|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
1-275 |
1.78e-154 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 438.43 E-value: 1.78e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLADRGNPGNITSRLMEKEKARDCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVP 80
Cdd:PLN02287 157 IGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVP 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 81 VTTTVHDDK-GTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVL 159
Cdd:PLN02287 237 VHTKIVDPKtGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVF 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 160 RSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGA 239
Cdd:PLN02287 317 RSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGA 396
|
250 260 270
....*....|....*....|....*....|....*..
gi 767923095 240 RQVITLLNELKRRGKRA-YGVVSMCIGTGMGAAAVFE 275
Cdd:PLN02287 397 RCVATLLHEMKRRGKDCrFGVVSMCIGTGMGAAAVFE 433
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
1-276 |
2.12e-149 |
|
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: 423.04 E-value: 2.12e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLA--------DRGNPGNITSRLMEKEKARD--CLIPMGITSENVAERFGISREKQDTFALASQQKAARAQS 70
Cdd:cd00751 107 VAGGVESMSRApyllpkarRGGRLGLNTLDGMLDDGLTDpfTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAAAQE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 71 KGCFQAEIVPVTTtvhddKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEE 150
Cdd:cd00751 187 AGRFKDEIVPVEV-----PGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAGNASGINDGAAAVLLMSEEKAKE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 151 LGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVAL 230
Cdd:cd00751 262 LGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIAL 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767923095 231 GHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFEY 276
Cdd:cd00751 342 GHPLGASGARIVVTLLHELKRRGGR-YGLATMCIGGGQGAAMVIER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
2-275 |
1.13e-139 |
|
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: 398.67 E-value: 1.13e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 2 ACGVESMSLA----------DRGNPGNITSRLMEKEKARDCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSK 71
Cdd:COG0183 112 AGGVESMSRApmllpkarwgYRMNAKLVDPMINPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 72 GCFQAEIVPVTTtvhddKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEEL 151
Cdd:COG0183 192 GRFDDEIVPVEV-----PDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAGNASGINDGAAALLLMSEEAAKEL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 152 GLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALG 231
Cdd:COG0183 267 GLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALG 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767923095 232 HPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:COG0183 347 HPLGASGARILVTLLHELERRGGR-YGLATMCIGGGQGIALIIE 389
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
2-275 |
1.51e-131 |
|
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: 377.72 E-value: 1.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 2 ACGVESMS---------LADRGNPGNITSRLMEKEKARD--CLIPMGITSENVAERFGISREKQDTFALASQQKAARAQS 70
Cdd:TIGR01930 107 AGGVESMSrvpygvprsLRWGVKPGNAELEDARLKDLTDanTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 71 KGCFQAEIVPVTttvhdDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEE 150
Cdd:TIGR01930 187 EGLFKDEIVPVT-----VKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAGNSSPLNDGAAALLLMSEEKAKE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 151 LGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVAL 230
Cdd:TIGR01930 262 LGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIAL 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767923095 231 GHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:TIGR01930 342 GHPLGASGARIVTTLLHELKRRGGR-YGLATMCIGGGQGAAVILE 385
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-277 |
1.45e-124 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 360.24 E-value: 1.45e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLADRGNPGNITSRLMEKEKARDCLI-----------PMGITSENVAERFGISREKQDTFALASQQKAARAQ 69
Cdd:PRK05790 111 VAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIhdgltdafngyHMGITAENLAEQYGITREEQDEFALASQQKAEAAI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 70 SKGCFQAEIVPVTttVHDDKGTkrSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAE 149
Cdd:PRK05790 191 KAGRFKDEIVPVT--IKQRKGD--PVVVDTDEHPRPDTTAESLAKLRPAFDKDGTVTAGNASGINDGAAAVVVMSEAKAK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 150 ELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVA 229
Cdd:PRK05790 267 ELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIA 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767923095 230 LGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFEYP 277
Cdd:PRK05790 347 LGHPIGASGARILVTLLHEMKRRGAK-KGLATLCIGGGQGVALIVERP 393
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-275 |
1.31e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 329.79 E-value: 1.31e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLADRGnpGNIT---SRLMEKekARDCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAE 77
Cdd:PRK07661 113 IAGGAESMSLVPMM--GHVVrpnPRLVEA--APEYYMGMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 78 IVPVTTTVH----DDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGL 153
