|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-391 |
0e+00 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 794.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPNVQLVENAPEYYMGMGHTAEQVAMKYGI 160
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVRPNPRLVEAAPEYYMGMGHTAEQVAVKYGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 161 SREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDENNKLREQKLMFSQDEGVRPGTTADVLGKLRPAFSIKGSV 240
Cdd:PRK07661 161 SREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGENNKLQEETITFSQDEGVRADTTLEILGKLRPAFNVKGSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 241 TAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLFELNEAFAS 320
Cdd:PRK07661 241 TAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAFAS 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504270775 321 QALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFELL 391
Cdd:PRK07661 321 QSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFELL 391
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-391 |
0e+00 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 553.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKkGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPeAEQGLNMARNIGALAGLPYT 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFG-GALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQ-AGQGQNPARQAALLAGLPES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARP----NVQLVE-------NAPEYYMGMGH 149
Cdd:COG0183 79 VPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWgyrmNAKLVDpminpglTDPYTGLSMGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 150 TAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDennklreqkLMFSQDEGVRPGTTADVLGK 229
Cdd:COG0183 159 TAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE---------VVVDRDEGPRPDTTLEKLAK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 230 LRPAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDI 309
Cdd:COG0183 230 LKPAFKKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 310 GLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:COG0183 310 DLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIE 389
|
..
gi 504270775 390 LL 391
Cdd:COG0183 390 RV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-389 |
0e+00 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 540.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 5 VIVAGARTPVGKAKkGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEqGLNMARNIGALAGLPYTVPAI 84
Cdd:cd00751 1 VIVSAVRTPIGRFG-GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 85 TINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPNVQLVEN-----------APEYYMGMGHTAEQ 153
Cdd:cd00751 79 TVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNtldgmlddgltDPFTGLSMGITAEN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 154 VAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKidennklreQKLMFSQDEGVRPGTTADVLGKLRPA 233
Cdd:cd00751 159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRK---------GPVVVDRDEGPRPDTTLEKLAKLKPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 234 FSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLFE 313
Cdd:cd00751 230 FKKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504270775 314 LNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:cd00751 310 INEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-391 |
0e+00 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 508.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKKGSLASVRPDDLGAIAVKETLRRAGGYE-GPIDDLIIGCAMPEAEQGLNMARnIGA-LAGLP 78
Cdd:PRK09052 5 LQDAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPGLDpKLIEDAIVGCAMPEAEQGLNVAR-IGAlLAGLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 79 YTVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPNVQLVENAPEYYM--GMGHTAEQVAM 156
Cdd:PRK09052 84 NSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSMSPAIFARDENVGIayGMGLTAEKVAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 157 KYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKID-ENNKLREQKLMFSQDEGVRPGTTADVLGKLRPAFS 235
Cdd:PRK09052 164 QWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDlATGEVDVKTRTVDLDEGPRADTSLEGLAKLKPVFA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 236 IKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLFELN 315
Cdd:PRK09052 244 NKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIELN 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504270775 316 EAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFELL 391
Cdd:PRK09052 324 EAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFERL 399
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-389 |
2.57e-169 |
|
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: 478.26 E-value: 2.57e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 6 IVAGARTPVGKAKkGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQgLNMARNIGALAGLPYTVPAIT 85
Cdd:TIGR01930 1 IVAAARTPIGKFG-GSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAYT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 86 INRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPN-------------VQLVENAPEYYMgMGHTAE 152
Cdd:TIGR01930 79 VNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkpgnaeledarLKDLTDANTGLP-MGVTAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 153 QVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVtlrkidennKLREQKLMFSQDEGVRPGTTADVLGKLRP 232
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTV---------KGRKGPVTVSSDEGIRPNTTLEKLAKLKP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 233 AFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLF 312
Cdd:TIGR01930 229 AFDPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLF 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504270775 313 ELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:TIGR01930 309 EINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-389 |
6.02e-168 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 475.03 E-value: 6.02e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKkGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPeAEQGLNMARNIGALAGLPYT 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFG-GALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQ-AGAGQNPARQAALKAGLPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVP-----MFGNVARPNVQLVENA---------PEYYMG 146
Cdd:PRK05790 79 VPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvlpgSRWGQKMGDVELVDTMihdgltdafNGYHMG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 147 MghTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKidennklrEQKLMFSQDEGVRPGTTADV 226
Cdd:PRK05790 159 I--TAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRK--------GDPVVVDTDEHPRPDTTAES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 227 LGKLRPAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLEL 306
Cdd:PRK05790 229 LAKLRPAFDKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 307 SDIGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAG 386
Cdd:PRK05790 309 ADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVAL 388
|
...
