|
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: 775.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNPSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPYQ 80
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSDSAFGRSQKIEDTTMGWRFINPKLKELYGV 160
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSRQAEIFDTTIGWRFVNPLMKAQYGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 161 DTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVVIDTDEHPRASTTLEALSKLKP 240
Cdd:PRK09050 161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALAKLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 241 VVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVI 320
Cdd:PRK09050 241 VFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 321 ELNEAFAAQALAVTRDLGLPDNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIER 400
Cdd:PRK09050 321 ELNEAFAAQGLAVLRQLGLADDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIER 400
|
.
gi 446709123 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: 696.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 2 KNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNPSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPYQV 81
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNPQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 82 PATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSDSAFGRSQKIEDTTMGWRFINPKLKELYGVD 161
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIEDTTIGWRFINPLMKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 162 TMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVVIDTDEHPRASTTLEALSKLKPV 241
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEGLAKLKPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 242 VKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVIE 321
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 322 LNEAFAAQALAVTRDLGLPDNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIERV 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: 591.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNPsVDWEQVDDVIYGCANQAGeDNRNVGRMSALLAGLPYQ 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAG-LDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSDSAFGRSQKIEDTTmgwrfINPKLKELYGV 160
Cdd:COG0183 79 VPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPM-----INPGLTDPYTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 161 DTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDaVVIDTDEHPRASTTLEALSKLKP 240
Cdd:COG0183 154 LSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 241 VVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVI 320
Cdd:COG0183 233 AFKKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 321 ELNEAFAAQALAVTRDLGLPDnsDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIER 400
Cdd:COG0183 313 EINEAFAAQVLAVLRELGLDP--DKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
.
gi 446709123 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: 549.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 5 YIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNPsVDWEQVDDVIYGCANQAGEdNRNVGRMSALLAGLPYQVPAT 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAG-LDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 85 TINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKsdsafGRSQKIEDTTMGWRFINPKLKELYGVDTMP 164
Cdd:cd00751 79 TVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPK-----ARRGGRLGLNTLDGMLDDGLTDPFTGLSMG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 165 QTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDaVVIDTDEHPRASTTLEALSKLKPVVKA 244
Cdd:cd00751 154 ITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPDTTLEKLAKLKPAFKK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 245 EGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVIELNE 324
Cdd:cd00751 233 DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446709123 325 AFAAQALAVTRDLGLPDnsDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIER 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: 515.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEdNRNVGRMSALLAGLPYQ 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERA-GVPPEQVDEVIMGQVLQAGA-GQNPARQAALKAGLPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSDSAFGR-SQKIEDTtmgwrFINPKLKELYG 159
Cdd:PRK05790 79 VPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMgDVELVDT-----MIHDGLTDAFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 160 VDTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVVIDTDEHPRASTTLEALSKLK 239
Cdd:PRK05790 154 GYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 240 PVVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDV 319
Cdd:PRK05790 234 PAFDKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 320 IELNEAFAAQALAVTRDLGLPDnsDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIE 399
Cdd:PRK05790 314 IEINEAFAAQALAVEKELGLDP--EKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVE 391
|
..
gi 446709123 400 RV 401
Cdd:PRK05790 392 RP 393
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-401 |
1.44e-177 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 500.46 E-value: 1.44e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNPsVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPYQ 80
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSG-FPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSDSAFGRSQKIEDTTMGWRFINPKLKELYGV 160
Cdd:PRK08131 80 VPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTTIGARFPNPKIVAQYGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 161 DTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQ-RKGDAVVIDTDEHPRASTTLEALSKLK 239
Cdd:PRK08131 160 DSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgRKLPPKLVAEDEHPRPSSTVEALTKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 240 PVVkAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDV 319
Cdd:PRK08131 240 PLF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 320 IELNEAFAAQALAVTRDLGLPDNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIE 399
Cdd:PRK08131 319 IEINEAFASQVLGCLKGLGVDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
..
gi 446709123 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 |
6.05e-161 |
|
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: 457.46 E-value: 6.05e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 6 IIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNPsVDWEQVDDVIYGCANQAGEDNrNVGRMSALLAGLPYQVPATT 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNP-LDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAYT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 86 INRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSDSAFGRSQKIEdttmgwrFINPKLKELYGVDT--- 162
Cdd:TIGR01930 79 VNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAE-------LEDARLKDLTDANTglp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 163 MPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDaVVIDTDEHPRASTTLEALSKLKPVV 242
Cdd:TIGR01930 152 MGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGP-VTVSSDEGIRPNTTLEKLAKLKPAF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 243 KAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVIEL 322
Cdd:TIGR01930 231 DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEI 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446709123 323 NEAFAAQALAVTRDLGLPDnsDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIE 399
Cdd:TIGR01930 311 NEAFAAQVLACIKELGLDL--EKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-401 |
4.12e-145 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 417.82 E-value: 4.12e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPYQ 80
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARA-GVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMgkSDSAFGrsQKIEDTTMgwrfINPKLKEL--- 157
Cdd:PRK09051 81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLL--PAARWG--ARMGDAKL----VDMMVGALhdp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 158 YGVDTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDaVVIDTDEHPRASTTLEALSK 237
Cdd:PRK09051 153 FGTIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGE-VVFDTDEHVRADTTLEDLAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 238 LKPVVKAE-GTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQ 316
Cdd:PRK09051 232 LKPVFKKEnGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 317 MDVIELNEAFAAQALAVTRDLGLPdnSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIAL 396
Cdd:PRK09051 312 LDVIEANEAFAAQACAVTRELGLD--PAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAA 389
|
....*
gi 446709123 397 IIERV 401
Cdd:PRK09051 390 IFERL 394
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-401 |
1.57e-141 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 408.20 E-value: 1.57e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGL-APVRADDLGAVPLKALMQRNPSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPY 79
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAfRNVRAEDLSAHLMRSLLARNPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 80 QVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSdsafgrsqkiedttmgwrfINPKLKELYG 159
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGVD-------------------FHPGLSKNVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 160 --VDTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVVIDTDEHPRASTTLEALSK 237
Cdd:PRK08947 142 kaAGMMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 238 LKPVVK-AEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQ 316
Cdd:PRK08947 222 LRPAFDpVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 317 MDVIELNEAFAAQALAVTRDLGLPDN-SDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIA 395
Cdd:PRK08947 302 IDVFELNEAFAAQSLPCLKDLGLLDKmDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIA 381
|
....*.
