|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-401 |
0e+00 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 789.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNPSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPHQ 80
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAYGRSQKIEDTTMGWRFINPKLKEMYGV 160
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSRQAEIFDTTIGWRFVNPLMKAQYGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 161 ETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPVVVDTDEHPRASTTLEGLAKLKP 240
Cdd:PRK09050 161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALAKLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 241 VVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVI 320
Cdd:PRK09050 241 VFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 321 ELNEAFAAQALACTRDLGLEDGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIER 400
Cdd:PRK09050 321 ELNEAFAAQGLAVLRQLGLADDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIER 400
|
.
gi 1126528343 401 V 401
Cdd:PRK09050 401 V 401
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-401 |
0e+00 |
|
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: 713.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 2 KNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNPSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPHQV 81
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNPQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 82 PATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAYGRSQKIEDTTMGWRFINPKLKEMYGVE 161
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIEDTTIGWRFINPLMKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 162 TMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPVVVDTDEHPRASTTLEGLAKLKPV 241
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEGLAKLKPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 242 VKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVIE 321
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 322 LNEAFAAQALACTRDLGLEDGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIERV 401
Cdd:TIGR02430 321 LNEAFAAQALAVLRELGLADDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIERV 400
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-401 |
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: 614.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNPsVNWEKVDDVIYGCANQAGeDNRNVGRMSALLAGVPHQ 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAG-LDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAYGRSQKIEDTTmgwrfINPKLKEMYGV 160
Cdd:COG0183 79 VPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPM-----INPGLTDPYTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 161 ETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEpVVVDTDEHPRASTTLEGLAKLKP 240
Cdd:COG0183 154 LSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 241 VVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVI 320
Cdd:COG0183 233 AFKKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 321 ELNEAFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIER 400
Cdd:COG0183 313 EINEAFAAQVLAVLRELGLDP--DKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
.
gi 1126528343 401 V 401
Cdd:COG0183 391 V 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-400 |
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: 574.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 5 YIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNPsVNWEKVDDVIYGCANQAGEdNRNVGRMSALLAGVPHQVPAT 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAG-LDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 85 TLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAYGRsqkieDTTMGWRFINPKLKEMYGVETMP 164
Cdd:cd00751 79 TVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRL-----GLNTLDGMLDDGLTDPFTGLSMG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 165 QTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGePVVVDTDEHPRASTTLEGLAKLKPVVKA 244
Cdd:cd00751 154 ITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKG-PVVVDRDEGPRPDTTLEKLAKLKPAFKK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 245 DGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVIELNE 324
Cdd:cd00751 233 DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126528343 325 AFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIER 400
Cdd:cd00751 313 AFAAQALACLKELGLDP--EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-401 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 545.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEdNRNVGRMSALLAGVPHQ 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERA-GVPPEQVDEVIMGQVLQAGA-GQNPARQAALKAGLPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAYGR-SQKIEDTtmgwrFINPKLKEMYG 159
Cdd:PRK05790 79 VPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMgDVELVDT-----MIHDGLTDAFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 160 VETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPVVVDTDEHPRASTTLEGLAKLK 239
Cdd:PRK05790 154 GYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 240 PVVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDV 319
Cdd:PRK05790 234 PAFDKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 320 IELNEAFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIE 399
Cdd:PRK05790 314 IEINEAFAAQALAVEKELGLDP--EKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVE 391
|
..
gi 1126528343 400 RV 401
Cdd:PRK05790 392 RP 393
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-401 |
0e+00 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 518.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNPSVNwEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPHQ 80
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPG-DDIEDVILGCTNQAGEDSRNVARNALLLAGLPVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAYGRSQKIEDTTMGWRFINPKLKEMYGV 160
Cdd:PRK08131 80 VPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTTIGARFPNPKIVAQYGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 161 ETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQ-RKGEPVVVDTDEHPRASTTLEGLAKLK 239
Cdd:PRK08131 160 DSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgRKLPPKLVAEDEHPRPSSTVEALTKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 240 PVVkADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDV 319
Cdd:PRK08131 240 PLF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 320 IELNEAFAAQALACTRDLGLEDGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIE 399
Cdd:PRK08131 319 IEINEAFASQVLGCLKGLGVDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
..
gi 1126528343 400 RV 401
Cdd:PRK08131 399 RV 400
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-399 |
1.06e-172 |
|
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: 487.12 E-value: 1.06e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 6 IIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNPsVNWEKVDDVIYGCANQAGEDNrNVGRMSALLAGVPHQVPATT 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNP-LDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAYT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 86 LNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAYGRSQKIEDTTMgwrfINPKLKEMYGVETMPQ 165
Cdd:TIGR01930 79 VNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEDA----RLKDLTDANTGLPMGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 166 TAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGePVVVDTDEHPRASTTLEGLAKLKPVVKAD 245
Cdd:TIGR01930 155 TAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKG-PVTVSSDEGIRPNTTLEKLAKLKPAFDPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 246 GTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVIELNEA 325
Cdd:TIGR01930 234 GTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEA 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126528343 326 FAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIE 399
Cdd:TIGR01930 314 FAAQVLACIKELGLDL--EKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-401 |
7.48e-153 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 437.09 E-value: 7.48e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGL-APVRADDLGAIPIQALMERNPSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPH 79
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAfRNVRAEDLSAHLMRSLLARNPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 80 QVPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSesaygrsqkiedttmgwrfINPKLKEMYG 159
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGVD-------------------FHPGLSKNVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 160 VET--MPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPVVVDTDEHPRASTTLEGLAK 237
Cdd:PRK08947 142 KAAgmMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 238 LKPVVK-ADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQ 316
Cdd:PRK08947 222 LRPAFDpVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 317 MDVIELNEAFAAQALACTRDLGLEDGA-AKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIA 395
Cdd:PRK08947 302 IDVFELNEAFAAQSLPCLKDLGLLDKMdEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIA 381
|
....*.
gi 1126528343 396 LIIERV 401
Cdd:PRK08947 382 TVFERV 387
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-401 |
6.61e-150 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 429.76 E-value: 6.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPHQ 80
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARA-GVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAygrsQKIEDTTMgwrfinpkLKEMYGV 160
Cdd:PRK09051 81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWG----ARMGDAKL--------VDMMVGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 161 ET-------MPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEpVVVDTDEHPRASTTLE 233
Cdd:PRK09051 149 LHdpfgtihMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGE-VVFDTDEHVRADTTLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 234 GLAKLKPVVKAD-GTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGL 312
Cdd:PRK09051 228 DLAKLKPVFKKEnGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 313 TLEQMDVIELNEAFAAQALACTRDLGLEdgAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQ 392
Cdd:PRK09051 308 TVADLDVIEANEAFAAQACAVTRELGLD--PAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQ 385
|
....*....