gi 504270775 387 VFE 389
Cdd:PRK05790 389 IVE 391
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
2-389 |
1.06e-148 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 428.41 E-value: 1.06e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 2 REAVIVAGARTPVGKAKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYTV 81
Cdd:PLN02287 46 DDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 82 PAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPM-FGNVARPNVQLVENAPEYYMGMGHTAEQVAMKYGI 160
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMaWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 161 SREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVtlrKIDENNKLREQKLMFSQDEGVRPGTTADVLGKLRPAFSIKGSV 240
Cdd:PLN02287 206 TREEQDQAAVESHRKAAAATASGKFKDEIVPVHT---KIVDPKTGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 241 TAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLFELNEAFAS 320
Cdd:PLN02287 283 TAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFAS 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504270775 321 QALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNE--QFGIVTMCIGGGMGAAGVFE 389
Cdd:PLN02287 363 QFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKdcRFGVVSMCIGTGMGAAAVFE 433
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-389 |
6.41e-147 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 421.68 E-value: 6.41e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKKGSLASVRPDDLGAIAVKETLRRAGGYE-GPIDDLIIGCAMPEAEQGLNMARNIGALAGLPY 79
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALDpAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 80 TVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVaRPNVQLVENAPEYYMGMGHTAEQVAMKYG 159
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGV-DFHPGLSKNVAKAAGMMGLTAEMLGKMHG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 160 ISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEvtlrKIDENNKLReqklMFSQDEGVRPGTTADVLGKLRPAFSIK-G 238
Cdd:PRK08947 160 ISREQQDAFAARSHQRAWAATQEGRFKNEIIPTE----GHDADGVLK----LFDYDEVIRPETTVEALAALRPAFDPVnG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 239 SVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLFELNEAF 318
Cdd:PRK08947 232 TVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAF 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504270775 319 ASQALGVIRELNI---NEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:PRK08947 312 AAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-391 |
1.03e-142 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 411.08 E-value: 1.03e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK07108 1 MTEAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVAR-PNVQLVENAPEYYMGMGHTAEQVAMKYG 159
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHMlREGWLVEHKPEIYWSMLQTAENVAKRYG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 160 ISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKID-ENNKLREQKLMFSQDEGVRPGTTADVLGKLRPAFSiKG 238
Cdd:PRK07108 161 ISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADkATGRLFTKEVTVSADEGIRPDTTLEGVSKIRSALP-GG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 239 SVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLFELNEAF 318
Cdd:PRK07108 240 VITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504270775 319 ASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFELL 391
Cdd:PRK07108 320 AVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFEVL 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-389 |
1.11e-136 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 396.28 E-value: 1.11e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKkGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEqglnmARNIG---AL-AG 76
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFG-GAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGE-----APAIGrvaALdAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 77 LPYTVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVP-----MFGNVARPNVQL--------VENAPEY 143
Cdd:PRK06205 75 LPVTVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEfyttdMRWGVRGGGVQLhdrlargrETAGGRR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 144 Y---MGMGHTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDEnnklreqkLMFSQDEGVRP 220
Cdd:PRK06205 155 FpvpGGMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDP--------TVVDRDEHPRA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 221 GTTADVLGKLRPAFSIK---GSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPK 297
Cdd:PRK06205 227 DTTLESLAKLRPIMGKQdpeATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 298 ALKLAGLELSDIGLFELNEAFASQALGVIRELNINED---KVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIV 374
Cdd:PRK06205 307 ALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLE 386
|
410
....*....|....*
gi 504270775 375 TMCIGGGMGAAGVFE 389
Cdd:PRK06205 387 TMCIGGGQGLAAVFE 401
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-391 |
1.88e-135 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 392.79 E-value: 1.88e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGkAKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK09051 2 MREVVVVSGVRTAIG-TFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVAR-----PNVQLVE------NAPEYYMGMGH 149
Cdd:PRK09051 81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARwgarmGDAKLVDmmvgalHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 150 TAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDennklreqkLMFSQDEGVRPGTTADVLGK 229
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGE---------VVFDTDEHVRADTTLEDLAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 230 LRPAFSI-KGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSD 308
Cdd:PRK09051 232 LKPVFKKeNGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 309 IGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVF 388
Cdd:PRK09051 312 LDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIF 391
|
...
gi 504270775 389 ELL 391
Cdd:PRK09051 392 ERL 394
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-392 |
9.51e-131 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 381.27 E-value: 9.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKKGSLASVRPDDLGAIAVKETLRRAGGYE-GPIDDLIIGCAMPEAEQGLNMARNIGALAGLPy 79
Cdd:PRK07851 1 MPEAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVPALDpTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 80 TVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMS-FV------------PMFGNVARPNVQLVENA------ 140
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrFAkgnsdslpdtknPLFAEAQARTAARAEGGaeawhd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 141 -------PEYYMGMGHTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVevTLRkidennklreQKLMFS 213
Cdd:PRK07851 160 predgllPDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPV--TLP----------DGTVVS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 214 QDEGVRPGTTADVLGKLRPAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVA 293
Cdd:PRK07851 228 TDDGPRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 294 AIPKALKLAGLELSDIGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGI 373
Cdd:PRK07851 308 ASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGL 387
|
410
....*....|....*....
gi 504270775 374 VTMCIGGGMGAAGVFELLA 392
Cdd:PRK07851 388 ETMCVGGGQGMAMVLERLS 406
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-389 |
1.60e-126 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 369.82 E-value: 1.60e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAK-----KGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALA 75
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIFLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 76 GLPYTVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGN-VARPNVQLVENaPEYY-------MGM 147
Cdd:PRK06445 81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNpHIEPNPKLLTD-PKYIeydlttgYVM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 148 GHTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVtlrkidennKLREQKLMFSQDEGVRPGTTADVL 227
Cdd:PRK06445 160 GLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV---------EVEGKKKVVDVDQSVRPDTSLEKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 228 GKLRPAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELS 307
Cdd:PRK06445 231 AKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 308 DIGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGV 387
Cdd:PRK06445 311 DIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVV 390
|
..