Cdd:PRK07661 189 IVPVDVTLRtvgeNNKLQEETITFSQDEGVRADTTLEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 154 PILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHP 233
Cdd:PRK07661 269 KPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHP 348
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767923095 234 LGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK07661 349 LGCTGAKLTLSLIHEMKRRNEQ-FGIVTMCIGGGMGAAGVFE 389
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-275 |
1.19e-106 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 315.02 E-value: 1.19e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLAD-RGNPGNITSRLMEKEKARDCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIV 79
Cdd:PRK09052 118 IAAGVESMSMVPmMGNKPSMSPAIFARDENVGIAYGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEIT 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 80 PVTTTVH--DDKGTK---RSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLP 154
Cdd:PRK09052 198 PYEITERfpDLATGEvdvKTRTVDLDEGPRADTSLEGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLT 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 155 ILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPL 234
Cdd:PRK09052 278 PLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPL 357
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767923095 235 GCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK09052 358 GATGAIRTATVVHGLRRTNLK-YGMVTMCVGTGMGAAGIFE 397
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
2-275 |
2.09e-97 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 291.09 E-value: 2.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 2 ACGVESMSLADRGNPGNITSRLMEKEKARDCL----------IPMGITSENVAERFGISREKQDTFALASQQKAARAQSK 71
Cdd:PRK09051 114 GGGAESMSRAPYLLPAARWGARMGDAKLVDMMvgalhdpfgtIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 72 GCFQAEIVPVTTtvhddKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKD-GSTTAGNSSQVSDGAAAILLARRSKAEE 150
Cdd:PRK09051 194 GYFKDQIVPVEI-----KTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKEnGTVTAGNASGINDGAAAVVLAEADAAEA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 151 LGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVAL 230
Cdd:PRK09051 269 RGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISL 348
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767923095 231 GHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK09051 349 GHPVGATGAIITVKALYELQRIGGR-YALVTMCIGGGQGIAAIFE 392
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
36-275 |
4.09e-93 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 279.93 E-value: 4.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 36 MGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTtvHDDKGTKrsITVTQDEGIRPSTTMEGLAKL 115
Cdd:PRK08947 147 MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEG--HDADGVL--KLFDYDEVIRPETTVEALAAL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 116 KPAFK-KDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDV 194
Cdd:PRK08947 223 RPAFDpVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDI 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 195 DIFEINEAFASQAAYCVEKLRL---PPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAA 271
Cdd:PRK08947 303 DVFELNEAFAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQ-FGLATMCIGLGQGIA 381
|
....
gi 767923095 272 AVFE 275
Cdd:PRK08947 382 TVFE 385
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
2-275 |
4.69e-92 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 277.99 E-value: 4.69e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 2 ACGVESMSLAD--RGNPGNITSR----------------LMEKEKARDcliPMGITSENVAERFGISREKQDTFALASQQ 63
Cdd:PRK09050 114 AGGVESMSRAPfvMGKADSAFSRqaeifdttigwrfvnpLMKAQYGVD---SMPETAENVAEDYNISRADQDAFALRSQQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 64 KAARAQSKGCFQAEIVPVttTVHDDKGTkrSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLA 143
Cdd:PRK09050 191 RAAAAQAAGFLAEEIVPV--TIPQKKGD--PVVVDRDEHPRPETTLEALAKLKPVFRPDGTVTAGNASGVNDGAAALLLA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 144 RRSKAEELGL-PILGVLrSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLP--PEK 220
Cdd:PRK09050 267 SEAAAKKHGLtPRARIL-GMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLAddDAR 345
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767923095 221 VNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK09050 346 VNPNGGAIALGHPLGMSGARLVLTALHQLERTGGR-YALCTMCIGVGQGIALAIE 399
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-275 |
7.61e-89 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 269.33 E-value: 7.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLA-DRGNPGNITSRLMEKEKArDCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIV 79
Cdd:PRK07108 113 VAGGVESISCVqNEMNRHMLREGWLVEHKP-EIYWSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 80 PVTTTVH-DDKGT----KRSITVTQDEGIRPSTTMEGLAKLKPAFKkDGSTTAGNSSQVSDGAAAILLARRSKAEELGLP 154
Cdd:PRK07108 192 PITVTAGvADKATgrlfTKEVTVSADEGIRPDTTLEGVSKIRSALP-GGVITAGNASQFSDGASACVVMNAKVAEREGLQ 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 155 ILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPL 234
Cdd:PRK07108 271 PLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPY 350
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767923095 235 GCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK07108 351 GVSGARLTGHALIEGKRRGAK-YVVVTMCIGGGQGAAGLFE 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-275 |