gi 446709123 396 LIIERV 401
Cdd:PRK08947 382 TVFERV 387
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-401 |
3.22e-139 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 403.21 E-value: 3.22e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEdNRNVGRMSALLAGLPYQ 80
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERT-GIDPARIDDVIFGQGYPNGE-APAIGRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMgkSDSAFGRSQkiEDTTMGWRFINPKLK---EL 157
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYT--TDMRWGVRG--GGVQLHDRLARGRETaggRR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 158 YGVDT-MPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVVIDTDEHPRASTTLEALS 236
Cdd:PRK06205 155 FPVPGgMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 237 KLKPV---VKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLT 313
Cdd:PRK06205 235 KLRPImgkQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 314 LDQMDVIELNEAFAAQALAVTRDLGL-PDNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQ 392
Cdd:PRK06205 315 LDDIDLIELNEAFAAQVLAVLKEWGFgADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQ 394
|
....*....
gi 446709123 393 GIALIIERV 401
Cdd:PRK06205 395 GLAAVFERV 403
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-401 |
3.52e-138 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 400.15 E-value: 3.52e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYA-GGLAPVRADDLGAVPLKALMQRNPSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPY 79
Cdd:PRK09052 5 LQDAYIVAATRTPVGKAPrGMFKNTRPDDLLAHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 80 QVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyVMGKSDSA----FGRSqkiEDTTMGwrfinpklk 155
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP-MMGNKPSMspaiFARD---ENVGIA--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 156 elYGvdtMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGD---------AVVIDTDEHP 226
Cdd:PRK09052 152 --YG---MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDlatgevdvkTRTVDLDEGP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 227 RASTTLEALSKLKPVVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKL 306
Cdd:PRK09052 227 RADTSLEGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 307 LKQANLTLDQMDVIELNEAFAAQALAVTRDLGLPdnSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSM 386
Cdd:PRK09052 307 LKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLD--PSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTM 384
|
410
....*....|....*
gi 446709123 387 CIGVGQGIALIIERV 401
Cdd:PRK09052 385 CVGTGMGAAGIFERL 399
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-400 |
1.25e-123 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 363.55 E-value: 1.25e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGR-YAGGLAPVRADDLGAVPLKALMQRNPSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPy 79
Cdd:PRK07851 1 MPEAVIVSTARSPIGRaFKGSLKDMRPDDLAAQMVRAALDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 80 QVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRapYVMGKSDS-----------AFGRSQKI-EDTTMGW 147
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSR--FAKGNSDSlpdtknplfaeAQARTAARaEGGAEAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 148 RfiNPK----LKELYgvDTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPqrkgDAVVIDTD 223
Cdd:PRK07851 158 H--DPRedglLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP----DGTVVSTD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 224 EHPRASTTLEALSKLKPVVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAI 303
Cdd:PRK07851 230 DGPRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEAS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 304 KKLLKQANLTLDQMDVIELNEAFAAQALAVTRDLGLPDnsDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYAL 383
Cdd:PRK07851 310 KQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDE--DKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGL 387
|
410
....*....|....*..
gi 446709123 384 CSMCIGVGQGIALIIER 400
Cdd:PRK07851 388 ETMCVGGGQGMAMVLER 404
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-401 |
2.62e-122 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 359.41 E-value: 2.62e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPYQ 80
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRT-GIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAP----YVMGKS---DSAFGRSQkiedttmGW--RFIN 151
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPissaMTAGEQlgfTSPFAESK-------GWlhRYGD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 152 PKLKELYGvdtmpqtAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEipqrkgdavVIDTDEHPRaSTT 231
Cdd:PRK07801 153 QEVSQFRG-------AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG---------GVTVDEGPR-ETS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 232 LEALSKLKPVVKAeGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQAN 311
Cdd:PRK07801 216 LEKMAGLKPLVEG-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 312 LTLDQMDVIELNEAFAAQALAVTRDLGLpdNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVG 391
Cdd:PRK07801 295 LSIDDIDVVEINEAFAPVVLAWLKETGA--DPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGG 372
|
410
....*....|
gi 446709123 392 QGIALIIERV 401
Cdd:PRK07801 373 TANVTIIERL 382
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-401 |
2.25e-121 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 357.66 E-value: 2.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGR--YAGGLAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLP 78
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKgkKDGSLHEVKPVRLAAGLLEALRDRN-GLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 79 YQVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyvMGKSDSAFgrsqkiedttmgwrFINPKLKelY 158
Cdd:PRK08242 80 ETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP--MGSDGGAW--------------AMDPSTN--F 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 159 GVDTMPQ--TAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEipQRKGdAVVIDTDEHPRASTTLEALS 236
Cdd:PRK08242 142 PTYFVPQgiSADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK--DQNG-LTILDHDEHMRPGTTMESLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 237 KLKPVVKAEGTV---------------------TAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIM 295
Cdd:PRK08242 219 KLKPSFAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 296 GFAPAPAIKKLLKQANLTLDQMDVIELNEAFAAQALAVTRDLGLPDnsDKVNPNGGAIALGHPLGASGARLVTTALNQLE 375
Cdd:PRK08242 299 LTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPH--DKVNVNGGAIAMGHPLGATGAMILGTVLDELE 376
|
410 420
....*....|....*....|....*.