gi 504270775 388 FE 389
Cdd:PRK06445 391 LE 392
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-389 |
5.42e-124 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 363.89 E-value: 5.42e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKkGSLASVRPDDLGAIAVKETLRRAGGYE-GPIDDLIIGCAMPEAEQGLNMARNIGALAGLPY 79
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYG-GALSSVRADDLGAVPLKALMARNPGVDwEAVDDVIYGCANQAGEDNRNVARMSALLAGLPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 80 TVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPM-----------------------FGNVARPNVQL 136
Cdd:PRK09050 80 SVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFvmgkadsafsrqaeifdttigwrFVNPLMKAQYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 137 VENAPEyymgmghTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDennklreqKLMFSQDE 216
Cdd:PRK09050 160 VDSMPE-------TAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGD--------PVVVDRDE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 217 GVRPGTTADVLGKLRPAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIP 296
Cdd:PRK09050 225 HPRPETTLEALAKLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 297 KALKLAGLELSDIGLFELNEAFASQALGVIRELNINED--KVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIV 374
Cdd:PRK09050 305 KLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLADDdaRVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALC 384
|
410
....*....|....*
gi 504270775 375 TMCIGGGMGAAGVFE 389
Cdd:PRK09050 385 TMCIGVGQGIALAIE 399
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-389 |
7.58e-121 |
|
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (TIGR02437). The FadBA complex is the major complex active for beta-oxidation of fatty acids in E. coli. [Fatty acid and phospholipid metabolism, Degradation]
Pssm-ID: 131498 Cd Length: 385 Bit Score: 355.40 E-value: 7.58e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 3 EAVIVAGARTPVGKAKKGSLASVRPDDLGAIAVKETLRRAGGYE-GPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYTV 81
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTRAEDLSAHLMSKLLARNPKVDpAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 82 PAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVaRPNVQLVENAPEYYMGMGHTAEQVAMKYGIS 161
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMHGV-DFHPGMSLHVAKAAGMMGLTAEMLGKMHGIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 162 REDQDAFAVRSHQKAAKALQEGKFNDEIVPVEvtlrKIDENNKLReqklMFSQDEGVRPGTTADVLGKLRPAFSIK-GSV 240
Cdd:TIGR02445 160 REQQDAFAARSHARAHAATQEGKFKNEIIPTQ----GHDADGFLK----QFDYDEVIRPETTVESLAALRPAFDPKnGTV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 241 TAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLFELNEAFAS 320
Cdd:TIGR02445 232 TAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAA 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504270775 321 QALGVIRELNINE---DKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:TIGR02445 312 QALPCLKDLGLLDkmdEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-389 |
3.17e-120 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 354.19 E-value: 3.17e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKK-GSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPY 79
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKKdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 80 TVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPNVQLVENAPEYYMGMGHTAEQVAMKYG 159
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKYG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 160 ISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEvtlrkiDENNKLreqklMFSQDEGVRPGTTADVLGKLRPAFSIKGS 239
Cdd:PRK08242 161 FSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK------DQNGLT-----ILDHDEHMRPGTTMESLAKLKPSFAMMGE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 240 V---------------------TAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKA 298
Cdd:PRK08242 230 MggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 299 LKLAGLELSDIGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCI 378
Cdd:PRK08242 310 LAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCV 389
|
410
....*....|.
gi 504270775 379 GGGMGAAGVFE 389
Cdd:PRK08242 390 GGGMGIATIIE 400
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-389 |
2.71e-115 |
|
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.
Pssm-ID: 131483 Cd Length: 400 Bit Score: 341.76 E-value: 2.71e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 2 REAVIVAGARTPVGKAKkGSLASVRPDDLGAIAVKETLRRAGGYE-GPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
Cdd:TIGR02430 1 REAYICDAIRTPIGRYG-GSLSSVRADDLAAVPIKALLARNPQLDwAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPNVQLVENAPEYYMG-------------- 146
Cdd:TIGR02430 80 VPGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIEDTTIGwrfinplmkalygv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 147 --MGHTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDEnnklreqkLMFSQDEGVRPGTTA 224
Cdd:TIGR02430 160 dsMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEP--------TVVDQDEHPRPETTL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 225 DVLGKLRPAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGL 304
Cdd:TIGR02430 232 EGLAKLKPVVRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 305 ELSDIGLFELNEAFASQALGVIRELNINED--KVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGM 382
Cdd:TIGR02430 312 SIDQFDVIELNEAFAAQALAVLRELGLADDdaRVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQ 391
|
....*..
gi 504270775 383 GAAGVFE 389
Cdd:TIGR02430 392 GIALAIE 398
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-385 |
4.87e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 333.01 E-value: 4.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGkAKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK05656 1 MQDVVIVAATRTAIG-SFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVL-TAGAGQNPARQAAIKAGLPHS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPNV-----QLVENA---------PEYYMG 146
Cdd:PRK05656 79 VPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLrmghaQLVDSMitdglwdafNDYHMG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 147 MghTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDennklreqKLMFSQDEGVRPGTTADV 226
Cdd:PRK05656 159 I--TAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGE--------PLAFATDEQPRAGTTAES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 227 LGKLRPAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLEL 306
Cdd:PRK05656 229 LAKLKPAFKKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSL 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504270775 307 SDIGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAA 385
Cdd:PRK05656 309 AELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVA 387
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-389 |
4.30e-111 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 330.97 E-value: 4.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKaKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK08131 1 MLDAYIYDGLRSPFGR-HAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVP---------------MFGNV--AR-PNVQLVENape 142
Cdd:PRK08131 80 VPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPfvmgkaesafsrdakVFDTTigARfPNPKIVAQ--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 143 yYMG--MGHTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKidennklREQKLMFSQDEGVRP 220
Cdd:PRK08131 157 -YGNdsMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGR-------KLPPKLVAEDEHPRP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 221 GTTADVLGKLRPAFSiKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALK 300
Cdd:PRK08131 229 SSTVEALTKLKPLFE-GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 301 LAGLELSDIGLFELNEAFASQALGVIRELNI--NEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCI 378
Cdd:PRK08131 308 RAGLTLDDMDIIEINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCI 387
|
410
....*....|.