gi 1126528343 393 GIALIIERV 401
Cdd:PRK09051 386 GIAAIFERL 394
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-401 |
2.14e-147 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 423.63 E-value: 2.14e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEdNRNVGRMSALLAGVPHQ 80
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERT-GIDPARIDDVIFGQGYPNGE-APAIGRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPF--------VMGKSESAYGRSQKIEDTTMGWRFinp 152
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFyttdmrwgVRGGGVQLHDRLARGRETAGGRRF--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 153 klkemyGVET-MPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPVVVDTDEHPRASTT 231
Cdd:PRK06205 156 ------PVPGgMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 232 LEGLAKLKPV---VKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLA 308
Cdd:PRK06205 230 LESLAKLRPImgkQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 309 QTGLTLEQMDVIELNEAFAAQALACTRDLGL-EDGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMC 387
Cdd:PRK06205 310 RAGLTLDDIDLIELNEAFAAQVLAVLKEWGFgADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMC 389
|
410
....*....|....
gi 1126528343 388 IGVGQGIALIIERV 401
Cdd:PRK06205 390 IGGGQGLAAVFERV 403
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-401 |
3.10e-145 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 418.25 E-value: 3.10e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYA-GGLAPVRADDLGAIPIQALMERNPSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPH 79
Cdd:PRK09052 5 LQDAYIVAATRTPVGKAPrGMFKNTRPDDLLAHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 80 QVPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFvMGKSESaygrsqkiedttmgwrfINPKLKEM-- 157
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM-MGNKPS-----------------MSPAIFARde 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 158 -----YGvetMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRK-----GEPVV----VDTD 223
Cdd:PRK09052 147 nvgiaYG---MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatGEVDVktrtVDLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 224 EHPRASTTLEGLAKLKPVVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAI 303
Cdd:PRK09052 224 EGPRADTSLEGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 304 KKLLAQTGLTLEQMDVIELNEAFAAQALACTRDLGLEdgAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYAL 383
Cdd:PRK09052 304 PAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLD--PSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGM 381
|
410
....*....|....*...
gi 1126528343 384 CSMCIGVGQGIALIIERV 401
Cdd:PRK09052 382 VTMCVGTGMGAAGIFERL 399
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-400 |
5.12e-132 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 384.74 E-value: 5.12e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGR-YAGGLAPVRADDLGAIPIQALMERNPSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPH 79
Cdd:PRK07851 1 MPEAVIVSTARSPIGRaFKGSLKDMRPDDLAAQMVRAALDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 80 qVPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRapFVMGKSES-----------AYGRSQKI-EDTTMGW 147
Cdd:PRK07851 81 -LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSR--FAKGNSDSlpdtknplfaeAQARTAARaEGGAEAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 148 RfiNPK----LKEMYgvETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPqrkgEPVVVDTD 223
Cdd:PRK07851 158 H--DPRedglLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP----DGTVVSTD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 224 EHPRASTTLEGLAKLKPVVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAI 303
Cdd:PRK07851 230 DGPRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEAS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 304 KKLLAQTGLTLEQMDVIELNEAFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYAL 383
Cdd:PRK07851 310 KQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDE--DKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGL 387
|
410
....*....|....*..
gi 1126528343 384 CSMCIGVGQGIALIIER 400
Cdd:PRK07851 388 ETMCVGGGQGMAMVLER 404
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-401 |
7.10e-126 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 368.27 E-value: 7.10e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPHQ 80
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRT-GIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPfvMGKSESA---YGRSQKIEDTTmGWRfinpklkEM 157
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTAgeqLGFTSPFAESK-GWL-------HR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 158 YGVETMPQ--TAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVvipqrkgEPVVVDtdEHPRaSTTLEGL 235
Cdd:PRK07801 150 YGDQEVSQfrGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV-------GGVTVD--EGPR-ETSLEKM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 236 AKLKPVVKaDGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLE 315
Cdd:PRK07801 220 AGLKPLVE-GGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSID 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 316 QMDVIELNEAFAAQALACTRDLGLEdgAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIA 395
Cdd:PRK07801 299 DIDVVEINEAFAPVVLAWLKETGAD--PAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANV 376
|
....*.
gi 1126528343 396 LIIERV 401
Cdd:PRK07801 377 TIIERL 382
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-401 |
3.49e-125 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 367.29 E-value: 3.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGR--YAGGLAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVP 78
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKgkKDGSLHEVKPVRLAAGLLEALRDRN-GLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 79 HQVPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPfvMGKSESAYgrsqkiedttmgwrFINPKLKemY 158
Cdd:PRK08242 80 ETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP--MGSDGGAW--------------AMDPSTN--F 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 159 GVETMPQ--TAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVipQRKGEpVVVDTDEHPRASTTLEGLA 236
Cdd:PRK08242 142 PTYFVPQgiSADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK--DQNGL-TILDHDEHMRPGTTMESLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 237 KLKPVVKADGTV---------------------TAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIM 295
Cdd:PRK08242 219 KLKPSFAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 296 GFGPAPAIKKLLAQTGLTLEQMDVIELNEAFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLE 375
Cdd:PRK08242 299 LTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPH--DKVNVNGGAIAMGHPLGATGAMILGTVLDELE 376
|
410 420
....*....|....*....|....*.
gi 1126528343 376 ATGGKYALCSMCIGVGQGIALIIERV 401
Cdd:PRK08242 377 RRGKRTALITLCVGGGMGIATIIERV 402
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-401 |
1.71e-124 |
|
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: 365.03 E-value: 1.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 3 NAYIIDAIRTPFGRYAGGL-APVRADDLGAIPIQALMERNPSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPHQV 81
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAfRNTRAEDLSAHLMSKLLARNPKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 82 PATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKsesaygrsqkieDTTMGWRFINPKLKEMYGVe 161
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMHGV------------DFHPGMSLHVAKAAGMMGL- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 162 tmpqTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPVVVDTDEHPRASTTLEGLAKLKPV 241
Cdd:TIGR02445 148 ----TAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 242 VK-ADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVI 320
Cdd:TIGR02445 224 FDpKNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 321 ELNEAFAAQALACTRDLGLEDGA-AKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIE 399
Cdd:TIGR02445 304 ELNEAFAAQALPCLKDLGLLDKMdEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
|
..