gi 446709123 376 QTGGRYALCSMCIGVGQGIALIIERV 401
Cdd:PRK08242 377 RRGKRTALITLCVGGGMGIATIIERV 402
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-399 |
2.78e-115 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 341.69 E-value: 2.78e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRnPSVDWEQVDDVIYGCANQAGEdNRNVGRMSALLAGLPYQ 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALER-ANVSAEDVEEVIMGTVLQGGQ-GQIPSRQAARAAGIPWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKsdsafGRsqkiedttMGWRFINPKLKELYGV 160
Cdd:PRK08235 79 VQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPG-----AR--------WGYRMGDNEVIDLMVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 161 DT---------MPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVVIDTDEHPRASTT 231
Cdd:PRK08235 146 DGltcafsgvhMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 232 LEALSKLKPVVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQAN 311
Cdd:PRK08235 226 IEKLAKLKPVFDKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 312 LTLDQMDVIELNEAFAAQALAVTRDLGLPDnsDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVG 391
Cdd:PRK08235 306 KTVEDIDLFEINEAFAAVALASTEIAGIDP--EKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGG 383
|
....*...
gi 446709123 392 QGIALIIE 399
Cdd:PRK08235 384 QGDAVLIE 391
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-401 |
2.79e-113 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 336.69 E-value: 2.79e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGG------LAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEDNRNVGRMSALL 74
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKT-GIKPEEIDDIITGCALQVGENWLYGGRHPIFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 75 AGLPYQVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyvMGkSDSAFGRSQKIedttmgwrFINPKL 154
Cdd:PRK06445 80 ARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP--MG-DNPHIEPNPKL--------LTDPKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 155 KElYGVDT---MPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIpQRKGDAVVIDTDEHPRASTT 231
Cdd:PRK06445 149 IE-YDLTTgyvMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-EVEGKKKVVDVDQSVRPDTS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 232 LEALSKLKPVVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQAN 311
Cdd:PRK06445 227 LEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 312 LTLDQMDVIELNEAFAAQALAVTRDLGLpdNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVG 391
Cdd:PRK06445 307 LSVKDIDLWEINEAFAVVVLYAIKELGL--DPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGG 384
|
410
....*....|
gi 446709123 392 QGIALIIERV 401
Cdd:PRK06445 385 QGGAVVLERV 394
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-401 |
7.76e-113 |
|
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: 335.37 E-value: 7.76e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 3 NAYIIDAIRTPFGRYAGGL-APVRADDLGAVPLKALMQRNPSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPYQV 81
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAfRNTRAEDLSAHLMSKLLARNPKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 82 PATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGkSDSAFGRSQKIEDTTmgwrfinpklkelygvD 161
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMHG-VDFHPGMSLHVAKAA----------------G 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 162 TMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVVIDTDEHPRASTTLEALSKLKPV 241
Cdd:TIGR02445 144 MMGLTAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 242 VK-AEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVI 320
Cdd:TIGR02445 224 FDpKNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 321 ELNEAFAAQALAVTRDLGLPDNSD-KVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIE 399
Cdd:TIGR02445 304 ELNEAFAAQALPCLKDLGLLDKMDeKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
|
..
gi 446709123 400 RV 401
Cdd:TIGR02445 384 RV 385
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-400 |
1.20e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 332.62 E-value: 1.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEdNRNVGRMSALLAGLPYQ 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQT-GLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLPHS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSDSA--FGRSQKIEDttmgwrFINPKLKELY 158
Cdd:PRK05656 79 VPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGlrMGHAQLVDS------MITDGLWDAF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 159 GVDTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVVIDTDEHPRASTTLEALSKL 238
Cdd:PRK05656 153 NDYHMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 239 KPVVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMD 318
Cdd:PRK05656 233 KPAFKKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 319 VIELNEAFAAQALAVTRDLGLpdNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALII 398
Cdd:PRK05656 313 LIEANEAFAAQSLAVGKELGW--DAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAI 390
|
..
gi 446709123 399 ER 400
Cdd:PRK05656 391 ER 392
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-401 |
1.03e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 330.17 E-value: 1.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYA-GGLAPVRADDLGAVPLKALMQRNPSVDwEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPY 79
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYE-GPIDDLIIGCAMPEAEQGLNMARNIGALAGLPY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 80 QVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyvmgksdsafgrsqkiedttMGWRFI--NPKLkel 157
Cdd:PRK07661 80 TVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVP--------------------MMGHVVrpNPRL--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 158 ygVDTMPQ-------TAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDA--------VVIDT 222
Cdd:PRK07661 137 --VEAAPEyymgmghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGEnnklqeetITFSQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 223 DEHPRASTTLEALSKLKPVVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPA 302
Cdd:PRK07661 215 DEGVRADTTLEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 303 IKKLLKQANLTLDQMDVIELNEAFAAQALAVTRDLGLpdNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYA 382
Cdd:PRK07661 295 IPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGL--DEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFG 372
|
410
....*....|....*....
gi 446709123 383 LCSMCIGVGQGIALIIERV 401
Cdd:PRK07661 373 IVTMCIGGGMGAAGVFELL 391
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-401 |
2.16e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 308.58 E-value: 2.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPYQ 80
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRS-GADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyvMGKSDSAFGRSqkiedtTMGwRFINPKLKELYGV 160
Cdd:PRK06504 80 VPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP--MGSPSTLPAKN------GLG-HYKSPGMEERYPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 161 DTMPQ--TAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVVIDTDEHPRASTTLEALSKL 238
Cdd:PRK06504 151 IQFSQftGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 239 KPVVKaEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMD 318
Cdd:PRK06504 231 KLIAE-GGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDID 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 319 VIELNEAFAAQALAVTRDLGLpdNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALII 398
Cdd:PRK06504 310 LYEVNEAFASVPLAWLKATGA--DPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIV 387
|
...
