|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-400 |
0e+00 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 839.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNPQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPDS 80
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSRDAAIYDTTIGWRFINPLMKAQYGV 160
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSRQAEIFDTTIGWRFVNPLMKAQYGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 161 DSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVVSRDEHPR-ATTMEALAKLKG 239
Cdd:PRK09050 161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRpETTLEALAKLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 240 VVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVI 319
Cdd:PRK09050 241 VFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 320 ELNEAFAAQGLAVTRQLGLRDDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIER 399
Cdd:PRK09050 321 ELNEAFAAQGLAVLRQLGLADDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIER 400
|
.
gi 1777068256 400 V 400
Cdd:PRK09050 401 V 401
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-400 |
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: 705.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 2 TEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNPQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPDSV 81
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNPQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 82 PGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSRDAAIYDTTIGWRFINPLMKAQYGVD 161
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIEDTTIGWRFINPLMKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 162 SMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVVSRDEHPRA-TTMEALAKLKGV 240
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPeTTLEGLAKLKPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 241 VRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVIE 320
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 321 LNEAFAAQGLAVTRQLGLRDDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIERV 400
Cdd:TIGR02430 321 LNEAFAAQALAVLRELGLADDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIERV 400
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-400 |
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: 601.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGeDNRNVARMSSLLAGLPDS 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERA-GLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSRDAAIYDTTIgwrfiNPLMKAQYGV 160
Cdd:COG0183 79 VPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPMI-----NPGLTDPYTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 161 DSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDaIVVSRDEHPRA-TTMEALAKLKG 239
Cdd:COG0183 154 LSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPdTTLEKLAKLKP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 240 VVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVI 319
Cdd:COG0183 233 AFKKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 320 ELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIER 399
Cdd:COG0183 313 EINEAFAAQVLAVLRELGL--DPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
.
gi 1777068256 400 V 400
Cdd:COG0183 391 V 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-399 |
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: 558.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 5 FICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNPqVDWSAIDDVIFGCANQAGEdNRNVARMSSLLAGLPDSVPGS 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAG-LDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 85 TINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSRDAAIYDttigwRFINPLMKAQYGVDSMP 164
Cdd:cd00751 79 TVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLD-----GMLDDGLTDPFTGLSMG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 165 ETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDaIVVSRDEHPRA-TTMEALAKLKGVVRP 243
Cdd:cd00751 154 ITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAFKK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 244 DGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVIELNE 323
Cdd:cd00751 233 DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777068256 324 AFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIER 399
Cdd:cd00751 313 AFAAQALACLKELGL--DPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-400 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 523.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGEdNRNVARMSSLLAGLPDS 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERA-GVPPEQVDEVIMGQVLQAGA-GQNPARQAALKAGLPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSR-DAAIYDTtigwrFINPLMKAQYG 159
Cdd:PRK05790 79 VPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMgDVELVDT-----MIHDGLTDAFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 160 VDSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVVSRDEHPRA-TTMEALAKLK 238
Cdd:PRK05790 154 GYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPdTTAESLAKLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 239 GVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDV 318
Cdd:PRK05790 234 PAFDKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 319 IELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIE 398
Cdd:PRK05790 314 IEINEAFAAQALAVEKELGL--DPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVE 391
|
..
gi 1777068256 399 RV 400
Cdd:PRK05790 392 RP 393
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-400 |
1.41e-180 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 507.78 E-value: 1.41e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNPqVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPDS 80
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSG-FPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSRDAAIYDTTIGWRFINPLMKAQYGV 160
Cdd:PRK08131 80 VPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTTIGARFPNPKIVAQYGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 161 DSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQ-KKGDAIVVSRDEHPRA-TTMEALAKLK 238
Cdd:PRK08131 160 DSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgRKLPPKLVAEDEHPRPsSTVEALTKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 239 GVVRpDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDV 318
Cdd:PRK08131 240 PLFE-GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 319 IELNEAFAAQGLAVTRQLGLRDDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIE 398
Cdd:PRK08131 319 IEINEAFASQVLGCLKGLGVDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
..