9.61e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 264.54 E-value: 9.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMS-------------------LADRGNPGNITSrlmekeKARDCLIPMGI--TSENVAERFGISREKQDTFAL 59
Cdd:PRK06205 111 IAGGAESMSnvefyttdmrwgvrgggvqLHDRLARGRETA------GGRRFPVPGGMieTAENLRREYGISREEQDALAV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 60 ASQQKAARAQSKGCFQAEIVPVTttVHDDKGTkrSITVTQDEGIRPSTTMEGLAKLKP---AFKKDGSTTAGNSSQVSDG 136
Cdd:PRK06205 185 RSHQRAVAAQEAGRFDDEIVPVT--VPQRKGD--PTVVDRDEHPRADTTLESLAKLRPimgKQDPEATVTAGNASGQNDA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 137 AAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRL 216
Cdd:PRK06205 261 AAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGF 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767923095 217 PP---EKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK06205 341 GAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQAR-YGLETMCIGGGQGLAAVFE 401
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-275 |
2.10e-86 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 263.12 E-value: 2.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLADRG-NPG-NITSRLMEKEKARDCLIP----MGITSENVAERFGISREKQDTFALASQQKAARAQSKGCF 74
Cdd:PRK06445 118 IAGGVEHMTRTPMGdNPHiEPNPKLLTDPKYIEYDLTtgyvMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 75 QAEIVPVTTTVHDDKgtkrsITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLP 154
Cdd:PRK06445 198 KDEILPIEVEVEGKK-----KVVDVDQSVRPDTSLEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 155 ILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPL 234
Cdd:PRK06445 273 PMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPL 352
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767923095 235 GCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK06445 353 GATGARIVGTLARQLQIKGKD-YGVATLCVGGGQGGAVVLE 392
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
31-275 |
1.80e-81 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 251.08 E-value: 1.80e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 31 DCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTvhddKGTkrsiTVTQDEGIRPSTTME 110
Cdd:PRK07851 168 DVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP----DGT----VVSTDDGPRAGTTYE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 111 GLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLT 190
Cdd:PRK07851 240 KVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAGMS 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 191 VSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGA 270
Cdd:PRK07851 320 IDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKT-FGLETMCVGGGQGM 398
|
....*
gi 767923095 271 AAVFE 275
Cdd:PRK07851 399 AMVLE 403
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-277 |
1.26e-78 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 243.26 E-value: 1.26e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLADRGNPGNITSRLMEKEKARDCLIP-----------MGITSENVAERFGISREKQDTFALASQQKAARAQ 69
Cdd:PRK05656 111 IAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITdglwdafndyhMGITAENLVEKYGISREAQDAFAAASQQKAVAAI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 70 SKGCFQAEIVPVTttVHDDKGtkRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAE 149
Cdd:PRK05656 191 EAGRFDDEITPIL--IPQRKG--EPLAFATDEQPRAGTTAESLAKLKPAFKKDGSVTAGNASSLNDGAAAVLLMSAAKAK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 150 ELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVA 229
Cdd:PRK05656 267 ALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIA 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767923095 230 LGHPLGCTGARQVITLLNELKRRGKRAyGVVSMCIGTGMGAAAVFEYP 277
Cdd:PRK05656 347 LGHPIGASGCRVLVTLLHEMIRRDAKK-GLATLCIGGGQGVALAIERD 393
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
2-277 |
4.80e-78 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 241.93 E-value: 4.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 2 ACGVESMSLADRGNPGNITSRLMEKEKARDCLI-----------PMGITSENVAERFGISREKQDTFALASQQKAARAQS 70
Cdd:PRK08235 112 AGGMESMSNAPYILPGARWGYRMGDNEVIDLMVadgltcafsgvHMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 71 KGCFQAEIVPVTttVHDDKGtkRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEE 150
Cdd:PRK08235 192 EGRFEEEIVPVT--IPQRKG--DPIVVAKDEAPRKDTTIEKLAKLKPVFDKTGTITAGNAPGVNDGAAALVLMSEDRAKQ 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 151 LGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVAL 230
Cdd:PRK08235 268 EGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVAL 347
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767923095 231 GHPLGCTGARQVITLLNELKRRGKrAYGVVSMCIGTGMGAAAVFEYP 277
Cdd:PRK08235 348 GHPIGASGARIIVTLIHELKRRGG-GIGIAAICSGGGQGDAVLIEVH 393
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
36-275 |
8.46e-77 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 238.91 E-value: 8.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 36 MGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRsitVTQDEGIRPSTTMEGLAKL 115
Cdd:PRK08131 162 MPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLPPKL---VAEDEHPRPSSTVEALTKL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 116 KPAFKkDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVD 195
Cdd:PRK08131 239 KPLFE-GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMD 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 196 IFEINEAFASQAAYCVEKLRLP--PEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAV 273
Cdd:PRK08131 318 IIEINEAFASQVLGCLKGLGVDfdDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKR-YAVVSLCIGVGQGLAMV 396
|
..