gi 446709123 399 ERV 401
Cdd:PRK06504 388 ERL 390
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-401 |
3.38e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 309.64 E-value: 3.38e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNPsVDWEQVDDVIYGCANQaGEDNRNVGRMSALLAGLPYQ 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQP-FAPDDLDEVILGCAMP-SPDEANIARVVALRLGCGEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYV--------MGKSDSAFGRSQKIED-TTMGWRFIN 151
Cdd:PRK08170 80 VPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLfsekmvrwLAGWYAAKSIGQKLAAlGKLRPSYLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 152 PKLKELYGVD------TMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFsKEIVaveiPQRKGDAVVIDTDEH 225
Cdd:PRK08170 160 PVIGLLRGLTdpvvglNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVV----PLFDRDGKFYDHDDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 226 PRASTTLEALSKLKPVV-KAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIK 304
Cdd:PRK08170 235 VRPDSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 305 KLLKQANLTLDQMDVIELNEAFAAQALAVTR----------DLGLPD-----NSDKVNPNGGAIALGHPLGASGARLVTT 369
Cdd:PRK08170 315 PLLQRHGLTLEDLDLWEINEAFAAQVLACLAawadeeycreQLGLDGalgelDRERLNVDGGAIALGHPVGASGARIVLH 394
|
410 420 430
....*....|....*....|....*....|..
gi 446709123 370 ALNQLEQTGGRYALCSMCIGVGQGIALIIERV 401
Cdd:PRK08170 395 LLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-401 |
7.58e-101 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 305.03 E-value: 7.58e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQrNPSVDWEQVDDVIYGCANQAGEDnRNVGRMSALLAGLPYQ 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQ-NSKIDPALVNEVILGQVITGGSG-QNPARQTLIHAGIPKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSrapyvMGKSDSAFGRSQKIEDTTMGWRFINPKLKELYGV 160
Cdd:PRK06633 80 VPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMS-----LGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 161 DTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVvIDTDEHPRASTTLEALSKLKP 240
Cdd:PRK06633 155 VFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSL-FDHDETVRPDTSLEILSKLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 241 VVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVI 320
Cdd:PRK06633 234 AFDKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 321 ELNEAFAAQALAVTRDLGLpdNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIER 400
Cdd:PRK06633 314 EVNEAFAAQSIYVNREMKW--DMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
|
.
gi 446709123 401 V 401
Cdd:PRK06633 392 V 392
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-401 |
9.95e-99 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 299.33 E-value: 9.95e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADD-LGAVPlKALMQRnPSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPY 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAElLGAVQ-RAVLDR-AGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 80 QVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyvMGkSDSAFGRSqkiedttmgwrfiNPKLKElYG 159
Cdd:PRK07850 79 HVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP--LG-ANAGPGRG-------------LPRPDS-WD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 160 VDTMPQ--TAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIP------QRKGDAVVIDTDEHPRaSTT 231
Cdd:PRK07850 142 IDMPNQfeAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPvldeegQPTGETRLVTRDQGLR-DTT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 232 LEALSKLKPVVKaEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQAN 311
Cdd:PRK07850 221 MEGLAGLKPVLE-GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 312 LTLDQMDVIELNEAFAAQALAVTRDLGlPDnSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVG 391
Cdd:PRK07850 300 MKIGDIDLVEINEAFASVVLSWAQVHE-PD-MDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGA 377
|
410
....*....|
gi 446709123 392 QGIALIIERV 401
Cdd:PRK07850 378 LSTGTIIERI 387
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
6-400 |
6.69e-96 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 294.36 E-value: 6.69e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 6 IIDAIRTPFGRYA-GGLAPVRADDLGAVPLKALMQRNPsVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPYQVPAT 84
Cdd:PLN02287 50 IVAAYRTPICKAKrGGFKDTYPDDLLAPVLKAVVEKTG-LNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 85 TINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyvmgksdsafgrsqkiedttMGWRF-INPKLKELYGVDT- 162
Cdd:PLN02287 129 TVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNP--------------------MAWEGgVNPRVESFSQAQDc 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 163 ---MPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVE---IPQRKGD--AVVIDTDEHPRASTTLEA 234
Cdd:PLN02287 189 llpMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHtkiVDPKTGEekPIVISVDDGIRPNTTLAD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 235 LSKLKPVVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTL 314
Cdd:PLN02287 269 LAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLEL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 315 DQMDVIELNEAFAAQALAVTRDLGLpdNSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTG--GRYALCSMCIGVGQ 392
Cdd:PLN02287 349 DDIDLFEINEAFASQFVYCCKKLGL--DPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGM 426
|
....*...
gi 446709123 393 GIALIIER 400
Cdd:PLN02287 427 GAAAVFER 434
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-401 |
1.90e-95 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 292.06 E-value: 1.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFG---RYAGGLAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGL 77
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERN-GLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 78 PYQVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyVMGKSDSAFGRSQKIEDTTmgwrfiNPKLKEL 157
Cdd:PRK06025 80 DIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTA-AMAAEDMAAGKPPLGMGSG------NLRLRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 158 YgvdtmPQT-----AENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVeipQRKGDAVVIDTDEHPRASTTL 232
Cdd:PRK06025 153 H-----PQShqgvcGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV---YRDDGSVALDHEEFPRPQTTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 233 EALSKLKPVVKA-------EGTVT-------------------AGNASGINDGAAALLIASDDAVQAYNLKPRAKIIAST 286
Cdd:PRK06025 225 EGLAALKPAFTAiadypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 287 AVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVIELNEAFAAQALAVTRDLGLPdnSDKVNPNGGAIALGHPLGASGARL 366
Cdd:PRK06025 305 NMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLD--RDKVNVNGGAIALGHPIGATGSIL 382
|
410 420 430
....*....|....*....|....*....|....*
gi 446709123 367 VTTALNQLEQTGGRYALCSMCIGVGQGIALIIERV 401
Cdd:PRK06025 383 IGTVLDELERRGLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-401 |
8.34e-93 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 284.29 E-value: 8.34e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 2 KNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNPsVDWEQVDDVIYG---CAN--QAGednrnvGRMSALLAG 76
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAG-VDPALVQEVFFGnvlSANlgQAP------ARQAALGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 77 LPYQVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSDsafgRSQKIEDTTMGWRFINPKLKE 156
Cdd:PLN02644 74 LPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEAR----KGSRLGHDTVVDGMLKDGLWD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 157 LYGVDTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGD-AVVIDTDEHPrASTTLEAL 235
Cdd:PLN02644 150 VYNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRpSVIVDKDEGL-GKFDPAKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 236 SKLKPVVKAE-GTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTL 314
Cdd:PLN02644 229 RKLRPSFKEDgGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 315 DQMDVIELNEAFAAQALAVTRDLGLPdnSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGI 394
Cdd:PLN02644 309 SQVDYYEINEAFSVVALANQKLLGLD--PEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGAS 386
|
....*..