gi 1126528343 400 RV 401
Cdd:TIGR02445 384 RV 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-399 |
9.78e-123 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 360.57 E-value: 9.78e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERnPSVNWEKVDDVIYGCANQAGEdNRNVGRMSALLAGVPHQ 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALER-ANVSAEDVEEVIMGTVLQGGQ-GQIPSRQAARAAGIPWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAYgrsqKIEDTTMGWRFINPKLKEMYGV 160
Cdd:PRK08235 79 VQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGY----RMGDNEVIDLMVADGLTCAFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 161 ETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPVVVDTDEHPRASTTLEGLAKLKP 240
Cdd:PRK08235 155 VHMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 241 VVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVI 320
Cdd:PRK08235 235 VFDKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLF 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126528343 321 ELNEAFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIE 399
Cdd:PRK08235 315 EINEAFAAVALASTEIAGIDP--EKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-401 |
2.12e-120 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 354.80 E-value: 2.12e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGG------LAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEDNRNVGRMSALL 74
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKT-GIKPEEIDDIITGCALQVGENWLYGGRHPIFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 75 AGVPHQVPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPfvMGKSESAygrsqKIEDTTMgwrfINPKL 154
Cdd:PRK06445 80 ARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP--MGDNPHI-----EPNPKLL----TDPKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 155 KEmYGVET---MPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIpQRKGEPVVVDTDEHPRASTT 231
Cdd:PRK06445 149 IE-YDLTTgyvMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-EVEGKKKVVDVDQSVRPDTS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 232 LEGLAKLKPVVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTG 311
Cdd:PRK06445 227 LEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 312 LTLEQMDVIELNEAFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVG 391
Cdd:PRK06445 307 LSVKDIDLWEINEAFAVVVLYAIKELGLDP--ETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGG 384
|
410
....*....|
gi 1126528343 392 QGIALIIERV 401
Cdd:PRK06445 385 QGGAVVLERV 394
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-400 |
1.68e-118 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 349.96 E-value: 1.68e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEdNRNVGRMSALLAGVPHQ 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQT-GLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLPHS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAygrsQKIEDTTMGWRFINPKLKEMYGV 160
Cdd:PRK05656 79 VPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTG----LRMGHAQLVDSMITDGLWDAFND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 161 ETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPVVVDTDEHPRASTTLEGLAKLKP 240
Cdd:PRK05656 155 YHMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 241 VVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVI 320
Cdd:PRK05656 235 AFKKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 321 ELNEAFAAQALACTRDLGLEdgAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIER 400
Cdd:PRK05656 315 EANEAFAAQSLAVGKELGWD--AAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-401 |
5.64e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 333.26 E-value: 5.64e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYA-GGLAPVRADDLGAIPIQALMERnpSVNWE-KVDDVIYGCANQAGEDNRNVGRMSALLAGVP 78
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKR--AGNYEgPIDDLIIGCAMPEAEQGLNMARNIGALAGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 79 HQVPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPfvmgksesaygrsqkiedttMGWRFI--NPKLke 156
Cdd:PRK07661 79 YTVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVP--------------------MMGHVVrpNPRL-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 157 mygVETMPQ-------TAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQR--------KGEPVVVD 221
Cdd:PRK07661 137 ---VEAAPEyymgmghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRtvgennklQEETITFS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 222 TDEHPRASTTLEGLAKLKPVVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAP 301
Cdd:PRK07661 214 QDEGVRADTTLEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 302 AIKKLLAQTGLTLEQMDVIELNEAFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKY 381
Cdd:PRK07661 294 AIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDE--EKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQF 371
|
410 420
....*....|....*....|
gi 1126528343 382 ALCSMCIGVGQGIALIIERV 401
Cdd:PRK07661 372 GIVTMCIGGGMGAAGVFELL 391
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-401 |
7.34e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 333.91 E-value: 7.34e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNPsVNWEKVDDVIYGCANQaGEDNRNVGRMSALLAGVPHQ 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQP-FAPDDLDEVILGCAMP-SPDEANIARVVALRLGCGEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFV--------MGKSESAYGRSQKIED-TTMGWRFIN 151
Cdd:PRK08170 80 VPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLfsekmvrwLAGWYAAKSIGQKLAAlGKLRPSYLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 152 PKLKEMYGVE------TMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKnEIVPVVipQRKGEpvVVDTDEH 225
Cdd:PRK08170 160 PVIGLLRGLTdpvvglNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLF--DRDGK--FYDHDDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 226 PRASTTLEGLAKLKPVV-KADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIK 304
Cdd:PRK08170 235 VRPDSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 305 KLLAQTGLTLEQMDVIELNEAFAAQALACTR----------DLGLEDGA-----AKVNPNGGAISLGHPLGASGARLVTT 369
Cdd:PRK08170 315 PLLQRHGLTLEDLDLWEINEAFAAQVLACLAawadeeycreQLGLDGALgeldrERLNVDGGAIALGHPVGASGARIVLH 394
|
410 420 430
....*....|....*....|....*....|..
gi 1126528343 370 ALNQLEATGGKYALCSMCIGVGQGIALIIERV 401
Cdd:PRK08170 395 LLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
6-400 |
1.04e-106 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 321.71 E-value: 1.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 6 IIDAIRTPFGRYA-GGLAPVRADDLGAIPIQALMERNPsVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPHQVPAT 84
Cdd:PLN02287 50 IVAAYRTPICKAKrGGFKDTYPDDLLAPVLKAVVEKTG-LNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 85 TLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPfvmgksesaygrsqkiedttMGWRF-INPKLKEMYGVET- 162
Cdd:PLN02287 129 TVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNP--------------------MAWEGgVNPRVESFSQAQDc 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 163 ---MPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPV----VIPQRKGE-PVVVDTDEHPRASTTLEG 234
Cdd:PLN02287 189 llpMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkiVDPKTGEEkPIVISVDDGIRPNTTLAD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 235 LAKLKPVVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKprakIIGA----TVVGVEPRIMGFGPAPAIKKLLAQT 310
Cdd:PLN02287 269 LAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLP----ILGVfrsfAAVGVDPAVMGIGPAVAIPAAVKAA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 311 GLTLEQMDVIELNEAFAAQALACTRDLGLEdgAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATG--GKYALCSMCI 388
Cdd:PLN02287 345 GLELDDIDLFEINEAFASQFVYCCKKLGLD--PEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCI 422
|
410
....*....|..