gi 767923095 274 FE 275
Cdd:PRK08131 397 IE 398
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
2-275 |
1.81e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 237.86 E-value: 1.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 2 ACGVESMSLADRGNPGNitSRLMEKEKARDC-LIPMGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVP 80
Cdd:PRK08242 115 AGGVESMSRVPMGSDGG--AWAMDPSTNFPTyFVPQGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 81 VTttvhDDKGtkrsITV-TQDEGIRPSTTMEGLAKLKPAFKKDGST---------------------TAGNSSQVSDGAA 138
Cdd:PRK08242 193 VK----DQNG----LTIlDHDEHMRPGTTMESLAKLKPSFAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 139 AILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPP 218
Cdd:PRK08242 265 AVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPH 344
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767923095 219 EKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK08242 345 DKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKR-TALITLCVGGGMGIATIIE 400
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-275 |
4.11e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 236.85 E-value: 4.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLADRGNP-------GNITS-RLMEKEKARDCL--IPMGITSENVAERFGISREKQDTFALASQQKAARAQS 70
Cdd:PRK06633 112 IAGGQENMSLGMHGSYiragakfGDIKMvDLMQYDGLTDVFsgVFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 71 KGCFQAEIVPVTTTVhddkgTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEE 150
Cdd:PRK06633 192 AGIFKDEILPIEVTI-----KKTTSLFDHDETVRPDTSLEILSKLRPAFDKNGVVTAGNASSINDGAACLMVVSEEALKK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 151 LGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVAL 230
Cdd:PRK06633 267 HNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAI 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767923095 231 GHPLGCTGARQVITLLNELkRRGKRAYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK06633 347 GHPIGASGGRVLITLIHGL-RRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-275 |
1.28e-75 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 235.37 E-value: 1.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 2 ACGVESMSLADRGNPGNITSRLMEKEKARDCLI-----------PMGITSENVAERFGISREKQDTFALASQQKAARAQS 70
Cdd:PLN02644 111 AGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLkdglwdvyndfGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 71 KGCFQAEIVPVTTTVhddKGTKRSITVTQDEGIRpSTTMEGLAKLKPAFKKD-GSTTAGNSSQVSDGAAAILLARRSKAE 149
Cdd:PLN02644 191 AGAFAWEIVPVEVPG---GRGRPSVIVDKDEGLG-KFDPAKLRKLRPSFKEDgGSVTAGNASSISDGAAALVLVSGEKAL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 150 ELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVA 229
Cdd:PLN02644 267 ELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVS 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767923095 230 LGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PLN02644 347 LGHPIGCSGARILVTLLGVLRSKNGK-YGVAGICNGGGGASAIVVE 391
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
36-275 |
7.21e-74 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 231.83 E-value: 7.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 36 MGITSENVAERFGISREKQDTFALASQQKAARAQSKGcFQAEIVPVTttvhDDKGTkrsiTVTQDEGIRPSTTMEGLAKL 115
Cdd:PRK08170 177 MGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEG-RLKEVVPLF----DRDGK----FYDHDDGVRPDSSMEKLAKL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 116 KPAF-KKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDV 194
Cdd:PRK08170 248 KPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 195 DIFEINEAFASQ----------AAYCVEKLRLP-------PEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRaY 257
Cdd:PRK08170 328 DLWEINEAFAAQvlaclaawadEEYCREQLGLDgalgeldRERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGTK-R 406
|
250
....*....|....*...
gi 767923095 258 GVVSMCIGTGMGAAAVFE 275
Cdd:PRK08170 407 GIAAICIGGGQGGAMLLE 424
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-275 |
2.89e-71 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 224.22 E-value: 2.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLA--------DRGNPgnitsrlmekeKARDCLIPMG---ITSENVAERFGISREKQDTFALASQQKAARAQ 69
Cdd:PRK07850 112 IACGVEAMSRVplganagpGRGLP-----------RPDSWDIDMPnqfEAAERIAKRRGITREDVDAFGLRSQRRAAQAW 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 70 SKGCFQAEIVPVTTTVHDDKG--TKRSITVTQDEGIRpSTTMEGLAKLKPAFKkDGSTTAGNSSQVSDGAAAILLARRSK 147
Cdd:PRK07850 181 AEGRFDREISPVQAPVLDEEGqpTGETRLVTRDQGLR-DTTMEGLAGLKPVLE-GGIHTAGTSSQISDGAAAVLWMDEDR 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 148 AEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGA 227
Cdd:PRK07850 259 ARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGA 338
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767923095 228 VALGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK07850 339 IALGHPVGSTGARLITTALHELERTDKS-TALITMCAGGALSTGTIIE 385
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
36-275 |
3.67e-71 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 225.25 E-value: 3.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 36 MGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDkgtkrsiTVTQDEGIRPSTTMEGLAKL 115
Cdd:PRK08963 176 MGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ-------PLEEDNNIRGDSTLEDYAKL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 116 KPAF-KKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPP-DIMGIGPAYAIPVALQKAGLTVSD 193
Cdd:PRK08963 249 RPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLALERAGLTLAD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 194 VDIFEINEAFASQAA----------YCVEKLRLP-------PEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKrA 256
Cdd:PRK08963 329 LTLIDMHEAFAAQTLanlqmfaserFAREKLGRSqaigevdMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRRGG-G 407
|
250
....*....|....*....