gi 446709123 395 ALIIERV 401
Cdd:PLN02644 387 AIVVELM 393
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-399 |
6.42e-89 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 274.34 E-value: 6.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGR-YAGGLAPVRADDLGAVPLKALMQRnPSVDWEQVDDVIYGCANQAGEDNRNVGRMSALLAGLPY 79
Cdd:PRK07108 1 MTEAVIVSTARTPLAKsWRGAFNMTHGATLGGHVVQHAVER-AKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 80 QVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKsdsafgrsQKIEDttmGWrfINPKLKELYG 159
Cdd:PRK07108 80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNR--------HMLRE---GW--LVEHKPEIYW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 160 vdTMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDA---------VVIDTDEHPRAST 230
Cdd:PRK07108 147 --SMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKatgrlftkeVTVSADEGIRPDT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 231 TLEALSKLKPVVKAeGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQA 310
Cdd:PRK07108 225 TLEGVSKIRSALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 311 NLTLDQMDVIELNEAFAAQALAVTRDLGLPDnsDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGV 390
Cdd:PRK07108 304 GLKVDDIDLWELNEAFAVQVLYCRDTLGIPM--DRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGG 381
|
....*....
gi 446709123 391 GQGIALIIE 399
Cdd:PRK07108 382 GQGAAGLFE 390
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-402 |
3.31e-87 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 268.94 E-value: 3.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 3 NAYIIDAIRTPFGRYAGGLAPVRADDLGAvPLKALMQRNPSvdwEQVDDVIYGCANQAGEdnrNVGRMSALLAGLPYQVP 82
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAA-PLLTFLSKGME---REIDDVILGNVVGPGG---NVARLSALEAGLGLHIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 83 ATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYvmgkSDSAFGRSQKIEDTTMGwrfinpklkelygvdt 162
Cdd:PRK06690 75 GVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF----QNRARFSPETIGDPDMG---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 163 mpQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVeipqrkgDAVVidtDEHPRASTTLEAL-SKLKPV 241
Cdd:PRK06690 135 --VAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF-------NGLL---DESIKKEMNYERIiKRTKPA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 242 VKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVIE 321
Cdd:PRK06690 203 FLHNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 322 LNEAFAAQALAVTRDLGLPdnSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIERV 401
Cdd:PRK06690 283 INEAFASKVVACAKELQIP--YEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
.
gi 446709123 402 E 402
Cdd:PRK06690 361 E 361
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
6-399 |
2.63e-83 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 260.21 E-value: 2.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 6 IIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRnPSVDWEQVDDVIYGCANQAGEdNRNVGRMSALLAGLPYQVPATT 85
Cdd:PRK06954 11 IASAARTPMAAFQGEFASLTAPQLGAAAIAAAVER-AGLKPEQIDEVVMGCVLPAGQ-GQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 86 INRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSDSAF--GRSQKIEDTTMGwrfinpKLKELYGVD-T 162
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMrmGHGQVLDHMFLD------GLEDAYDKGrL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 163 MPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDaVVIDTDEHPRaSTTLEALSKLKPVV 242
Cdd:PRK06954 163 MGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGD-TVIDRDEQPF-KANPEKIPTLKPAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 243 KAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVIEL 322
Cdd:PRK06954 241 SKTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446709123 323 NEAFAAQALAVTRDLGLPdnSDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIE 399
Cdd:PRK06954 321 NEAFAVVTMAAMKEHGLP--HEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
5-269 |
1.89e-82 |
|
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: 252.99 E-value: 1.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 5 YIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNPsVDWEQVDDVIYGCANQAGEDnRNVGRMSALLAGLPYQVPAT 84
Cdd:pfam00108 2 VIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAG-VDPEDVDEVIVGNVLQAGEG-QNPARQAALKAGIPDSAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 85 TINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGkSDSAFGRSQ---KIEDTTmgwrfINPKLKELYGVD 161
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALP-TDARSGLKHgdeKKHDLL-----IPDGLTDAFNGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 162 TMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDAVViDTDEHPRASTTLEALSKLKPV 241
Cdd:pfam00108 154 HMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTV-DKDEGIRPPTTAEPLAKLKPA 232
|
250 260
....*....|....*....|....*...
gi 446709123 242 VKAEGTVTAGNASGINDGAAALLIASDD 269
Cdd:pfam00108 233 FDKEGTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-402 |
2.40e-79 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 249.54 E-value: 2.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQrNPSVDWEQVDDVIYGCANQAGEDNRNVGRmSALLAGLPYQ 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVID-DAKLDPALVQEVIMGNVIQAGVGQNPAGQ-AAYHAGLPFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 81 VPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMgKSDSAFG------RSQKIEDTTMGWRFINPKL 154
Cdd:PRK06366 79 VTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLL-PSDLRWGpkhllhKNYKIDDAMLVDGLIDAFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 155 KELYGVdtmpqTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEipqrkgdavVIDTDEHPRaSTTLEA 234
Cdd:PRK06366 158 FEHMGV-----SAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------DLDRDEGIR-KTTMED 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 235 LSKLKPVVKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTL 314
Cdd:PRK06366 223 LAKLPPAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 315 DQMDVIELNEAFAAQALAVTRDLGLpDNsDKVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGI 394
Cdd:PRK06366 303 DYYDLVEHNEAFSIASIIVRDQLKI-DN-ERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAH 380
|
....*...