gi 1126528343 389 GVGQGIALIIER 400
Cdd:PLN02287 423 GTGMGAAAVFER 434
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-401 |
5.77e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 307.43 E-value: 5.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPHQ 80
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRS-GADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPfvMGKSesaygrSQKIEDTTMGwRFINPKLKEMYGV 160
Cdd:PRK06504 80 VPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP--MGSP------STLPAKNGLG-HYKSPGMEERYPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 161 ETMPQ--TAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPVVVDTDEHPRASTTLEGLAKL 238
Cdd:PRK06504 151 IQFSQftGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 239 KPVVKaDGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMD 318
Cdd:PRK06504 231 KLIAE-GGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDID 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 319 VIELNEAFAAQALACTRDLGLEdgAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALII 398
Cdd:PRK06504 310 LYEVNEAFASVPLAWLKATGAD--PERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIV 387
|
...
gi 1126528343 399 ERV 401
Cdd:PRK06504 388 ERL 390
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-401 |
9.38e-102 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 307.02 E-value: 9.38e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 2 KNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNPsVNWEKVDDVIYG---CAN--QAGednrnvGRMSALLAG 76
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAG-VDPALVQEVFFGnvlSANlgQAP------ARQAALGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 77 VPHQVPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSEsaygRSQKIEDTTMGWRFINPKLKE 156
Cdd:PLN02644 74 LPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEAR----KGSRLGHDTVVDGMLKDGLWD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 157 MYGVETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKG-EPVVVDTDEHPrASTTLEGL 235
Cdd:PLN02644 150 VYNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGrPSVIVDKDEGL-GKFDPAKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 236 AKLKPVVKAD-GTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTL 314
Cdd:PLN02644 229 RKLRPSFKEDgGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 315 EQMDVIELNEAFAAQALACTRDLGLEdgAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGI 394
Cdd:PLN02644 309 SQVDYYEINEAFSVVALANQKLLGLD--PEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGAS 386
|
....*..
gi 1126528343 395 ALIIERV 401
Cdd:PLN02644 387 AIVVELM 393
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-401 |
1.97e-100 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 303.57 E-value: 1.97e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERnPSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPHQ 80
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDR-AGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAYGRSQKIEDTTMGWRFinpklkemygv 160
Cdd:PRK07850 80 VGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPRPDSWDIDMPNQF----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 161 etmpQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIP------QRKGEPVVVDTDEHPRaSTTLEG 234
Cdd:PRK07850 149 ----EAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPvldeegQPTGETRLVTRDQGLR-DTTMEG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 235 LAKLKPVVKaDGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTL 314
Cdd:PRK07850 224 LAGLKPVLE-GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 315 EQMDVIELNEAFAAQALACTRDLGLEdgAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGI 394
Cdd:PRK07850 303 GDIDLVEINEAFASVVLSWAQVHEPD--MDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALST 380
|
....*..
gi 1126528343 395 ALIIERV 401
Cdd:PRK07850 381 GTIIERI 387
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-401 |
3.99e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 297.71 E-value: 3.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMErNPSVNWEKVDDVIYGCANQAGEDnRNVGRMSALLAGVPHQ 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQ-NSKIDPALVNEVILGQVITGGSG-QNPARQTLIHAGIPKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSrapfvMGKSESAYGRSQKIEDTTMGWRFINPKLKEMYGV 160
Cdd:PRK06633 80 VPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMS-----LGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 161 ETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPVVvDTDEHPRASTTLEGLAKLKP 240
Cdd:PRK06633 155 VFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLF-DHDETVRPDTSLEILSKLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 241 VVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVI 320
Cdd:PRK06633 234 AFDKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 321 ELNEAFAAQALACTRDLGLEdgAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIER 400
Cdd:PRK06633 314 EVNEAFAAQSIYVNREMKWD--MEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
|
.
gi 1126528343 401 V 401
Cdd:PRK06633 392 V 392
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-399 |
3.25e-97 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 295.53 E-value: 3.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGR-YAGGLAPVRADDLGAIPIQALMERnPSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGVPH 79
Cdd:PRK07108 1 MTEAVIVSTARTPLAKsWRGAFNMTHGATLGGHVVQHAVER-AKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 80 QVPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSEsaygrsqkiedTTMGWrfINPKLKEMYG 159
Cdd:PRK07108 80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHM-----------LREGW--LVEHKPEIYW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 160 veTMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEP---------VVVDTDEHPRAST 230
Cdd:PRK07108 147 --SMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKatgrlftkeVTVSADEGIRPDT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 231 TLEGLAKLKPVVKAdGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQT 310
Cdd:PRK07108 225 TLEGVSKIRSALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 311 GLTLEQMDVIELNEAFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGV 390
Cdd:PRK07108 304 GLKVDDIDLWELNEAFAVQVLYCRDTLGIPM--DRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGG 381
|
....*....
gi 1126528343 391 GQGIALIIE 399
Cdd:PRK07108 382 GQGAAGLFE 390
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-401 |
9.32e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 295.15 E-value: 9.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFG---RYAGGLAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEDNRNVGRMSALLAGV 77
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERN-GLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 78 PHQVPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPfVMGKSESAYGRSQKIEDTTmgwrfiNPKLKEM 157
Cdd:PRK06025 80 DIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTA-AMAAEDMAAGKPPLGMGSG------NLRLRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 158 YgvetmPQT-----AENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVipqRKGEPVVVDTDEHPRASTTL 232
Cdd:PRK06025 153 H-----PQShqgvcGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY---RDDGSVALDHEEFPRPQTTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 233 EGLAKLKPVVKA-------DGTVT-------------------AGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGAT 286
Cdd:PRK06025 225 EGLAALKPAFTAiadypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 287 VVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVIELNEAFAAQALACTRDLGLEdgAAKVNPNGGAISLGHPLGASGARL 366
Cdd:PRK06025 305 NMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLD--RDKVNVNGGAIALGHPIGATGSIL 382
|
410 420 430
....*....|....*....|....*....|....*
gi 1126528343 367 VTTALNQLEATGGKYALCSMCIGVGQGIALIIERV 401
Cdd:PRK06025 383 IGTVLDELERRGLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
5-269 |
3.84e-90 |
|
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: 272.64 E-value: 3.84e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 5 YIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNPsVNWEKVDDVIYGCANQAGEDnRNVGRMSALLAGVPHQVPAT 84
Cdd:pfam00108 2 VIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAG-VDPEDVDEVIVGNVLQAGEG-QNPARQAALKAGIPDSAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 85 TLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMG---KSESAYGRSQKIEDTtmgwrfINPKLKEMYGVE 161
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLL------IPDGLTDAFNGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 162 TMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEPvVVDTDEHPRASTTLEGLAKLKPV 241
Cdd:pfam00108 154 HMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPA 232
|
250 260
....*....|....*....|....*...