gi 504270775 379 GGGMGAAGVFE 389
Cdd:PRK08131 388 GVGQGLAMVIE 398
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-385 |
9.06e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 329.75 E-value: 9.06e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKkGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFG-GSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVL-QGGQGQIPSRQAARAAGIPWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPNVQLVENAPEYYM------------GMG 148
Cdd:PRK08235 79 VQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMvadgltcafsgvHMG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 149 HTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDEnnklreqkLMFSQDEGVRPGTTADVLG 228
Cdd:PRK08235 159 VYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDP--------IVVAKDEAPRKDTTIEKLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 229 KLRPAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSD 308
Cdd:PRK08235 231 KLKPVFDKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVED 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504270775 309 IGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAA 385
Cdd:PRK08235 311 IDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDA 387
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-389 |
1.48e-101 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 306.26 E-value: 1.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKaKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK07850 1 MGNPVIVEAVRTPIGK-RNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVArPNVQLVEnAPEYYMGMGH---TAEQVAMK 157
Cdd:PRK07850 80 VGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAG-PGRGLPR-PDSWDIDMPNqfeAAERIAKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 158 YGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLrkIDENNKLREQKLMFSQDEGVRPgTTADVLGKLRPAfsIK 237
Cdd:PRK07850 158 RGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPV--LDEEGQPTGETRLVTRDQGLRD-TTMEGLAGLKPV--LE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 238 GSV-TAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLFELNE 316
Cdd:PRK07850 233 GGIhTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504270775 317 AFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:PRK07850 313 AFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-391 |
3.45e-101 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 305.09 E-value: 3.45e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKaKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK07801 1 MAEAYIVDAVRTPVGK-RKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGN--VARPN---------VQLVENAPEYYMGMGH 149
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAmtAGEQLgftspfaesKGWLHRYGDQEVSQFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 150 TAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEvtlrkidennklreqklMFSQDEGVRPgTTADVLGK 229
Cdd:PRK07801 160 GAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG-----------------GVTVDEGPRE-TSLEKMAG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 230 LRPAFSiKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDI 309
Cdd:PRK07801 222 LKPLVE-GGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 310 GLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:PRK07801 301 DVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380
|
..
gi 504270775 390 LL 391
Cdd:PRK07801 381 RL 382
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-389 |
5.04e-100 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 302.33 E-value: 5.04e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGkAKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK06633 2 TKPVYITHAKRTAFG-SFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVI-TGGSGQNPARQTLIHAGIPKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFV---------PMFGNVARPNVQLVENAPEYYMG--MGH 149
Cdd:PRK06633 80 VPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGmhgsyiragAKFGDIKMVDLMQYDGLTDVFSGvfMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 150 TAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDEnnklreqklMFSQDEGVRPGTTADVLGK 229
Cdd:PRK06633 160 TAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTS---------LFDHDETVRPDTSLEILSK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 230 LRPAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDI 309
Cdd:PRK06633 231 LRPAFDKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 310 GLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:PRK06633 311 EVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.09e-99 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 301.26 E-value: 1.09e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKaKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK06504 1 MAEAYIVAAARTAGGR-KGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPM-----------FGNVARPNVQLVENAPEYYMGMGh 149
Cdd:PRK06504 80 VPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMgspstlpakngLGHYKSPGMEERYPGIQFSQFTG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 150 tAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDENnklreqklMFSQDEGVRPGTTADVLGK 229
Cdd:PRK06504 159 -AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGE--------MHTVDEGIRFDATLEGIAG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 230 LRPaFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDI 309
Cdd:PRK06504 230 VKL-IAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 310 GLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:PRK06504 309 DLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
|
..
gi 504270775 390 LL 391
Cdd:PRK06504 389 RL 390
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-392 |
5.98e-99 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 299.70 E-value: 5.98e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 2 REAVIVAGARTPVGKAKkGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYTV 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFL-GSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVL-SANLGQAPARQAALGAGLPPST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 82 PAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPNVQLVENA------------PEYYMGMGH 149
Cdd:PLN02644 79 ICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTvvdgmlkdglwdVYNDFGMGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 150 TAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKidennklREQKLMFSQDEGVRPgTTADVLGK 229
Cdd:PLN02644 159 CAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGR-------GRPSVIVDKDEGLGK-FDPAKLRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 230 LRPAFSIK-GSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSD 308
Cdd:PLN02644 231 LRPSFKEDgGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 309 IGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVF 388
Cdd:PLN02644 311 VDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVV 390
|
....