gi 767923095 257 YGVVSMCIGTGMGAAAVFE 275
Cdd:PRK08963 408 LGLTTACAAGGLGAAMVLE 426
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
153-276 |
8.29e-66 |
|
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: 201.33 E-value: 8.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 153 LPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGH 232
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767923095 233 PLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFEY 276
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGK-YGLASLCIGGGQGVAMIIER 123
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-275 |
6.97e-62 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 200.77 E-value: 6.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSL----ADRGNPGNITSRLMEKEKAR-DCLIPM---GITSENVAERFGISREKQDTFALASQQKAARAQSKG 72
Cdd:PRK06025 115 IAGGTEMMSYtaamAAEDMAAGKPPLGMGSGNLRlRALHPQshqGVCGDAIATMEGITREALDALGLESQRRAARAIKEG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 73 CFQAEIVPVtttvHDDKGtkrSITVTQDEGIRPSTTMEGLAKLKPAFKK-------DGSTT------------------- 126
Cdd:PRK06025 195 RFDKSLVPV----YRDDG---SVALDHEEFPRPQTTAEGLAALKPAFTAiadypldDKGTTyrglinqkypdleikhvhh 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 127 AGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQ 206
Cdd:PRK06025 268 AGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVV 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767923095 207 AAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK06025 348 AEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLK-RGLVTMCAAGGMAPAIIIE 415
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
40-275 |
4.55e-61 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 197.62 E-value: 4.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 40 SENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTtvhddkgtkrsitVTQDEGIRpSTTMEGLAKLKPaF 119
Cdd:PRK07801 161 AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG-------------VTVDEGPR-ETSLEKMAGLKP-L 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 120 KKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEI 199
Cdd:PRK07801 226 VEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEI 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767923095 200 NEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK07801 306 NEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGR-YGLQTMCEGGGTANVTIIE 380
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
36-275 |
5.63e-60 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 194.21 E-value: 5.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 36 MGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPvtttvhddkgtkrsITVTQDEGIRPSTTMEGL-AK 114
Cdd:PRK06690 133 MGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILS--------------FNGLLDESIKKEMNYERIiKR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 115 LKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGL-PILGVLRSyAVVGVPPDIMGIGPAYAIPVALQKAGLTVSD 193
Cdd:PRK06690 199 TKPAFLHNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVED 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 194 VDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAV 273
Cdd:PRK06690 278 IDYFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMK-YGIATLGIGGGIGLALL 356
|
..
gi 767923095 274 FE 275
Cdd:PRK06690 357 FE 358
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-275 |
1.35e-57 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 189.17 E-value: 1.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLADRGNP---------GNITSRLMEkEKARDCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSK 71
Cdd:PRK06504 112 IAAGVESMTRVPMGSPstlpaknglGHYKSPGME-ERYPGIQFSQFTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 72 GCFQAEIVPVTTTVHDDKGTKRSItvtqDEGIRPSTTMEGLAKLKPaFKKDGSTTAGNSSQVSDGAAAILLARRSKAEEL 151
Cdd:PRK06504 191 GKFKAEIVPLEITRADGSGEMHTV----DEGIRFDATLEGIAGVKL-IAEGGRLTAATASQICDGASGVMVVNERGLKAL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 152 GLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALG 231
Cdd:PRK06504 266 GVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALG 345
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767923095 232 HPLGCTGARQVITLLNELKRRGKRaYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK06504 346 HPLGASGTKLMTTLVHALKQRGKR-YGLQTMCEGGGMANVTIVE 388
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
1-146 |
5.05e-57 |
|
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: 183.66 E-value: 5.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLADRGNPGNITSRL-MEKEKARDCLIP-----------MGITSENVAERFGISREKQDTFALASQQKAARA 68
Cdd:pfam00108 108 LAGGVESMSHAPYALPTDARSGLkHGDEKKHDLLIPdgltdafngyhMGLTAENVAKKYGISREEQDAFAVKSHQKAAAA 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767923095 69 QSKGCFQAEIVPVTTTVHDDKGTkrsitVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRS 146
Cdd:pfam00108 188 PKAGKFKDEIVPVTVKGRKGKPT-----VDKDEGIRPPTTAEPLAKLKPAFDKEGTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
36-275 |
7.54e-55 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 182.01 E-value: 7.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 36 MGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTvhddkGTKRSITVTQDEGIRpSTTMEGLAKL 115
Cdd:PRK06954 163 MGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVA-----GKKGDTVIDRDEQPF-KANPEKIPTL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 116 KPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVD 195
Cdd:PRK06954 237 KPAFSKTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVD 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 196 IFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAyGVVSMCIGTGMGAAAVFE 275
Cdd:PRK06954 317 LFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKR-GVASLCIGGGEATAMGIE 395
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
36-275 |
3.09e-54 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 181.25 E-value: 3.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 36 MGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVtttvhddKGtkrsitVTQDEGIRPSTTMEGLAKL 115
Cdd:PRK09268 178 MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-------LG------LTRDNNLRPDSSLEKLAKL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 116 KPAFKK--DGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVP----PDIMGIGPAYAIPVALQKAGL 189
Cdd:PRK09268 245 KPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhgKEGLLMAPAYAVPRLLARNGL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 190 TVSDVDIFEINEAFASQ----------AAYCVEKLRLP-------PEKVNPLGGAVALGHPLGCTGARQVITLLNELKRR 252
Cdd:PRK09268 325 TLQDFDFYEIHEAFASQvlatlkawedEEYCRERLGLDaplgsidRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEK 404
|
250 260
....*....|....*....|...