gi 1126528343 242 VKADGTVTAGNASGINDGAAALLIASDE 269
Cdd:pfam00108 233 FDKEGTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-401 |
1.35e-87 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 269.71 E-value: 1.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 3 NAYIIDAIRTPFGRYAGGLAPVRADDLGAiPIQALMERNPSvnwEKVDDVIYGCANQAGEdnrNVGRMSALLAGVPHQVP 82
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAA-PLLTFLSKGME---REIDDVILGNVVGPGG---NVARLSALEAGLGLHIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 83 ATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFvmgkSESAYGRSQKIEDTTMGwrfinpklkemygvet 162
Cdd:PRK06690 75 GVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF----QNRARFSPETIGDPDMG---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 163 mpQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPV-------VIPQRKGEPVVvdtdehPRAsttlegl 235
Cdd:PRK06690 135 --VAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFnglldesIKKEMNYERII------KRT------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 236 aklKPVVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLE 315
Cdd:PRK06690 200 ---KPAFLHNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 316 QMDVIELNEAFAAQALACTRDLGLEDGaaKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIA 395
Cdd:PRK06690 277 DIDYFEINEAFASKVVACAKELQIPYE--KLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLA 354
|
....*.
gi 1126528343 396 LIIERV 401
Cdd:PRK06690 355 LLFEKV 360
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
6-399 |
1.60e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 263.29 E-value: 1.60e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 6 IIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERnPSVNWEKVDDVIYGCANQAGEdNRNVGRMSALLAGVPHQVPATT 85
Cdd:PRK06954 11 IASAARTPMAAFQGEFASLTAPQLGAAAIAAAVER-AGLKPEQIDEVVMGCVLPAGQ-GQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 86 LNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAY--GRSQKIEDTTMGwrfinpKLKEMYGV-ET 162
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMrmGHGQVLDHMFLD------GLEDAYDKgRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 163 MPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEpVVVDTDEHPRaSTTLEGLAKLKPVV 242
Cdd:PRK06954 163 MGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGD-TVIDRDEQPF-KANPEKIPTLKPAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 243 KADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVIEL 322
Cdd:PRK06954 241 SKTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126528343 323 NEAFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIE 399
Cdd:PRK06954 321 NEAFAVVTMAAMKEHGLPH--EKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-401 |
3.89e-83 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 259.17 E-value: 3.89e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMErNPSVNWEKVDDVIYGCANQAGEDNRNVGRmSALLAGVPHQ 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVID-DAKLDPALVQEVIMGNVIQAGVGQNPAGQ-AAYHAGLPFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 81 VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMgKSESAYG------RSQKIEDTTMgwrfINPKL 154
Cdd:PRK06366 79 VTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLL-PSDLRWGpkhllhKNYKIDDAML----VDGLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 155 KEMYgVETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVipqrkgepvVVDTDEHPRaSTTLEG 234
Cdd:PRK06366 154 DAFY-FEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------DLDRDEGIR-KTTMED 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 235 LAKLKPVVKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTL 314
Cdd:PRK06366 223 LAKLPPAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 315 EQMDVIELNEAFAAQALACTRDLGLEDgaAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGI 394
Cdd:PRK06366 303 DYYDLVEHNEAFSIASIIVRDQLKIDN--ERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAH 380
|
....*..
gi 1126528343 395 ALIIERV 401
Cdd:PRK06366 381 TLTLEMV 387
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
6-400 |
2.82e-73 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 234.88 E-value: 2.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 6 IIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEdNRNVGRMSALLAGVPHQVPATT 85
Cdd:PRK08963 9 IVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARS-EIDPELIEQLVFGQVVQMPE-APNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 86 LNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAP-FVMGKSESAYGRSQKIEdtTMGWRF-------------IN 151
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPiGVSKKLARALVDLNKAR--TLGQRLklfsrlrlrdllpVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 152 PKLKEMYGVETMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGepvVVDTDEHPRASTT 231
Cdd:PRK08963 165 PAVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ---PLEEDNNIRGDST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 232 LEGLAKLKPVV-KADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGATVVGVEPRI-MGFGPAPAIKKLLAQ 309
Cdd:PRK08963 242 LEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQdMLLGPAYATPLALER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 310 TGLTLEQMDVIELNEAFAAQALACTRDLGLEDGA---------------AKVNPNGGAISLGHPLGASGARLVTTALNQL 374
Cdd:PRK08963 322 AGLTLADLTLIDMHEAFAAQTLANLQMFASERFAreklgrsqaigevdmSKFNVLGGSIAYGHPFAATGARMITQTLHEL 401
|
410 420
....*....|....*....|....*.
gi 1126528343 375 EATGGKYALCSMCIGVGQGIALIIER 400
Cdd:PRK08963 402 RRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
14-399 |
1.91e-63 |
|
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238422 [Multi-domain] Cd Length: 393 Bit Score: 208.50 E-value: 1.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 14 FGRYAGGLAPVRADDLGAIPIQALMERnPSVNWEKVDDVIYGCANQAGEdNRNVGRMSALLAGVPHQVPATTLNRLCGSS 93
Cdd:cd00826 11 FGGENGADANDLAHEAGAKAIAAALEP-AGVAAGAVEEACLGQVLGAGE-GQNCAQQAAMHAGGLQEAPAIGMNNLCGSG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 94 LDAVAMAARTIKAGEAHLIVAGGVESMSrapfvmgksesaygrsqkiedttmgwrfinpklkemygvetmpQTAENVAEQ 173
Cdd:cd00826 89 LRALALAMQLIAGGDANCILAGGFEKME-------------------------------------------TSAENNAKE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 174 FKIN--------REDQDKFAFESQQRTAAAQAKGFFKNEIVPVVIPQRKGEpVVVDTDEHPR--ASTTLEGLAKLKPVVK 243
Cdd:cd00826 126 KHIDvlinkygmRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGD-IHSDADEYIQfgDEASLDEIAKLRPAFD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 244 ADGTVTAGNASGINDGAAALLIASDEAVAEYGLK-------PRAKIIGATVVGVEPR----IMGFGPAPAIKKLLAQTGL 312
Cdd:cd00826 205 KEDFLTAGNACGLNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 313 TLEQMDVIELNEAFAAQALACTRDLGLE----------------DGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEA 376
Cdd:cd00826 285 GIGDLDLIEAHDAFAANACATNEALGLCpegqggalvdrgdntyGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKG 364
|
410 420
....*....|....*....|....*...