gi 446709123 395 ALIIERVE 402
Cdd:PRK06366 381 TLTLEMVE 388
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
6-400 |
8.65e-69 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 223.32 E-value: 8.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 6 IIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEdNRNVGRMSALLAGLPYQVPATT 85
Cdd:PRK08963 9 IVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARS-EIDPELIEQLVFGQVVQMPE-APNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 86 INRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKS------DSAFGRsqkiedtTMGWR---FINPKLKE 156
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKlaralvDLNKAR-------TLGQRlklFSRLRLRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 157 LYGVD----------TMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGdavVIDTDEHP 226
Cdd:PRK08963 160 LLPVPpavaeystglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ---PLEEDNNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 227 RASTTLEALSKLKPVV-KAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKI--IASTAVGVEpRIMGFAPAPAI 303
Cdd:PRK08963 237 RGDSTLEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLrsYAFAAIDVW-QDMLLGPAYAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 304 KKLLKQANLTLDQMDVIELNEAFAAQALAVTRDLGLPD---------------NSDKVNPNGGAIALGHPLGASGARLVT 368
Cdd:PRK08963 316 PLALERAGLTLADLTLIDMHEAFAAQTLANLQMFASERfareklgrsqaigevDMSKFNVLGGSIAYGHPFAATGARMIT 395
|
410 420 430
....*....|....*....|....*....|..
gi 446709123 369 TALNQLEQTGGRYALCSMCIGVGQGIALIIER 400
Cdd:PRK08963 396 QTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
14-399 |
2.67e-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: 192.71 E-value: 2.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 14 FGRYAGGLAPVRADDLGAVPLKALMQRnPSVDWEQVDDVIYGCANQAGEdNRNVGRMSALLAGLPYQVPATTINRLCGSS 93
Cdd:cd00826 11 FGGENGADANDLAHEAGAKAIAAALEP-AGVAAGAVEEACLGQVLGAGE-GQNCAQQAAMHAGGLQEAPAIGMNNLCGSG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 94 LDAIAIAARAIKAGEANLVIAGGVESMSRApyvmgksdsafGRSqkiedttmgwrfiNPKLKELygvdtmpqtaeNVAEQ 173
Cdd:cd00826 89 LRALALAMQLIAGGDANCILAGGFEKMETS-----------AEN-------------NAKEKHI-----------DVLIN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 174 FNVNRADQDQFALVSQQRTASAQAKGFFSKEIVAVEIPQRKGDaVVIDTDEHPR--ASTTLEALSKLKPVVKAEGTVTAG 251
Cdd:cd00826 134 KYGMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGD-IHSDADEYIQfgDEASLDEIAKLRPAFDKEDFLTAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 252 NASGINDGAAALLIASDDAVQAYNLK-------PRAKIIASTAVGVEPR----IMGFAPAPAIKKLLKQANLTLDQMDVI 320
Cdd:cd00826 213 NACGLNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDLI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 321 ELNEAFAAQALAVTRDLG---------LPDNSDK-------VNPNGGAIALGHPLGASGARLVTTALNQL-----EQTGG 379
Cdd:cd00826 293 EAHDAFAANACATNEALGlcpegqggaLVDRGDNtyggksiINPNGGAIAIGHPIGASGAAICAELCFELkgeagKRQGA 372
|
410 420
....*....|....*....|
gi 446709123 380 RYALCSMCIGVGQGIALIIE 399
Cdd:cd00826 373 GAGLALLCIGGGGGAAMCIE 392
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
276-400 |
4.22e-56 |
|
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: 180.53 E-value: 4.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 276 LKPRAKIIASTAVGVEPRIMGFAPAPAIKKLLKQANLTLDQMDVIELNEAFAAQALAVTRDLGLPDNsdKVNPNGGAIAL 355
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE--KVNVNGGAIAL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446709123 356 GHPLGASGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIER 400
Cdd:pfam02803 79 GHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
4-400 |
1.13e-54 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 186.64 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 4 AYIIDAIRTPFGRYAGGLAPVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANQAGEDNrNVGRMSALLAGLPYQVPA 83
Cdd:PRK09268 9 VAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRF-GLQGERLGEVVAGAVLKHSRDF-NLTRECVLGSALSPYTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 84 TTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPYVMGKSDSAFGRSQKIEDTTMGwrfinpKLKELYGVD-- 161
Cdd:PRK09268 87 YDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLELNRAKTTGD------RLKALGKLRpk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 162 ----------------TMPQTAENVAEQFNVNRADQDQFALVSQQRTASAQAKGFFSKEIVaveiPQRKgdavvIDTDEH 225
Cdd:PRK09268 161 hlapeiprngeprtglSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLIT----PFLG-----LTRDNN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 226 PRASTTLEALSKLKPV--VKAEGTVTAGNASGINDGAAALLIASDDAVQAYNLKPRAKIIAS--TAV----GVEPRIMgf 297
Cdd:PRK09268 232 LRPDSSLEKLAKLKPVfgKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetAAVdfvhGKEGLLM-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 298 APAPAIKKLLKQANLTLDQMDVIELNEAFAAQALAVTR----------DLGLP------DNSdKVNPNGGAIALGHPLGA 361
Cdd:PRK09268 310 APAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKawedeeycreRLGLDaplgsiDRS-KLNVNGSSLAAGHPFAA 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 446709123 362 SGARLVTTALNQLEQTGGRYALCSMCIGVGQGIALIIER 400
Cdd:PRK09268 389 TGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
250-398 |
1.04e-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: 90.58 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 250 AGNASGINDGAAALLIASDDAVQAYNLKPRAKII--ASTAVG--VEPRIMGFAPAPAIKKLLKQANLTLDQMDVIELNEA 325
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVstAATFDGasMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 326 FAAQALAVTRDLGL-PDNSDKVNPNGGAIALGHPLGASGARLVTTALNQLE-------QTGGRYALCSMCIGVGQGIALI 397
Cdd:cd00327 174 GTPIGDAVELALGLdPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVV 253
|
.