gi 767923095 253 GKrAYGVVSMCIGTGMGAAAVFE 275
Cdd:PRK09268 405 GS-GRGLISICAAGGQGVTAILE 426
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-275 |
5.20e-50 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 169.42 E-value: 5.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLAD-------RGNPGNITSRLMEKEKAR--DCLIP------MGITSENVAERFGISREKQDTFALASQQKA 65
Cdd:PRK06366 111 IAGGMENMSNAPfllpsdlRWGPKHLLHKNYKIDDAMlvDGLIDafyfehMGVSAERTARKYGITREMADEYSVQSYERA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 66 ARAQSKGCFQAEIVPVTTtvhddkgtkrsitVTQDEGIRpSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARR 145
Cdd:PRK06366 191 IRATESGEFRNEIVPFND-------------LDRDEGIR-KTTMEDLAKLPPAFDKNGILTAGNSAQLSDGGSALVMASE 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 146 SKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLG 225
Cdd:PRK06366 257 KAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQLKIDNERFNVNG 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767923095 226 GAVALGHPLGCTGARQVITLLNELKRRGKRAyGVVSMCIGTGMGAAAVFE 275
Cdd:PRK06366 337 GAVAIGHPIGNSGSRIIVTLINALKTRHMKT-GLATLCHGGGGAHTLTLE 385
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
1-276 |
5.50e-47 |
|
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: 161.51 E-value: 5.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 1 MACGVESMSLADRGNPgnitsrlmeKEKARDCLIpmgitsenvaERFGiSREKQDTFALASQQKAARAQSKGCFQAEIVP 80
Cdd:cd00826 108 LAGGFEKMETSAENNA---------KEKHIDVLI----------NKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 81 VTTtvhddKGTKRSITVTQDEGIR--PSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPI--- 155
Cdd:cd00826 168 FGV-----KGRKGDIHSDADEYIQfgDEASLDEIAKLRPAFDKEDFLTAGNACGLNDGAAAAILMSEAEAQKHGLQSkar 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 156 ----LGVLRSYAVVGVPPD----IMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEK------- 220
Cdd:cd00826 243 eiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvd 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767923095 221 -----------VNPLGGAVALGHPLGCTGARQVITLLNELKRR-GKRA---YGVVSMCIGTGMGAAAVFEY 276
Cdd:cd00826 323 rgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEaGKRQgagAGLALLCIGGGGGAAMCIES 393
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
127-273 |
4.45e-18 |
|
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: 81.34 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 127 AGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPD----IMGIGPAYAIPVALQKAGLTVSDVDIFEINEA 202
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 203 FASQAAYCVEKLRLPPEKVNPL---GGAVALGHPLGCTGARQVITLLNELKRRGKRAY------GVVSMCIGTGMGAAAV 273
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVRSPavsATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTpreprtVLLLGFGLGGTNAAVV 253
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
131-273 |
7.90e-13 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 67.67 E-value: 7.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 131 SQVSDGAAAILLARRSKAEELGLP---ILGV---LRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFA 204
Cdd:cd00829 202 CPVSDGAAAVVLASEERARELTDRpvwILGVgaaSDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFT 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 205 S---------------QAAYCVEKL------RLPpekVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKrAYGV---- 259
Cdd:cd00829 282 IaellaledlgfcekgEGGKLVREGdtaiggDLP---VNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAG-ARQVpgar 357
|
170
....*....|....