gi 1126528343 377 TGGKYA-----LCSMCIGVGQGIALIIE 399
Cdd:cd00826 365 EAGKRQgagagLALLCIGGGGGAAMCIE 392
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
4-400 |
6.25e-63 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 208.22 E-value: 6.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 4 AYIIDAIRTPFGRYAGGLAPVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANQAGEDNrNVGRMSALLAGVPHQVPA 83
Cdd:PRK09268 9 VAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRF-GLQGERLGEVVAGAVLKHSRDF-NLTRECVLGSALSPYTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 84 TTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAYGRSQKIEDTTMGwrfinpKLKEMYGVE-- 161
Cdd:PRK09268 87 YDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLELNRAKTTGD------RLKALGKLRpk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 162 ----------------TMPQTAENVAEQFKINREDQDKFAFESQQRTAAAQAKGFFKNEIVPVvipqrKGepvvVDTDEH 225
Cdd:PRK09268 161 hlapeiprngeprtglSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-----LG----LTRDNN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 226 PRASTTLEGLAKLKPV--VKADGTVTAGNASGINDGAAALLIASDEAVAEYGLKPRAKIIGAT------VVGVEPRIMGf 297
Cdd:PRK09268 232 LRPDSSLEKLAKLKPVfgKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAEtaavdfVHGKEGLLMA- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 298 gPAPAIKKLLAQTGLTLEQMDVIELNEAFAAQALA----------CTRDLGLeDGA------AKVNPNGGAISLGHPLGA 361
Cdd:PRK09268 311 -PAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLAtlkawedeeyCRERLGL-DAPlgsidrSKLNVNGSSLAAGHPFAA 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 1126528343 362 SGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIER 400
Cdd:PRK09268 389 TGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
276-400 |
3.02e-54 |
|
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: 175.52 E-value: 3.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 276 LKPRAKIIGATVVGVEPRIMGFGPAPAIKKLLAQTGLTLEQMDVIELNEAFAAQALACTRDLGLEDgaAKVNPNGGAISL 355
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDP--EKVNVNGGAIAL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1126528343 356 GHPLGASGARLVTTALNQLEATGGKYALCSMCIGVGQGIALIIER 400
Cdd:pfam02803 79 GHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
12-397 |
4.09e-23 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 99.65 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 12 TPFGRYAGglapVRADDLGAIPIQALMERNpSVNWEKVDDVIYGCANqAGEDNRNVGRMSALLAGVPHqVPATTLNRLCG 91
Cdd:cd00829 6 TPFGRRSD----RSPLELAAEAARAALDDA-GLEPADIDAVVVGNAA-GGRFQSFPGALIAEYLGLLG-KPATRVEAAGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 92 SSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESAygrsqkiedTTMGWRFINPklkemYGVETMPQTAENVA 171
Cdd:cd00829 79 SGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRA---------SDLEWEGPEP-----PGGLTPPALYALAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 172 ----EQFKINREDQDKFAfESQQRTAAAQAKGFFKNEIVPVVIpqrKGEPVVVDtdehprasttleglaklkPVVKADgt 247
Cdd:cd00829 145 rrymHRYGTTREDLAKVA-VKNHRNAARNPYAQFRKPITVEDV---LNSRMIAD------------------PLRLLD-- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 248 vtagnASGINDGAAALLIASDEAVAEYGLKPrAKIIGATVV----GVEPRIMGFGPAP---AIKKLLAQTGLTLEQMDVI 320
Cdd:cd00829 201 -----CCPVSDGAAAVVLASEERARELTDRP-VWILGVGAAsdtpSLSERDDFLSLDAarlAARRAYKMAGITPDDIDVA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 321 ELNEAFAAQALACTRDLGL----------------EDGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYALC 384
Cdd:cd00829 275 ELYDCFTIAELLALEDLGFcekgeggklvregdtaIGGDLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVP 354
|
410
....*....|...
gi 1126528343 385 SMCIGVGQGIALI 397
Cdd:cd00829 355 GARVGLAHNIGGT 367
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
250-398 |
2.10e-20 |
|
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: 89.81 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 250 AGNASGINDGAAALLIASDEAVAEYGLKPRAKIIG--ATVVG--VEPRIMGFGPAPAIKKLLAQTGLTLEQMDVIELNEA 325
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVStaATFDGasMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 326 FAAQALACTRDLGLE-DGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKY-------ALCSMCIGVGQGIALI 397
Cdd:cd00327 174 GTPIGDAVELALGLDpDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtpreprtVLLLGFGLGGTNAAVV 253
|
.
gi 1126528343 398 I 398
Cdd:cd00327 254 L 254
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
57-381 |
2.23e-12 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 68.18 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 57 ANQAGEDNRNVGRMSALLAGVPHQ---VPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPfvmGKSESA 133
Cdd:PRK06289 54 GNFFGELFAGQGHLGAMPATVHPAlwgVPASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVP---GDVAAE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 134 Y-GRSQKIEDTTMGWRFINPKlkeMYGvetmpQTAENVAEQFKINREDQDKFA---FESQQRTAAAQAKGFFKNEivpvv 209
Cdd:PRK06289 131 HlGAAAWTGHEGQDARFPWPS---MFA-----RVADEYDRRYGLDEEHLRAIAeinFANARRNPNAQTRGWAFPD----- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 210 ipqrkgePVVVDTDEhprasttleglakLKPVVkaDGTVTAGNASGINDGAAALLIASDEAVAEYGLK---PRAKIIGAT 286
Cdd:PRK06289 198 -------EATNDDDA-------------TNPVV--EGRLRRQDCSQVTDGGAGVVLASDAYLRDYADArpiPRIKGWGHR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 287 VVGV--EPRIMGFGPAP--------AIKKLLAQTGLTLEQMDVIELNEAFAAQALACTRDLGLE---------------- 340
Cdd:PRK06289 256 TAPLglEQKLDRSAGDPyvlphvrqAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHIGLTgpgeswkaiengeiai 335
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1126528343 341 DGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKY 381
Cdd:PRK06289 336 GGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGDY 376
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
66-380 |
3.40e-12 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 67.23 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 66 NVGRMSALLAGVPHqVPATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPfvMGKSESAYGRSQKIE-DTT 144
Cdd:PRK06064 62 HIAALIADYAGLAP-IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVP--TPDATEAIARAGDYEwEEF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 145 MGWRFinPKLKEMYGVETMpqtaenvaEQFKINREDQDKFAFESQqRTAAAQAKGFFKNEIvpvvipqrkgepvvvdtde 224
Cdd:PRK06064 139 FGATF--PGLYALIARRYM--------HKYGTTEEDLALVAVKNH-YNGSKNPYAQFQKEI------------------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 225 hprastTLEGLAKLKPVvkADgTVTAGNASGINDGAAALLIASDEAVAEYGLKP-----------------RAKI--IGA 285
Cdd:PRK06064 189 ------TVEQVLNSPPV--AD-PLKLLDCSPITDGAAAVILASEEKAKEYTDTPvwikasgqasdtialhdRKDFttLDA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 286 TVVgveprimgfgpapAIKKLLAQTGLTLEQMDVIELNEAFAAQALACTRDLGL-EDGAAK---------------VNPN 349
Cdd:PRK06064 260 AVV-------------AAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFaKKGEGGklaregqtyiggdipVNPS 326
|
330 340 350
....*....|....*....|....*....|...