gi 504270775 389 ELLA 392
Cdd:PLN02644 391 ELMQ 394
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
2-389 |
2.19e-98 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 299.21 E-value: 2.19e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 2 REAVIVAGARTPVGKAKKgSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIG--CAMPEAeqgLNMARNIGALAGLPY 79
Cdd:PRK08963 5 DRIAIVSGLRTPFAKQAT-AFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGqvVQMPEA---PNIAREIVLGTGMNV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 80 TVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMF-----------GNVARPNVQ------------L 136
Cdd:PRK08963 81 HTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGvskklaralvdLNKARTLGQrlklfsrlrlrdL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 137 VENAP---EYYMG--MGHTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTlrkidennklrEQKLM 211
Cdd:PRK08963 161 LPVPPavaEYSTGlrMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVP-----------PYKQP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 212 FSQDEGVRPGTTADVLGKLRPAFSIK-GSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPP-EVMGI 289
Cdd:PRK08963 230 LEEDNNIRGDSTLEDYAKLRPAFDRKhGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 290 GPVAAIPKALKLAGLELSDIGLFELNEAFASQALGVIRELN-----------------INEDKVNVNGGAIALGHPLGCT 352
Cdd:PRK08963 310 GPAYATPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFAserfareklgrsqaigeVDMSKFNVLGGSIAYGHPFAAT 389
|
410 420 430
....*....|....*....|....*....|....*..
gi 504270775 353 GAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:PRK08963 390 GARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLE 426
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-389 |
1.72e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 289.22 E-value: 1.72e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKKGSlASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQgLNMARNIGALAGLPYT 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGP-GPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDE-ANIARVVALRLGCGEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPM---------FGNVARPN-----VQLVENAPEYY-- 144
Cdd:PRK08170 80 VPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLlfsekmvrwLAGWYAAKsigqkLAALGKLRPSYla 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 145 ---------------MGMGHTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNdEIVPVevtlrkIDENNKLreqk 209
Cdd:PRK08170 160 pvigllrgltdpvvgLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL------FDRDGKF---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 210 lmFSQDEGVRPGTTADVLGKLRPAFSIK-GSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMG 288
Cdd:PRK08170 229 --YDHDDGVRPDSSMEKLAKLKPFFDRPyGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 289 IGPVAAIPKALKLAGLELSDIGLFELNEAFASQALGVIRELN-----------------INEDKVNVNGGAIALGHPLGC 351
Cdd:PRK08170 307 LGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGA 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 504270775 352 TGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:PRK08170 387 SGARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLE 424
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-392 |
1.14e-87 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 269.71 E-value: 1.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 3 EAVIVAGARTPVGKaKKGSLASVRPDDLGAIAVKETLRragGYEGPIDDLIIGCAMpeaEQGLNMARNIGALAGLPYTVP 82
Cdd:PRK06690 2 RAVIVEAKRTPIGK-KNGMLKDYEVQQLAAPLLTFLSK---GMEREIDDVILGNVV---GPGGNVARLSALEAGLGLHIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 83 AITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPmFGNVARPNVQLVENaPEyymgMGHTAEQVAMKYGISR 162
Cdd:PRK06690 75 GVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSP-FQNRARFSPETIGD-PD----MGVAAEYVAERYNITR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 163 EDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLrkiDENNKLReqklmfsqdegvRPgtTADVLGKLRPAFSIKGSVTA 242
Cdd:PRK06690 149 EMQDEYACLSYKRTLQALEKGYIHEEILSFNGLL---DESIKKE------------MN--YERIIKRTKPAFLHNGTVTA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 243 GNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLFELNEAFASQA 322
Cdd:PRK06690 212 GNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKV 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 323 LGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFELLA 392
Cdd:PRK06690 292 VACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKVE 361
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-389 |
4.78e-86 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 267.41 E-value: 4.78e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTP--VGKAKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLP 78
Cdd:PRK06025 1 MAEAYIIDAVRTPrgIGKVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 79 YTVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARP-----------NVQLVENAPEYYMGM 147
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAagkpplgmgsgNLRLRALHPQSHQGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 148 ghTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVevtlrKIDENNklreqkLMFSQDEGVRPGTTADVL 227
Cdd:PRK06025 161 --CGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV-----YRDDGS------VALDHEEFPRPQTTAEGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 228 GKLRPAFS--------------------------IKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGG 281
Cdd:PRK06025 228 AALKPAFTaiadyplddkgttyrglinqkypdleIKHVHHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 282 VPPEVMGIGPVAAIPKALKLAGLELSDIGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLM 361
Cdd:PRK06025 308 DDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVL 387
|
410 420
....*....|....*....|....*...
gi 504270775 362 HEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:PRK06025 388 DELERRGLKRGLVTMCAAGGMAPAIIIE 415
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
5-258 |
1.13e-85 |
|
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: 261.08 E-value: 1.13e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 5 VIVAGARTPVGKaKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCaMPEAEQGLNMARNIGALAGLPYTVPAI 84
Cdd:pfam00108 2 VIVSAARTPFGS-FGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGN-VLQAGEGQNPARQAALKAGIPDSAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 85 TINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPM-----------FGNVARPNVQLVENAPEYYMG--MGHTA 151
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYalptdarsglkHGDEKKHDLLIPDGLTDAFNGyhMGLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 152 EQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKidennklreQKLMFSQDEGVRPGTTADVLGKLR 231
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRK---------GKPTVDKDEGIRPPTTAEPLAKLK 230
|
250 260
....*....|....*....|....*..