gi 767923095 260 VSMCIGTGMGAAAV 273
Cdd:cd00829 358 VGLAHNIGGTGSAA 371
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
130-272 |
1.02e-11 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 64.53 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 130 SSQVSDGAAAILLARRSKAEELGLPILGVLRS-----YAVVGVPPDIMGIGPA-YAIPVALQKAGLTVSDVDIFEINEAF 203
Cdd:PRK06064 208 CSPITDGAAAVILASEEKAKEYTDTPVWIKASgqasdTIALHDRKDFTTLDAAvVAAEKAYKMAGIEPKDIDVAEVHDCF 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 204 ASQAAYCVEKL---------------------RLPpekVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVVsm 262
Cdd:PRK06064 288 TIAEILAYEDLgfakkgeggklaregqtyiggDIP---VNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAEKGRQQV-- 362
|
170
....*....|
gi 767923095 263 cIGTGMGAAA 272
Cdd:PRK06064 363 -IGAGYGLTH 371
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
131-276 |
2.80e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 54.18 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 131 SQVSDGAAAILLARRSKAEELGLPIlgVLRSYAVVGvppDIMGI---------GPAYAIPVALQKAGLTVSDVDIFEINE 201
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALQRAV--RFRARAHVN---DFLPLsrrdplafeGPRRAWQRALAQAGVTLDDLSFVETHD 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 202 AF---------------ASQAAYCVEKL------RLPpekVNPLGGAVALGHPLGCTG-------ARQVITLLNELKRRG 253
Cdd:PRK07516 288 CFtiaelieyeamglapPGQGARAIREGwtakdgKLP---VNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPG 364
|
170 180
....*....|....*....|...
gi 767923095 254 KRAYGVVSmcigtgMGAAAVFEY 276
Cdd:PRK07516 365 AKLAGVFN------MGGAAVANY 381
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
131-240 |
5.41e-08 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 53.15 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 131 SQVSDGAAAILLARRSKAEELG----LP-ILGVLRSYAVVGVPPDI-MGIGPAYAIPV-------ALQKAGLTVSDVDIF 197
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDYAdarpIPrIKGWGHRTAPLGLEQKLdRSAGDPYVLPHvrqavldAYRRAGVGLDDLDGF 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767923095 198 EINEAFASQAAYCVEKLRL-PPEK-----------------VNPLGGAVALGHPLGCTGAR 240
Cdd:PRK06289 300 EVHDCFTPSEYLAIDHIGLtGPGEswkaiengeiaiggrlpINPSGGLIGGGHPVGASGVR 360
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
131-250 |
1.37e-07 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 52.20 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 131 SQVSDGAAAILLARRSKAEELGL-----PILGVLRSYAVVGV----PPDIMGIGPAY-AIPVALQKAGLTVSDVDIFEIN 200
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLspndsRLVEIKSLACASGNlyedPPDATRMFTSRaAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767923095 201 EAFASQAAYCVEKL---------------------RLPpekVNPLGGAVALGHPLGCTGARQVITLLNELK 250
Cdd:PTZ00455 336 DCFTIAELLMYEALgiaeyghakdlirngatalegRIP---VNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
184-276 |
1.49e-05 |
|
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: 42.49 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 184 LQKAGLTVSDVDIF-------EINEAFAsqaaycvEKLRLPPEKVnplggAVALGHpLGCTGARQVITLLNELKRRGKRA 256
Cdd:pfam08541 1 LEKAGLTPEDIDWFvphqanlRIIDAVA-------KRLGLPPEKV-----VVNLDE-YGNTSAASIPLALDEAVEEGKLK 67
|
90 100
....*....|....*....|...
gi 767923095 257 YGVVSMCIGTGMG---AAAVFEY 276
Cdd:pfam08541 68 PGDLVLLVGFGAGltwGAALLRW 90
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
129-267 |
1.87e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 45.61 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 129 NSSQVSDGAAAILLARRSKAEELGL--PI----LGVLRSYAVVGVPPDIMGIGPAY-AIPVALQKAGLTVSDVDIFEINE 201
Cdd:PRK12578 205 DSCPISDGSATAIFASEEKVKELKIdsPVwitgIGYANDYAYVARRGEWVGFKATQlAARQAYNMAKVTPNDIEVATVHD 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 202 AF--ASQAAY----CVEKLRL-------PPEK-----VNPLGGAVALGHPLGCTGARQVITLLNELKRRG-------KRA 256
Cdd:PRK12578 285 AFtiAEIMGYedlgFTEKGKGgkfieegQSEKggkvgVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAgklqqplKKY 364
|
170
....*....|.
gi 767923095 257 YGVVSMCIGTG 267
Cdd:PRK12578 365 IGLVHNVGGTG 375
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
134-252 |
5.04e-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: 44.35 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 134 SDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPD----IMGIGPAYAIPVALQKAGLTVSDVDIfeINEAFASQAAY 209
Cdd:cd00828 230 AEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGrsvpAGGKGIARAIRTALAKAGLSLDDLDV--ISAHGTSTPAN 307
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767923095 210 CVEKLRLPPEKVNPLGGAVAL-------GHPLGCTGARQVITLLNELKRR 252
Cdd:cd00828 308 DVAESRAIAEVAGALGAPLPVtaqkalfGHSKGAAGALQLIGALQSLEHG 357
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
133-238 |
1.02e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 43.14 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 133 VSDGAAAILLARRSKAEEL--------GL------PILGVlRSYAVVgvppdimgigPAYAIpvALQKA-GLTVSDVDIF 197
Cdd:PRK07937 204 ITDGAAAVVLAAGDRARELrerpawitGIehriesPSLGA-RDLTRS----------PSTAL--AAEAAtGGDAGGVDVA 270
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767923095 198 EINEAFASQAAYCVEKLRLPPE-KVNPLGGAVAlGHPLGCTG 238
Cdd:PRK07937 271 ELHAPFTHQELILREALGLGDKtKVNPSGGALA-ANPMFAAG 311
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
183-276 |
2.39e-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: 42.02 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 183 ALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVnplggaVALGHPLGCTGARQVITLLNELKRRGKRAYGVVSM 262
Cdd:COG0332 233 ALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKV------VVNIDRYGNTSAASIPLALDEALREGRIKPGDLVL 306
|
90
....*....|....*..