gi 1126528343 350 GGAISLGHPLGASGARLVTTALNQL--EATGGK 380
Cdd:PRK06064 327 GGLKAKGHPVGATGVSQAVEIVWQLrgEAEKGR 359
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
258-380 |
1.02e-11 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 66.08 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 258 DGAAALLIASDEAVAEYGLKPRAKIIG--------ATVVGVEP-RIMGFG-PAPAIKKLLAQTGLTLEQMDVIELNEAFA 327
Cdd:PRK08256 215 CGAAAAIVCSEEFARKHGLDRAVEIVAqamttdtpSTFDGRSMiDLVGYDmTRAAAQQVYEQAGIGPEDIDVVELHDCFS 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126528343 328 AQALACTRDLGL--EDGAAK--------------VNPNGGAISLGHPLGASG----ARLVTtalnQLEATGGK 380
Cdd:PRK08256 295 ANELLTYEALGLcpEGEAEKfiddgdntyggrwvVNPSGGLLSKGHPLGATGlaqcAELTW----QLRGTAGA 363
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
82-383 |
6.07e-09 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 57.60 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 82 PATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPFVMGKSESA----YGRSQKIEDTTMGWRFInpklKEM 157
Cdd:PTZ00455 112 PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSARVGGDYLAraadYRRQRKLDDFTFPCLFA----KRM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 158 ygvetmpqtaENVAEQFKINREDQDKFAFEsqqrtaaAQAKGFfKNEIVPVVIPQRKGEPVVVDTDEHPRasttLEGLAK 237
Cdd:PTZ00455 188 ----------KYIQEHGHFTMEDTARVAAK-------AYANGN-KNPLAHMHTRKLSLEFCTGASDKNPK----FLGNET 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 238 LKPVVKADgtvtagNASGINDGAAALLIASDEAVAEYGLKPR----------AKIIGATVVGVEPRIMGFGPAPAIKKLL 307
Cdd:PTZ00455 246 YKPFLRMT------DCSQVSDGGAGLVLASEEGLQKMGLSPNdsrlveikslACASGNLYEDPPDATRMFTSRAAAQKAL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 308 AQTGLTLEQMDVIELNEAFAAQALACTRDLGLED-GAAK---------------VNPNGGAISLGHPLGASGARLVTTAL 371
Cdd:PTZ00455 320 SMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEyGHAKdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVY 399
|
330
....*....|..
gi 1126528343 372 NQLEATGGKYAL 383
Cdd:PTZ00455 400 RQMKGQCGEYQM 411
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
67-380 |
1.98e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 52.54 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 67 VGRMSALLAGVPHQVPAttlnrLCGSSLDAVAMAARTIKAGEAHLIVAGGVESMSRAPfvMGKSESAYGRSQKIEdttmg 146
Cdd:PRK12578 64 VAEYSGLTGKVPLRVEA-----MCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEVD--TSTSLAIGGRGGNYQ----- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 147 WRFinpklkEMYGVeTMPQT----AENVAEQFKINREDQDKFAFESQqRTAAAQAKGFFKNEIvpvvipqrkgepvvvdt 222
Cdd:PRK12578 132 WEY------HFYGT-TFPTYyalyATRHMAVYGTTEEQMALVSVKAH-KYGAMNPKAHFQKPV----------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 223 dehprastTLEGLAKLK----PVVKADgtvtagnASGINDGAAALLIASDEAVAEYGLKPRAKIIG----ATVVGVEPRI 294
Cdd:PRK12578 187 --------TVEEVLKSRaiswPIKLLD-------SCPISDGSATAIFASEEKVKELKIDSPVWITGigyaNDYAYVARRG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 295 --MGFGPAP-AIKKLLAQTGLTLEQMDVIELNEAFAAQALACTRDLGL----------------EDGAAKVNPNGGAISL 355
Cdd:PRK12578 252 ewVGFKATQlAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFtekgkggkfieegqseKGGKVGVNLFGGLKAK 331
|
330 340
....*....|....*....|....*
gi 1126528343 356 GHPLGASGARLVTTALNQLEATGGK 380
Cdd:PRK12578 332 GHPLGATGLSMIYEITKQLRDEAGK 356
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
254-379 |
6.87e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 51.10 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 254 SGINDGAAALLIASDEAVAEYglkPRAKIIGATV-----VGVEPR-IMGF-GPAPAIKKLLAQTGLTLEQMDVIELNEAF 326
Cdd:PRK07516 213 SLVSDGAAALVLADAETARAL---QRAVRFRARAhvndfLPLSRRdPLAFeGPRRAWQRALAQAGVTLDDLSFVETHDCF 289
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126528343 327 AAQALACTRDLGL----------------EDGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGG 379
Cdd:PRK07516 290 TIAELIEYEAMGLappgqgarairegwtaKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAG 358
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
254-383 |
2.21e-06 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 49.26 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 254 SGINDGAAALLIASDEAVAEYGLKPRAKIIGATVV---GVEPRIMG--FGPAP----AIKKLLAQTGLT--LEQMDVIEL 322
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGKKDPVYVKALQLAvsnGWELQYNGwdGSYFPttriAARKAYREAGITdpREELSMAEV 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126528343 323 NEAFAAQALACTRDLGLE----------------DGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEATGGKYAL 383
Cdd:PRK06157 294 HDCFSITELVTMEDLGLSergqawrdvldgffdaDGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGERQL 370
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
256-363 |
5.23e-06 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 48.15 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 256 INDGAAALLIASDEAVAEYGLKPrakiigATVVGVEPRIMGfgPAPAIKKLL----------AQTGLTLEQMDVIELNEA 325
Cdd:PRK07937 204 ITDGAAAVVLAAGDRARELRERP------AWITGIEHRIES--PSLGARDLTrspstalaaeAATGGDAGGVDVAELHAP 275
|
90 100 110
....*....|....*....|....*....|....*...
