSQDEGVRpS 99
Cdd:PRK06954 154 EDAYDKGRLMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVA-----GKKGDTVIDRDEQPF-K 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 100 TTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQK 179
Cdd:PRK06954 228 ANPEKIPTLKPAFSKTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 180 AGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAyGVVSMCIGT 259
Cdd:PRK06954 308 NGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKR-GVASLCIGG 386
|
....*....
gi 1274095745 260 GMGAAAVFE 268
Cdd:PRK06954 387 GEATAMGIE 395
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
1-139 |
3.73e-48 |
|
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: 160.55 E-value: 3.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 1 MSLSGMGNPGN-ISSRLLESEKARDCLTP-----------MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFR 68
Cdd:pfam00108 115 MSHAPYALPTDaRSGLKHGDEKKHDLLIPdgltdafngyhMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFK 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095745 69 AEIVPVTTTVLDDKGdkktiTVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRS 139
Cdd:pfam00108 195 DEIVPVTVKGRKGKP-----TVDKDEGIRPPTTAEPLAKLKPAFDKEGTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
29-268 |
3.72e-47 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 161.72 E-value: 3.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTtvlddkgdkktitVSQDEGVRpSTTMQGLAKL 108
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND-------------LDRDEGIR-KTTMEDLAKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 109 KPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDID 188
Cdd:PRK06366 227 PPAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 189 IFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAyGVVSMCIGTGMGAAAVFE 268
Cdd:PRK06366 307 LVEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKT-GLATLCHGGGGAHTLTLE 385
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
29-269 |
1.25e-42 |
|
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: 149.95 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 29 MGMTSENVAERFGI--------SRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTtvlddKGDKKTITVSQDEGVR--P 98
Cdd:cd00826 115 METSAENNAKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGV-----KGRKGDIHSDADEYIQfgD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 99 STTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPI-------LGVLRSYAVVGVPPD----VMGI 167
Cdd:cd00826 190 EASLDEIAKLRPAFDKEDFLTAGNACGLNDGAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGD 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 168 GPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEK------------------VNPLGGAIALGHPLGC 229
Cdd:cd00826 270 GPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGA 349
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1274095745 230 TGARQVVTLLNELKRRGRRAY----GVVSMCIGTGMGAAAVFEY 269
Cdd:cd00826 350 SGAAICAELCFELKGEAGKRQgagaGLALLCIGGGGGAAMCIES 393
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
120-266 |
1.06e-17 |
|
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: 80.18 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 120 AGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPD----VMGIGPAYAIPAALQKAGLTVNDIDIFEINEA 195
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 196 FASQAVYCVEKLGIPAEKVNPL---GGAIALGHPLGCTGARQVVTLLNELKRRGRRAY------GVVSMCIGTGMGAAAV 266
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVRSPavsATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTpreprtVLLLGFGLGGTNAAVV 253
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
124-266 |
7.76e-15 |
|
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: 73.45 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 124 SQVSDGAAAVLLARRSKAEELGLP---ILGV---LRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFA 197
Cdd:cd00829 202 CPVSDGAAAVVLASEERARELTDRpvwILGVgaaSDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFT 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 198 SQAVYCVEKLGIpAEK-------------------VNPLGGAIALGHPLGCTGARQVVTLLNELKRRGrRAYGV----VS 254
Cdd:cd00829 282 IAELLALEDLGF-CEKgeggklvregdtaiggdlpVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEA-GARQVpgarVG 359
|
170
....*....|..
gi 1274095745 255 MCIGTGMGAAAV 266
Cdd:cd00829 360 LAHNIGGTGSAA 371
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
123-265 |
2.00e-14 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 72.24 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 123 SSQVSDGAAAVLLARRSKAEELGLPILGVLRS-----YAVVGVPPDVMGIGPA-YAIPAALQKAGLTVNDIDIFEINEAF 196
Cdd:PRK06064 208 CSPITDGAAAVILASEEKAKEYTDTPVWIKASgqasdTIALHDRKDFTTLDAAvVAAEKAYKMAGIEPKDIDVAEVHDCF 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 197 ASQAVYCVEKLGIpAEK-------------------VNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVsmcI 257
Cdd:PRK06064 288 TIAEILAYEDLGF-AKKgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAEKGRQQV---I 363
|
....*...