gi 767923095 263 CIGTGMG---AAAVFEY 276
Cdd:COG0332 307 LAGFGAGltwGAAVLRW 323
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
183-258 |
6.39e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 40.66 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 183 ALQKAGLT--VSDVDIFEINEAFASQAAYCVEKLRLPPE------------------KVNPLGGAVALGHPLGCTGARQV 242
Cdd:PRK06365 302 AYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLCKYgeggqfiesgkpelpgklPVNPSGGLLAAGHAVGATGIMQA 381
|
90
....*....|....*.
gi 767923095 243 ITLLNELKRRGKRAYG 258
Cdd:PRK06365 382 VFMFWQLQGRIKKHFH 397
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
135-246 |
1.16e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 40.10 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 135 DGAAAILLARRSKAEELGLPILGVLRSYAVVG-----VPPDIMGIGPAYAIPVALQKAGLTVSDVD----------IFEI 199
Cdd:PRK07910 242 EGGALMVIETEEHAKARGANILARIMGASITSdgfhmVAPDPNGERAGHAMTRAIELAGLTPGDIDhvnahatgtsVGDV 321
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767923095 200 NEAFASQAAYCVEKlrlpPEKVNPLGgavALGHPLGCTGA-RQVITLL 246
Cdd:PRK07910 322 AEGKAINNALGGHR----PAVYAPKS---ALGHSVGAVGAvESILTVL 362
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
185-254 |
2.55e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 38.73 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 185 QKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEK------------------VNPLGGAVALGHPLGCTGARQVITLL 246
Cdd:PRK08256 275 EQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGeaekfiddgdntyggrwvVNPSGGLLSKGHPLGATGLAQCAELT 354
|
....*...
gi 767923095 247 NELkrRGK 254
Cdd:PRK08256 355 WQL--RGT 360
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
134-195 |
3.95e-03 |
|
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: 38.15 E-value: 3.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767923095 134 SDGAAAILLARRSKAEELGLPILGVLRSYA-------VVGVPPDimGIGPAYAIPVALQKAGLTVSDVD 195
Cdd:COG0304 230 GEGAGVLVLEELEHAKARGAKIYAEVVGYGassdayhITAPAPD--GEGAARAMRAALKDAGLSPEDID 296
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
133-203 |
4.24e-03 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 38.09 E-value: 4.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767923095 133 VSDGAAAILLARRSKAEELGLPILGVLRSYAVV-----GVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAF 203
Cdd:PRK06158 208 VTDGAGAVVMVRADRARDLPRPPVYVLGAAAATwhrqiSSMPDLTVTAAAESGPRAFAMAGLTPADIDVVELYDAF 283
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
134-239 |
4.52e-03 |
|
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: 38.29 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 134 SDGAAAILLARRSKAEELGLPILGVLRSYAVVG-----VPPDIMGIGPAYAIPVALQKAGLTVSDVDIfeIN-------- 200
Cdd:cd00834 230 GEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDY--INahgtstpl 307
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767923095 201 ----EAFASQAAYCVEKLRLPpekVNPLGGavALGHPLGCTGA 239
Cdd:cd00834 308 ndaaESKAIKRVFGEHAKKVP---VSSTKS--MTGHLLGAAGA 345
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
134-275 |
9.46e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 37.04 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 134 SDGAAAILLARRSKAEELG---LPILGVlrSYAVVGVPPDIMGIGPA----YAIPVALQKAGLT--VSDVDIFEINEAFA 204
Cdd:PRK06066 211 VDGAIVVVLASEEVAKKLTddpVWIKGI--GWSTESSNLETAELGKAnymrIAADMAYKMAGIEspRKEVDAAEVDDRYS 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923095 205 SQAAYCVEKLRLPPE------------------KVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVVSMC--- 263
Cdd:PRK06066 289 YKELQHIEALRLSEEpekdsllregnfdpqgelPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGARQGKAERAvva 368
|
170
....*....|....*.
gi 767923095 264 ----IGTGMGAAAVFE 275
Cdd:PRK06066 369 swrgIPTLTGSVVVVE 384
|
|
| |