gi 1126528343 326 FAAQALACTRDLGLEDgAAKVNPNGGAISlGHPLGASG 363
Cdd:PRK07937 276 FTHQELILREALGLGD-KTKVNPSGGALA-ANPMFAAG 311
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
248-377 |
1.23e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 47.21 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 248 VTAGNASGINDGAAALLIASDEAVAEYGLKP-RAKIIGATVVGVEPRIMGFGPAP------------------------- 301
Cdd:PRK06365 217 LTRLDVCAMSDGAACAILASEDKAFEITDKPvLIKAIGTGSDTLRLADRPFGEVPllpnespddykdlrypgvhsfragr 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 302 -AIKKLLAQTGLT--LEQMDVIELNEAFAAQALACTRDLGL----------------EDGAAKVNPNGGAISLGHPLGAS 362
Cdd:PRK06365 297 mAAKEAYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgkpeLPGKLPVNPSGGLLAAGHAVGAT 376
|
170
....*....|....*
gi 1126528343 363 GARLVTTALNQLEAT 377
Cdd:PRK06365 377 GIMQAVFMFWQLQGR 391
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
67-120 |
2.85e-04 |
|
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: 42.24 E-value: 2.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1126528343 67 VGRMSALLAG-VPHQV----PATTLNRLCGSSLDAVAMAARTIKAGEAHLIVAGGVESM 120
Cdd:pfam00109 145 VGTMPSVIAGrISYFLglrgPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
90-121 |
6.33e-04 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 41.76 E-value: 6.33e-04
10 20 30
....*....|....*....|....*....|..
gi 1126528343 90 CGSSLDAVAMAARTIKAGEAHLIVAGGVESMS 121
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALI 192
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
258-364 |
8.65e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 41.19 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 258 DGAAALLIASdeavAEYGLKPRAKIIGatvvgvepRIMGFG----------PAP-------AIKKLLAQTGLTLEQMDVI 320
Cdd:PRK05952 210 EGGAILVLES----AELAQKRGAKIYG--------QILGFGltcdayhmsaPEPdgksaiaAIQQCLARSGLTPEDIDYI 277
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1126528343 321 -------ELNEAFAAQALactrdlgledgaAKVNPNGGAIS-----LGHPLGASGA 364
Cdd:PRK05952 278 hahgtatRLNDQREANLI------------QALFPHRVAVSstkgaTGHTLGASGA 321
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
90-120 |
1.77e-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: 40.08 E-value: 1.77e-03
10 20 30
....*....|....*....|....*....|.
gi 1126528343 90 CGSSLDAVAMAARTIKAGEAHLIVAGGVESM 120
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAA 191
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
256-376 |
1.91e-03 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 39.93 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 256 INDGAAALLIASDEAVAEYGLKPRAKIIG--ATVVG---VEPRIMGFGPAPAIKKLLAQTGLTLEQMDVIELNEAFAAQA 330
Cdd:cd00825 159 FGDGAGALVVEELEHALARGAHIYAEIVGtaATIDGagmGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIG 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1126528343 331 LACTRDLGL-EDGAAKVNPNGGAISLGHPLGASGARLVTTALNQLEA 376
Cdd:cd00825 239 DVKELKLLRsEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEH 285
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
226-380 |
2.07e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 40.12 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 226 PRAS----TTLEGLAKLKPVVKAdgtVTAGNASGINDGAAALLIASDEAVAEYGLKPR-AKIIGATVVGVEPRIMGFGPA 300
Cdd:PRK06066 179 PRASyasnISLEDVLSSEYVVYP---LTELDIAPFVDGAIVVVLASEEVAKKLTDDPVwIKGIGWSTESSNLETAELGKA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 301 PAIKK--LLA--QTGLTLEQMDV--IELNEAFAAQALACTRDLGL----------------EDGAAKVNPNGGAISLGHP 358
Cdd:PRK06066 256 NYMRIaaDMAykMAGIESPRKEVdaAEVDDRYSYKELQHIEALRLseepekdsllregnfdPQGELPVNPSGGHLAKGVP 335
|
170 180
....*....|....*....|..
gi 1126528343 359 LGASGARLVTTALNQLEATGGK 380
Cdd:PRK06066 336 LEASGLSLLLDAVEYLRGEAGA 357
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
90-119 |
5.12e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 38.62 E-value: 5.12e-03
10 20 30
....*....|....*....|....*....|
gi 1126528343 90 CGSSLDAVAMAARTIKAGEAHLIVAGGVES 119
Cdd:PRK07314 162 CATGAHAIGDAARLIAYGDADVMVAGGAEA 191
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
254-364 |
5.98e-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: 38.67 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 254 SGIN--DGAAALLIASDEAVAEYGLKPRAKIIGATVVG-----VEPRIMGFGPAPAIKKLLAQTGLTLEQMDVI------ 320
Cdd:cd00834 225 DGFVlgEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDYInahgts 304
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1126528343 321 -ELNEAfaAQALACTRDLGLEDGAAKVNPNGGAIslGHPLGASGA 364
Cdd:cd00834 305 tPLNDA--AESKAIKRVFGEHAKKVPVSSTKSMT--GHLLGAAGA 345
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
308-379 |
8.89e-03 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 38.09 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528343 308 AQTGLTLEQMDVIELNEAFAAQALACTRDLG----------LEDGAAK------VNPNGGAISLGHPlGASGARLVTTAL 371
Cdd:PRK06158 265 AMAGLTPADIDVVELYDAFTINTILFLEDLGfcakgeggafVEGGRIApggrlpVNTNGGGLSCVHP-GMYGLFLLIEAV 343
|
....*...
gi 1126528343 372 NQLEATGG 379
Cdd:PRK06158 344 RQLRGEAG 351
|
|
| |