gi 1274095745 258 GTGMGAAA 265
Cdd:PRK06064 364 GAGYGLTH 371
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
124-233 |
7.79e-10 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 58.55 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 124 SQVSDGAAAVLLARRSKAEELG----LP-ILGVLRSYAVVGVPPDV-MGIGPAYAIPA-------ALQKAGLTVNDIDIF 190
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDYAdarpIPrIKGWGHRTAPLGLEQKLdRSAGDPYVLPHvrqavldAYRRAGVGLDDLDGF 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095745 191 EINEAFASQAVYCVEKLGI--PAEK----------------VNPLGGAIALGHPLGCTGAR 233
Cdd:PRK06289 300 EVHDCFTPSEYLAIDHIGLtgPGESwkaiengeiaiggrlpINPSGGLIGGGHPVGASGVR 360
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
124-243 |
6.02e-09 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 56.05 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 124 SQVSDGAAAVLLARRSKAEELGL-----PILGVLRSYAVVGV----PPDVMGIGPAY-AIPAALQKAGLTVNDIDIFEIN 193
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLspndsRLVEIKSLACASGNlyedPPDATRMFTSRaAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095745 194 EAFASQAVYCVEKLGIpAE-------------------KVNPLGGAIALGHPLGCTGARQVVTLLNELK 243
Cdd:PTZ00455 336 DCFTIAELLMYEALGI-AEyghakdlirngatalegriPVNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
122-243 |
2.32e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 54.08 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 122 NSSQVSDGAAAVLLARRSKAEELGL--PI----LGVLRSYAVVGVPPDVMGIGPAY-AIPAALQKAGLTVNDIDIFEINE 194
Cdd:PRK12578 205 DSCPISDGSATAIFASEEKVKELKIdsPVwitgIGYANDYAYVARRGEWVGFKATQlAARQAYNMAKVTPNDIEVATVHD 284
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095745 195 AFASQAVYCVEKLGIpAEK-------------------VNPLGGAIALGHPLGCTGARQVVTLLNELK 243
Cdd:PRK12578 285 AFTIAEIMGYEDLGF-TEKgkggkfieegqsekggkvgVNLFGGLKAKGHPLGATGLSMIYEITKQLR 351
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
124-269 |
3.96e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 53.41 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 124 SQVSDGAAAVLLARRSKAEELGLPIlgVLRSYAVVGvppDVMGI---------GPAYAIPAALQKAGLTVNDIDIFEINE 194
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALQRAV--RFRARAHVN---DFLPLsrrdplafeGPRRAWQRALAQAGVTLDDLSFVETHD 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 195 AFASQAVYCVEKLGIPAE------------------KVNPLGGAIALGHPLGCTG-------ARQVVTLLNELKRRGRRA 249
Cdd:PRK07516 288 CFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPGAKL 367
|
170 180
....*....|....*....|
gi 1274095745 250 YGVVSmcigtgMGAAAVFEY 269
Cdd:PRK07516 368 AGVFN------MGGAAVANY 381
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
176-251 |
1.57e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 48.75 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 176 ALQKAGLT--VNDIDIFEINEAFASQAVYCVEKLGI--------------PAEK----VNPLGGAIALGHPLGCTGARQV 235
Cdd:PRK06365 302 AYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgkPELPgklpVNPSGGLLAAGHAVGATGIMQA 381
|
90
....*....|....*.
gi 1274095745 236 VTLLNELKRRGRRAYG 251
Cdd:PRK06365 382 VFMFWQLQGRIKKHFH 397
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
177-269 |
6.14e-06 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 43.64 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 177 LQKAGLTVNDIDIFEINEA--FASQAVycVEKLGIPAEKVnplggAIALGHpLGCTGARQVVTLLNELKRRGRRAYGVVS 254
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQAnlRIIDAV--AKRLGLPPEKV-----VVNLDE-YGNTSAASIPLALDEAVEEGKLKPGDLV 72
|
90
....*....|....*...
gi 1274095745 255 MCIGTGMG---AAAVFEY 269
Cdd:pfam08541 73 LLVGFGAGltwGAALLRW 90
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
127-191 |
6.55e-06 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 46.78 E-value: 6.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095745 127 SDGAAAVLLARRSKAEELGLPILGVLRSYAV-------VGVPPDvmGIGPAYAIPAALQKAGLTVNDIDIFE 191
Cdd:cd00833 234 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVnqdgrtkGITAPS--GEAQAALIRRAYARAGVDPSDIDYVE 303
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
127-234 |
2.86e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 44.89 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 127 SDGAAAVLLARRSKAEELGLPilgvlRSYAVVGV-----------PPDVMG-IGPAYAIPAALQ---KAGLTVNDIDIFE 191
Cdd:PRK08256 214 TCGAAAAIVCSEEFARKHGLD-----RAVEIVAQamttdtpstfdGRSMIDlVGYDMTRAAAQQvyeQAGIGPEDIDVVE 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095745 192 INEAFASQAVYCVEKLGI----PAEK--------------VNPLGGAIALGHPLGCTGARQ 234
Cdd:PRK08256 289 LHDCFSANELLTYEALGLcpegEAEKfiddgdntyggrwvVNPSGGLLSKGHPLGATGLAQ 349
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
126-231 |
3.03e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 44.68 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 126 VSDGAAAVLLARRSKAEEL--------GL------PILGVlRSYAVVgvppdvmgigPAYAIpAALQKAGLTVNDIDIFE 191
Cdd:PRK07937 204 ITDGAAAVVLAAGDRARELrerpawitGIehriesPSLGA-RDLTRS----------PSTAL-AAEAATGGDAGGVDVAE 271
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1274095745 192 INEAFASQAVYCVEKLGIPAE-KVNPLGGAIAlGHPLGCTG 231
Cdd:PRK07937 272 LHAPFTHQELILREALGLGDKtKVNPSGGALA-ANPMFAAG 311
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
127-269 |
3.23e-05 |
|
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: 44.33 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 127 SDGAAAVLLarrsKAEELGLPILG-VLRSYA-----------VVGVPPDVMGIGPAY------------------AIPAA 176
Cdd:COG0332 158 GDGAGAVVL----EASEEGPGILGsVLGSDGsgadllvvpagGSRNPPSPVDEGDHYlrmdgrevfkfavrnlpeVIREA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 177 LQKAGLTVNDIDIF-------EINEAFAsqavycvEKLGIPAEKVnplggaIALGHPLGCTGARQVVTLLNELKRRGRRA 249
Cdd:COG0332 234 LEKAGLTLDDIDWFiphqanlRIIEAVA-------KRLGLPEEKV------VVNIDRYGNTSAASIPLALDEALREGRIK 300
|
170 180
....*....|....*....|...