gi 504270775 232 PAFSIKGSVTAGNSSQTSDGAASVFLM 258
Cdd:pfam00108 231 PAFDKEGTVTAGNASPINDGAAAVLLM 257
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
5-391 |
6.38e-74 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 235.56 E-value: 6.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 5 VIVAGARTPVGkAKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPeAEQGLNMARNIGALAGLPYTVPAI 84
Cdd:PRK06954 10 VIASAARTPMA-AFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLP-AGQGQAPARQAALGAGLPLSVGCT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 85 TINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPNVQL-------------VENAPEYYMGMGHTA 151
Cdd:PRK06954 88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMghgqvldhmfldgLEDAYDKGRLMGTFA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 152 EQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDennklreqkLMFSQDEGVRPGTTaDVLGKLR 231
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGD---------TVIDRDEQPFKANP-EKIPTLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 232 PAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGL 311
Cdd:PRK06954 238 PAFSKTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 312 FELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFELL 391
Cdd:PRK06954 318 FEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIELI 397
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.26e-72 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 231.82 E-value: 1.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKKgSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGR-SFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVI-QAGVGQNPAGQAAYHAGLPFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 81 VPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVP--------------MFGNVARPNVQLVENAPE--YY 144
Cdd:PRK06366 79 VTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPfllpsdlrwgpkhlLHKNYKIDDAMLVDGLIDafYF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 145 MGMGHTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVEvtlrkidennklreqklMFSQDEGVRPGTTA 224
Cdd:PRK06366 159 EHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN-----------------DLDRDEGIRKTTME 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 225 DvLGKLRPAFSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGL 304
Cdd:PRK06366 222 D-LAKLPPAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 305 ELSDIGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGA 384
Cdd:PRK06366 301 SIDYYDLVEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAH 380
|
....*..
gi 504270775 385 AGVFELL 391
Cdd:PRK06366 381 TLTLEMV 387
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
268-389 |
1.29e-59 |
|
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: 189.01 E-value: 1.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 268 LKPLLKFRSFAVGGVPPEVMGIGPVAAIPKALKLAGLELSDIGLFELNEAFASQALGVIRELNINEDKVNVNGGAIALGH 347
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 504270775 348 PLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-389 |
5.23e-57 |
|
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: 191.55 E-value: 5.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 7 VAGARTPVGK--AKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEqGLNMARNIGALAGLPYTVPAI 84
Cdd:cd00826 1 AGAAMTAFGKfgGENGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGE-GQNCAQQAAMHAGGLQEAPAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 85 TINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMfgnvarpnvqlvENAPEYYMgmghtaEQVAMKYGiSRED 164
Cdd:cd00826 80 GMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAE------------NNAKEKHI------DVLINKYG-MRAC 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 165 QDAFAVRSHQKAAKALQEGKFNDEIVPVEVTLRKIDENNklreqklmfSQDEGVRPGTTA--DVLGKLRPAFSIKGSVTA 242
Cdd:cd00826 141 PDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHS---------DADEYIQFGDEAslDEIAKLRPAFDKEDFLTA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 243 GNSSQTSDGAASVFLMDKE-------QAEAEGLKPLLKFRSFAVGGVPPE----VMGIGPVAAIPKALKLAGLELSDIGL 311
Cdd:cd00826 212 GNACGLNDGAAAAILMSEAeaqkhglQSKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 312 FELNEAFASQALGVIRELNINEDK------------------VNVNGGAIALGHPLGCTGAKLTLSLMHEMQRRNEQF-- 371
Cdd:cd00826 292 IEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRqg 371
|
410 420
....*....|....*....|.
gi 504270775 372 ---GIVTMCIGGGMGAAGVFE 389
Cdd:cd00826 372 agaGLALLCIGGGGGAAMCIE 392
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
78-389 |
3.90e-52 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 179.33 E-value: 3.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 78 PYTvPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPM-FG----------NVARPNVQLVE-------- 138
Cdd:PRK09268 82 PYT-PAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIaVNeglrkillelNRAKTTGDRLKalgklrpk 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 139 --------NA-PEYYMGMGHTAEQVAMKYGISREDQDAFAVRSHQKAAKALQEGKFNDEIVPVevtlrkidennklreqk 209
Cdd:PRK09268 161 hlapeiprNGePRTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF----------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 210 LMFSQDEGVRPGTTADVLGKLRPAF--SIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVP---- 283
Cdd:PRK09268 224 LGLTRDNNLRPDSSLEKLAKLKPVFgkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhg 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 284 PEVMGIGPVAAIPKALKLAGLELSDIGLFELNEAFASQ----------------ALGVIREL-NINEDKVNVNGGAIALG 346
Cdd:PRK09268 304 KEGLLMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQvlatlkawedeeycreRLGLDAPLgSIDRSKLNVNGSSLAAG 383
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 504270775 347 HPLGCTGAKLTLSLMHEMQRRNEQFGIVTMCIGGGMGAAGVFE 389
Cdd:PRK09268 384 HPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILE 426
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
14-388 |
2.68e-20 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 91.17 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 14 VGKAKKGSLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGCAMPEAEQGlNMARNIGALAGLPYtVPAITINRYCSSG 93
Cdd:cd00829 3 VGMTPFGRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQS-FPGALIAEYLGLLG-KPATRVEAAGASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 94 LQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFGNVARPNVQLVENAPEYYMGMGHTAeQVAM-------KYGISREDQD 166
Cdd:cd00829 81 SAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPPGGLTPPA-LYALaarrymhRYGTTREDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 167 AFAVRSHQKAA---KALqegkFNDEIVPVEVtlrkidENNKLreqklmfsqdegvrpgtTADVLGKLrpafsikgsvtag 243
Cdd:cd00829 160 KVAVKNHRNAArnpYAQ----FRKPITVEDV------LNSRM-----------------IADPLRLL------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 244 NSSQTSDGAASVFLMDKEQAEAEGLKP-LLKFRSFAVGGVPPEVMGI-----GPVAAIPKALKLAGLELSDIGLFELNEA 317
Cdd:cd00829 200 DCCPVSDGAAAVVLASEERARELTDRPvWILGVGAASDTPSLSERDDflsldAARLAARRAYKMAGITPDDIDVAELYDC 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 318 F------ASQALG---------VIRELNINED---KVNVNGGAIALGHPLGCTG----AKLTLSLMHE---MQRRNEQFG 372
Cdd:cd00829 280 FtiaellALEDLGfcekgeggkLVREGDTAIGgdlPVNTSGGLLSKGHPLGATGlaqaVEAVRQLRGEagaRQVPGARVG 359
|
410
....*....|....*.