gi 446709123 398 I 398
Cdd:cd00327 254 L 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
12-374 |
2.38e-19 |
|
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: 88.86 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 12 TPFGRYAGglapVRADDLGAVPLKALMQRNpSVDWEQVDDVIYGCANqAGEDNRNVGRMSALLAGLPYqVPATTINRLCG 91
Cdd:cd00829 6 TPFGRRSD----RSPLELAAEAARAALDDA-GLEPADIDAVVVGNAA-GGRFQSFPGALIAEYLGLLG-KPATRVEAAGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 92 SSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyvmgKSDSAFGRSQkiedtTMGWRFINPklkelYGVDTMPQTAENVA 171
Cdd:cd00829 79 SGSAAVRAAAAAIASGLADVVLVVGAEKMSDVP----TGDEAGGRAS-----DLEWEGPEP-----PGGLTPPALYALAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 172 ----EQFNVNRadqDQFALVSQQRTASAQakgffskeivaveipqrkgdavvidtdEHPRAST----TLEALSKLKPVVk 243
Cdd:cd00829 145 rrymHRYGTTR---EDLAKVAVKNHRNAA---------------------------RNPYAQFrkpiTVEDVLNSRMIA- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 244 aeGTVTAGNASGINDGAAALLIASDDAVQAYNLKPrAKIIASTAVGVEPRIM------GFAPA-PAIKKLLKQANLTLDQ 316
Cdd:cd00829 194 --DPLRLLDCCPVSDGAAAVVLASEERARELTDRP-VWILGVGAASDTPSLSerddflSLDAArLAARRAYKMAGITPDD 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446709123 317 MDVIELNEAFAAQALAVTRDLGL--PDNSDK--------------VNPNGGAIALGHPLGASGARLVTTALNQL 374
Cdd:cd00829 271 IDVAELYDCFTIAELLALEDLGFceKGEGGKlvregdtaiggdlpVNTSGGLLSKGHPLGATGLAQAVEAVRQL 344
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
240-381 |
1.25e-12 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 68.95 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 240 PVVkaEGTVTAGNASGINDGAAALLIASDDAVQAYnlkPRAKIIA--------STAVGVEPRIMGFAPAP--------AI 303
Cdd:PRK06289 208 PVV--EGRLRRQDCSQVTDGGAGVVLASDAYLRDY---ADARPIPrikgwghrTAPLGLEQKLDRSAGDPyvlphvrqAV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 304 KKLLKQANLTLDQMDVIELNEAFAAQALAVTRDLGL--PDNSDK--------------VNPNGGAIALGHPLGASGARLV 367
Cdd:PRK06289 283 LDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHIGLtgPGESWKaiengeiaiggrlpINPSGGLIGGGHPVGASGVRML 362
|
170
....*....|....
gi 446709123 368 TTALNQLEQTGGRY 381
Cdd:PRK06289 363 LDAAKQVTGTAGDY 376
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-376 |
1.55e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 62.22 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 1 MKNAYIIDAIRTPFGRyaggLAPVRADDLgAVP--LKALMQRNpsVDWEQVDDVIYGcaNQAG---EDNRNVGRMSALLA 75
Cdd:PRK06064 1 MRDVAIIGVGQTKFGE----LWDVSLRDL-AVEagLEALEDAG--IDGKDIDAMYVG--NMSAglfVSQEHIAALIADYA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 76 GLPyQVPATTINRLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyvMGKSDSAFGRSQKIE-DTTMGWRFinPKL 154
Cdd:PRK06064 72 GLA-PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVP--TPDATEAIARAGDYEwEEFFGATF--PGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 155 KELYGVDTMpqtaenvaEQFNVNRADQDQFAlVSQQRTASAQAKGFFSKEIvaveipqrkgdavvidtdehprastTLEA 234
Cdd:PRK06064 147 YALIARRYM--------HKYGTTEEDLALVA-VKNHYNGSKNPYAQFQKEI-------------------------TVEQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 235 LSKLKPVvkAEgTVTAGNASGINDGAAALLIASDDAVQAYNLKPrAKIIAST------AVGVEPRIMGF-APAPAIKKLL 307
Cdd:PRK06064 193 VLNSPPV--AD-PLKLLDCSPITDGAAAVILASEEKAKEYTDTP-VWIKASGqasdtiALHDRKDFTTLdAAVVAAEKAY 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 308 KQANLTLDQMDVIELNEAFAAQALAVTRDLGLP----------------DNSDKVNPNGGAIALGHPLGASGARLVTTAL 371
Cdd:PRK06064 269 KMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFAkkgeggklaregqtyiGGDIPVNPSGGLKAKGHPVGATGVSQAVEIV 348
|
....*
gi 446709123 372 NQLEQ 376
Cdd:PRK06064 349 WQLRG 353
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
256-363 |
3.22e-08 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 55.08 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 256 INDGAAALLIASDDavQAYNLKPRAKIIASTAVGVEPRIMG---FAPAPAIKKLLKQA-NLTLDQMDVIELNEAFAAQAL 331
Cdd:PRK07937 204 ITDGAAAVVLAAGD--RARELRERPAWITGIEHRIESPSLGardLTRSPSTALAAEAAtGGDAGGVDVAELHAPFTHQEL 281
|
90 100 110
....*....|....*....|....*....|..