gi 1274095745 250 YGVVSMCIGTGMG---AAAVFEY 269
Cdd:COG0332 301 PGDLVLLAGFGAGltwGAAVLRW 323
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
127-245 |
3.60e-05 |
|
"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: 44.74 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 127 SDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPD----VMGIGPAYAIPAALQKAGLTVNDIDIfeINEAFASQAVY 202
Cdd:cd00828 230 AEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGrsvpAGGKGIARAIRTALAKAGLSLDDLDV--ISAHGTSTPAN 307
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1274095745 203 CVEKLGIPAEKVNPLGGAIAL-------GHPLGCTGARQVVTLLNELKRR 245
Cdd:cd00828 308 DVAESRAIAEVAGALGAPLPVtaqkalfGHSKGAAGALQLIGALQSLEHG 357
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
127-232 |
1.28e-04 |
|
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: 42.91 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 127 SDGAAAVLLARRSKAEELGLPILGVLRSYAVVG-----VPPDVMGIGPAYAIPAALQKAGLTVNDIDIfeIN-------- 193
Cdd:cd00834 230 GEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDY--INahgtstpl 307
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1274095745 194 ----EAFASQAVYCVEKLGIPaekVNPLGGAIalGHPLGCTGA 232
Cdd:cd00834 308 ndaaESKAIKRVFGEHAKKVP---VSSTKSMT--GHLLGAAGA 345
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
127-188 |
3.53e-04 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 41.62 E-value: 3.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095745 127 SDGAAAVLLARRSKAEELGLPILGVLRSYA-------VVGVPPDvmGIGPAYAIPAALQKAGLTVNDID 188
Cdd:COG0304 230 GEGAGVLVLEELEHAKARGAKIYAEVVGYGassdayhITAPAPD--GEGAARAMRAALKDAGLSPEDID 296
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
126-208 |
5.99e-04 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 40.78 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 126 VSDGAAAVLLARRSKAEELGLPILGVLRSYAVV-----GVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQA 200
Cdd:PRK06158 208 VTDGAGAVVMVRADRARDLPRPPVYVLGAAAATwhrqiSSMPDLTVTAAAESGPRAFAMAGLTPADIDVVELYDAFTINT 287
|
....*...
gi 1274095745 201 VYCVEKLG 208
Cdd:PRK06158 288 ILFLEDLG 295
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
128-239 |
2.25e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 38.94 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 128 DGAAAVLLARRSKAEELGLPILGVLRSYAVVG-----VPPDVMGIGPAYAIPAALQKAGLTVNDID----------IFEI 192
Cdd:PRK07910 242 EGGALMVIETEEHAKARGANILARIMGASITSdgfhmVAPDPNGERAGHAMTRAIELAGLTPGDIDhvnahatgtsVGDV 321
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1274095745 193 NEAFASQAVYCVEKLGIPAEKVnplggaiALGHPLGCTGA-RQVVTLL 239
Cdd:PRK07910 322 AEGKAINNALGGHRPAVYAPKS-------ALGHSVGAVGAvESILTVL 362
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
129-188 |
2.61e-03 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 38.86 E-value: 2.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095745 129 GAAAVLLARRSKAEELGLPILGVLRSYAVV-----GVPPDVmgIGPAYAIPAALQKAGLTVNDID 188
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMRldanrGPDPSL--EGEMRVIRAALRRAGLGPEDID 302
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
128-270 |
5.42e-03 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 37.75 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 128 DGAAAVLLarrSKAEELGlpILG-VLRS------YAVVGVPPDVMGIGPAY------------------AIPAALQKAGL 182
Cdd:PRK09352 160 DGAGAVVL---GASEEPG--ILStHLGSdgsygdLLYLPGGGSRGPASPGYlrmegrevfkfavrelakVAREALEAAGL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095745 183 TVNDIDIF-------EINEAFAsqavycvEKLGIPAEKVnplggAIALGHpLGCTGARQVVTLLNELKRRGRRAYGVVSM 255
Cdd:PRK09352 235 TPEDIDWLvphqanlRIIDATA-------KKLGLPMEKV-----VVTVDK-YGNTSAASIPLALDEAVRDGRIKRGDLVL 301
|
170
....*....|....*...
gi 1274095745 256 CIGTGMG---AAAVFEYP 270
Cdd:PRK09352 302 LEGFGGGltwGAALVRWP 319
|
|
| |