gi 504270775 373 IVTMciGGGMGAAGVF 388
Cdd:cd00829 360 LAHN--IGGTGSAAVV 373
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
242-387 |
3.16e-13 |
|
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: 69.01 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 242 AGNSSQTSDGAASVFLMDKEQAEAEGLKPLLKFRSFAVGGVPPE----VMGIGPVAAIPKALKLAGLELSDIGLFELNEA 317
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 318 FASQALGVIRELNINEDKV---NVNGGAIALGHPLGCTG----AKLTLSLMHEM---QRRNEQFGIVTMCIGGGMGAAGV 387
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGlailDELLLMLEHEFippTPREPRTVLLLGFGLGGTNAAVV 253
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-363 |
1.60e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 62.22 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKAKKGSLAsvrpdDLGAIAVKETLRRAGGYEGPIDDLIIGcampeaeqglNMAR-------NIGA 73
Cdd:PRK06064 1 MRDVAIIGVGQTKFGELWDVSLR-----DLAVEAGLEALEDAGIDGKDIDAMYVG----------NMSAglfvsqeHIAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 74 L----AGLPYtVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVP------MFGNVArpNVQLVENA--- 140
Cdd:PRK06064 66 LiadyAGLAP-IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPtpdateAIARAG--DYEWEEFFgat 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 141 -PEYYMGMghtAEQVAMKYGISREDQDAFAVRSHQKAAKalqegkfndeivpvevtlrkidenNKlreqKLMFSqdegvR 219
Cdd:PRK06064 143 fPGLYALI---ARRYMHKYGTTEEDLALVAVKNHYNGSK------------------------NP----YAQFQ-----K 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 220 PGTTADVLGKLRPAFSIKgsvtAGNSSQTSDGAASVFLMDKE--------------QAEAEGLKPLLKFRSFAVGGvppe 285
Cdd:PRK06064 187 EITVEQVLNSPPVADPLK----LLDCSPITDGAAAVILASEEkakeytdtpvwikaSGQASDTIALHDRKDFTTLD---- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 286 vmgiGPVAAIPKALKLAGLELSDIGLFELNEAF------ASQALG---------VIRELNINED---KVNVNGGAIALGH 347
Cdd:PRK06064 259 ----AAVVAAEKAYKMAGIEPKDIDVAEVHDCFtiaeilAYEDLGfakkgeggkLAREGQTYIGgdiPVNPSGGLKAKGH 334
|
410 420
....*....|....*....|
gi 504270775 348 PLGCTGAK----LTLSLMHE 363
Cdd:PRK06064 335 PVGATGVSqaveIVWQLRGE 354
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
1-365 |
3.02e-09 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 58.37 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTP-VGKAKKGSLASVRPD----------DLGAIAVKETLRRAG--GYEGPIDDLIIGCAMPE--AEQG- 64
Cdd:PTZ00455 11 AKRVFVVGGHITPfVGKGSPLFIDKKHPDfgkkenktleELLATAIQGTLENTGldGKAALVDKVVVGNFLGElfSSQGh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 65 -----LNMARNIGALAGLPYTvPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAEsmsfvpmfgnvarpnvqlVEN 139
Cdd:PTZ00455 91 lgpaaVGSLGQSGASNALLYK-PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVE------------------VQT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 140 APEYYMGMGHTAEqvAMKYGISREDQDAFAVRSHQKAAKALQE-GKFNDEIVpVEVTLRKIDENNK-----LREQKLMFS 213
Cdd:PTZ00455 152 TVSARVGGDYLAR--AADYRRQRKLDDFTFPCLFAKRMKYIQEhGHFTMEDT-ARVAAKAYANGNKnplahMHTRKLSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 214 QDEGVRPgTTADVLGKLrpafSIKGSVTAGNSSQTSDGAASVFLMDKEQAEAEGLKP----LLKFRSFAVGGV-----PP 284
Cdd:PTZ00455 229 FCTGASD-KNPKFLGNE----TYKPFLRMTDCSQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASGnlyedPP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 285 EVMGI-GPVAAIPKALKLAGLELSDIGLFELNEAFASQALGVIRELNINED------------------KVNVNGGAIAL 345
Cdd:PTZ00455 304 DATRMfTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYghakdlirngatalegriPVNTGGGLLSF 383
|
410 420
....*....|....*....|
gi 504270775 346 GHPLGCTGAKLTLSLMHEMQ 365
Cdd:PTZ00455 384 GHPVGATGVKQIMEVYRQMK 403
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
30-121 |
1.74e-08 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 56.01 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 30 LGAIAVKETLRRAGGYEGPIDD----LIIGCAMPEAEQGLNMARNI---GALAGLPYTVPAITIN--------RY----- 89
Cdd:cd00834 74 FALAAAEEALADAGLDPEELDPerigVVIGSGIGGLATIEEAYRALlekGPRRVSPFFVPMALPNmaagqvaiRLglrgp 153
|
90 100 110
....*....|....*....|....*....|....*....