gi 446709123 332 AVTRDLGLPDNSdKVNPNGGAIAlGHPLGASG 363
Cdd:PRK07937 282 ILREALGLGDKT-KVNPSGGALA-ANPMFAAG 311
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
258-363 |
3.11e-07 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 51.82 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 258 DGAAALLIASDDAVQAYNLKPRAKIIA--------STAVGVEP-RIMGF-APAPAIKKLLKQANLTLDQMDVIELNEAFA 327
Cdd:PRK08256 215 CGAAAAIVCSEEFARKHGLDRAVEIVAqamttdtpSTFDGRSMiDLVGYdMTRAAAQQVYEQAGIGPEDIDVVELHDCFS 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446709123 328 AQALAVTRDLGLP---------DNSDK-------VNPNGGAIALGHPLGASG 363
Cdd:PRK08256 295 ANELLTYEALGLCpegeaekfiDDGDNtyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
254-383 |
9.38e-07 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 50.66 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 254 SGINDGAAALLIASDDAVQAYNLKP---RAKIIASTAVGV-------EPRIMGFAPAPAIKKLLKQANLTLDQMDVIELN 323
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsRLVEIKSLACASgnlyedpPDATRMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446709123 324 EAFAAQALAVTRDLGLPD---------NSD-------KVNPNGGAIALGHPLGASGARLVTTALNQLEQTGGRYAL 383
Cdd:PTZ00455 336 DCFTIAELLMYEALGIAEyghakdlirNGAtalegriPVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQM 411
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
67-379 |
1.70e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 49.84 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 67 VGRMSALLAGLPYQVPAttinrLCGSSLDAIAIAARAIKAGEANLVIAGGVESMSRAPyvMGKSDSAFGRSQKIEdttmg 146
Cdd:PRK12578 64 VAEYSGLTGKVPLRVEA-----MCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEVD--TSTSLAIGGRGGNYQ----- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 147 WRFinpklkELYGVdTMPQT-AENVAEQFNVNRADQDQFALVS--QQRTASAQAKGFFSKEIVAVEIPQRKgdavVIdtd 223
Cdd:PRK12578 132 WEY------HFYGT-TFPTYyALYATRHMAVYGTTEEQMALVSvkAHKYGAMNPKAHFQKPVTVEEVLKSR----AI--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 224 ehpraSTTLEALsklkpvvkaegtvtagNASGINDGAAALLIASDDAVQAYNLKPRAKI----IASTAVGVEPRI--MGF 297
Cdd:PRK12578 198 -----SWPIKLL----------------DSCPISDGSATAIFASEEKVKELKIDSPVWItgigYANDYAYVARRGewVGF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 298 -APAPAIKKLLKQANLTLDQMDVIELNEAFAAQALAVTRDLGLPD-----------NSDK-----VNPNGGAIALGHPLG 360
Cdd:PRK12578 257 kATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEkgkggkfieegQSEKggkvgVNLFGGLKAKGHPLG 336
|
330
....*....|....*....
gi 446709123 361 ASGARLVTTALNQLEQTGG 379
Cdd:PRK12578 337 ATGLSMIYEITKQLRDEAG 355
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
254-379 |
2.18e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 49.18 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 254 SGINDGAAALLIASDDAVQAYnlkPRAKIIASTA-----VGVEPR-IMGF-APAPAIKKLLKQANLTLDQMDVIELNEAF 326
Cdd:PRK07516 213 SLVSDGAAALVLADAETARAL---QRAVRFRARAhvndfLPLSRRdPLAFeGPRRAWQRALAQAGVTLDDLSFVETHDCF 289
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446709123 327 ------------------AAQALA---VTRDLGLPdnsdkVNPNGGAIALGHPLGASGARLVTTALNQLEQTGG 379
Cdd:PRK07516 290 tiaelieyeamglappgqGARAIRegwTAKDGKLP-----VNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAG 358
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
226-380 |
1.11e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 43.97 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 226 PRASTTleALSKLKPVVKAEGTV---TAGNASGINDGAAALLIASDDAVQAYNLKP---RAKIIASTAVGVEPRIMGFAP 299
Cdd:PRK06066 179 PRASYA--SNISLEDVLSSEYVVyplTELDIAPFVDGAIVVVLASEEVAKKLTDDPvwiKGIGWSTESSNLETAELGKAN 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 300 AP--AIKKLLKQANLTLDQMDV--IELNEAFAAQALAVTRDLGLPDNSDK----------------VNPNGGAIALGHPL 359
Cdd:PRK06066 257 YMriAADMAYKMAGIESPRKEVdaAEVDDRYSYKELQHIEALRLSEEPEKdsllregnfdpqgelpVNPSGGHLAKGVPL 336
|
170 180
....*....|....*....|.
gi 446709123 360 GASGARLVTTALNQLEQTGGR 380
Cdd:PRK06066 337 EASGLSLLLDAVEYLRGEAGA 357
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
248-377 |
1.26e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 43.75 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 248 VTAGNASGINDGAAALLIASDDAVQAYNLKP-RAKIIASTAVGVEPRIMGFAPAP------------------------- 301
Cdd:PRK06365 217 LTRLDVCAMSDGAACAILASEDKAFEITDKPvLIKAIGTGSDTLRLADRPFGEVPllpnespddykdlrypgvhsfragr 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 302 -AIKKLLKQANLT--LDQMDVIELNEAFAAQALAVTRDLGL--------------PDNSDK--VNPNGGAIALGHPLGAS 362
Cdd:PRK06365 297 mAAKEAYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgkPELPGKlpVNPSGGLLAAGHAVGAT 376
|
170
....*....|....*
gi 446709123 363 GARLVTTALNQLEQT 377
Cdd:PRK06365 377 GIMQAVFMFWQLQGR 391
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
254-380 |
3.29e-04 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 42.71 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446709123 254 SGINDGAAALLIASDDAVQAYNLKPRAKIIA-STAVGVEPRIMG----FAPAP----AIKKLLKQANLT--LDQMDVIEL 322
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGKKDPVYVKAlQLAVSNGWELQYngwdGSYFPttriAARKAYREAGITdpREELSMAEV 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446709123 323 NEAFAAQALAVTRDLGLP----------------DNSDKVNPNGGAIALGHPLGASGARLVTTALNQL-EQTGGR 380
Cdd:PRK06157 294 HDCFSITELVTMEDLGLSergqawrdvldgffdaDGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLlGRAGER 368
|
|
| |