gi 504270775 90 -------CSSGLQSIAYGAERIMLGQAKAVLAGGAESMS 121
Cdd:cd00834 154 nytvstaCASGAHAIGDAARLIRLGRADVVIAGGAEALI 192
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
30-120 |
2.18e-07 |
|
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: 52.40 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 30 LGAIAVKETLRRAGGYEGPIDD----LIIGCA---MPEAEQGLNMARNIGALAGLPYTVPAITIN--------RY----- 89
Cdd:COG0304 74 YALAAAREALADAGLDLDEVDPdrtgVIIGSGiggLDTLEEAYRALLEKGPRRVSPFFVPMMMPNmaaghvsiRFglkgp 153
|
90 100 110
....*....|....*....|....*....|....*...
gi 504270775 90 -------CSSGLQSIAYGAERIMLGQAKAVLAGGAESM 120
Cdd:COG0304 154 nytvstaCASGAHAIGEAYRLIRRGRADVMIAGGAEAA 191
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-387 |
1.40e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 49.95 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 1 MREAVIVAGARTPVGKakkgsLASVRPDDLGAIAVKETLRRAGGYEGPIDDLIIGC----AMPEAEQGLNMARNIGALAG 76
Cdd:PRK07516 1 MMTASIVGWAHTPFGK-----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHfnagFSPQDFPASLVLQADPALRF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 77 lpytVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVP---MFGNVARPNVQLVE-NAPEYYMGM-GHTA 151
Cdd:PRK07516 76 ----KPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPtaeVGDILLGASYLKEEgDTPGGFAGVfGRIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 152 EQVAMKYGISREDQDAFAVRSHQKAAK---ALQEGKFNDEIVpvevtlRKIDENNKLreqklmfsqdegvrpgttadVLG 228
Cdd:PRK07516 152 QAYFQRYGDQSDALAMIAAKNHANGVAnpyAQMRKDLGFEFC------RTVSEKNPL--------------------VAG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 229 KLRPAfsikgsvtagNSSQTSDGAASVFLMDKEQAEAegLKPLLKFRSFA-VGGVPP---------EvmgiGPVAAIPKA 298
Cdd:PRK07516 206 PLRRT----------DCSLVSDGAAALVLADAETARA--LQRAVRFRARAhVNDFLPlsrrdplafE----GPRRAWQRA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 299 LKLAGLELSDIGLFELNEAF------ASQALG---------VIRELNINED---KVNVNGGAIALGHPLGCTGAKL-TLS 359
Cdd:PRK07516 270 LAQAGVTLDDLSFVETHDCFtiaeliEYEAMGlappgqgarAIREGWTAKDgklPVNPSGGLKAKGHPIGATGVSMhVLA 349
|
410 420 430
....*....|....*....|....*....|....
gi 504270775 360 LMH------EMQRRNEQFGIVTmciggGMGAAGV 387
Cdd:PRK07516 350 AMQltgeagGMQIPGAKLAGVF-----NMGGAAV 378
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
59-127 |
1.48e-03 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 40.50 E-value: 1.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504270775 59 PEAEQGLNMARNIGALAGLPYTVPAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMSFVPMFG 127
Cdd:cd00828 131 PKWMLSPNTVAGWVNILLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSG 199
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
246-363 |
2.31e-03 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 39.67 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 246 SQTSDGAASVFLMDKEQAEAEGLK--------------PLL---KFRSfAVGG--VPPEVMGigpvaAIPKALKLAGLEL 306
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDYADArpiprikgwghrtaPLGleqKLDR-SAGDpyVLPHVRQ-----AVLDAYRRAGVGL 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504270775 307 SDIGLFELNEAFASQALGVIRELNINED------------------KVNVNGGAIALGHPLGCTGAKLTLSLMHE 363
Cdd:PRK06289 294 DDLDGFEVHDCFTPSEYLAIDHIGLTGPgeswkaiengeiaiggrlPINPSGGLIGGGHPVGASGVRMLLDAAKQ 368
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
82-121 |
2.95e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 39.60 E-value: 2.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 504270775 82 PAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMS 121
Cdd:PRK08722 156 PNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKAS 195
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
68-121 |
3.12e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 39.59 E-value: 3.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 504270775 68 ARNIGALAGLPYTVpaITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAESMS 121
Cdd:PRK09116 144 AVNVGLFFGLKGRV--IPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELC 195
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
34-120 |
3.19e-03 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 38.77 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270775 34 AVKETLRRAGGYEGPIDD----LIIGCAMPEAEQGLNMARNIGALAGLPYTV-------------------PAITINRYC 90
Cdd:pfam00109 94 AAWEALEDAGITPDSLDGsrtgVFIGSGIGDYAALLLLDEDGGPRRGSPFAVgtmpsviagrisyflglrgPSVTVDTAC 173
|
90 100 110
....*....|....*....|....*....|
gi 504270775 91 SSGLQSIAYGAERIMLGQAKAVLAGGAESM 120
Cdd:pfam00109 174 SSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
82-119 |
6.78e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 38.23 E-value: 6.78e-03
10 20 30
....*....|....*....|....*....|....*...
gi 504270775 82 PAITINRYCSSGLQSIAYGAERIMLGQAKAVLAGGAES 119
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
|
|
| |