gi 1777068256 399 RV 400
Cdd:PRK08131 399 RV 400
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-398 |
5.47e-167 |
|
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: 472.87 E-value: 5.47e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 6 ICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNPqVDWSAIDDVIFGCANQAGEDNrNVARMSSLLAGLPDSVPGST 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNP-LDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAYT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 86 INRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGK--AASAFSRDAAIYDttigwrFINPLMKAQYGVDSM 163
Cdd:TIGR01930 79 VNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRslRWGVKPGNAELED------ARLKDLTDANTGLPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 164 PETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDaIVVSRDEHPRA-TTMEALAKLKGVVR 242
Cdd:TIGR01930 153 GVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGP-VTVSSDEGIRPnTTLEKLAKLKPAFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 243 PDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVIELN 322
Cdd:TIGR01930 232 PDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEIN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777068256 323 EAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIE 398
Cdd:TIGR01930 312 EAFAAQVLACIKELGL--DLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-400 |
1.21e-151 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 434.42 E-value: 1.21e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGEdNRNVARMSSLLAGLPDS 80
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERT-GIDPARIDDVIFGQGYPNGE-APAIGRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPF-VMGKAASAFSRDAAIYDttigwRFINPLMKAQ-- 157
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFyTTDMRWGVRGGGVQLHD-----RLARGRETAGgr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 158 -YGVDS-MPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVVSRDEHPRA-TTMEAL 234
Cdd:PRK06205 154 rFPVPGgMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRAdTTLESL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 235 AKLK---GVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGL 311
Cdd:PRK06205 234 AKLRpimGKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 312 SIDQLDVIELNEAFAAQGLAVTRQLGLRDDDP-RVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVG 390
Cdd:PRK06205 314 TLDDIDLIELNEAFAAQVLAVLKEWGFGADDEeRLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGG 393
|
410
....*....|
gi 1777068256 391 QGIALVIERV 400
Cdd:PRK06205 394 QGLAAVFERV 403
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-400 |
4.02e-146 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 420.13 E-value: 4.02e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPDS 80
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARA-GVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMgKAASAFSR--DAAIYDTTIGwrfinpLMKAQY 158
Cdd:PRK09051 81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLL-PAARWGARmgDAKLVDMMVG------ALHDPF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 159 GVDSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDaIVVSRDEHPRA-TTMEALAKL 237
Cdd:PRK09051 154 GTIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGE-VVFDTDEHVRAdTTLEDLAKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 238 KGVVRPD-GTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQL 316
Cdd:PRK09051 233 KPVFKKEnGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 317 DVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALV 396
Cdd:PRK09051 313 DVIEANEAFAAQACAVTRELGL--DPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAI 390
|
....
gi 1777068256 397 IERV 400
Cdd:PRK09051 391 FERL 394
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-400 |
1.57e-143 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 413.63 E-value: 1.57e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRY-GGSLSAVRADDLGAVPLKALMARNPQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPD 79
Cdd:PRK09052 5 LQDAYIVAATRTPVGKApRGMFKNTRPDDLLAHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 80 SVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFvMGKAASA----FSRDAaiyDTTIGwrfinplmk 155
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM-MGNKPSMspaiFARDE---NVGIA--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 156 aqYGvdsMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGD---------AIVVSRDEHP 226
Cdd:PRK09052 152 --YG---MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDlatgevdvkTRTVDLDEGP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 227 RA-TTMEALAKLKGVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKL 305
Cdd:PRK09052 227 RAdTSLEGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 306 LKQLGLSIDQLDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTM 385
Cdd:PRK09052 307 LKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGL--DPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTM 384
|
410
....*....|....*
gi 1777068256 386 CIGVGQGIALVIERV 400
Cdd:PRK09052 385 CVGTGMGAAGIFERL 399
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-400 |
5.77e-141 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 406.66 E-value: 5.77e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRY-GGSLSAVRADDLGAVPLKALMARNPQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPD 79
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 80 SVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMG-KAASAFSRDAAiydttigwrfinplmKAQy 158
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGvDFHPGLSKNVA---------------KAA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 159 gvDSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVVSRDEHPRA-TTMEALAKL 237
Cdd:PRK08947 145 --GMMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPeTTVEALAAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 238 KGVVRP-DGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQL 316
Cdd:PRK08947 223 RPAFDPvNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 317 DVIELNEAFAAQGLAVTRQLGLRDD-DPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIAL 395
Cdd:PRK08947 303 DVFELNEAFAAQSLPCLKDLGLLDKmDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIAT 382
|
....*
gi 1777068256 396 VIERV 400
Cdd:PRK08947 383 VFERV 387
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-399 |
9.14e-131 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 381.66 E-value: 9.14e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYG-GSLSAVRADDLGAVPLKALMARNPQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLpD 79
Cdd:PRK07851 1 MPEAVIVSTARSPIGRAFkGSLKDMRPDDLAAQMVRAALDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGY-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 80 SVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRapFVMGKAasafsrdaaiyDTTIGWRfiNPLM----- 154
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSR--FAKGNS-----------DSLPDTK--NPLFaeaqa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 155 ----KAQYGVD----------------SMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPqkk 214
Cdd:PRK07851 145 rtaaRAEGGAEawhdpredgllpdvyiAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 215 gDAIVVSRDEHPRA-TTMEALAKLKGVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRV 293
Cdd:PRK07851 222 -DGTVVSTDDGPRAgTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 294 MGIGPAPASQKLLKQLGLSIDQLDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQL 373
Cdd:PRK07851 301 MGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGI--DEDKLNVSGGAIALGHPFGMTGARITTTLLNNL 378
|
410 420
....*....|....*....|....*.
gi 1777068256 374 QRTGGRYALCTMCIGVGQGIALVIER 399
Cdd:PRK07851 379 QTHDKTFGLETMCVGGGQGMAMVLER 404
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-400 |
1.74e-121 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 357.66 E-value: 1.74e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGR--YGGSLSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLP 78
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKgkKDGSLHEVKPVRLAAGLLEALRDRN-GLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 79 DSVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPfvMGKAASAFSRDAAIydttigwrfinplmkaQY 158
Cdd:PRK08242 80 ETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP--MGSDGGAWAMDPST----------------NF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 159 GVDSMPE--TAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTipqKKGDAIVVSRDEHPRA-TTMEALA 235
Cdd:PRK08242 142 PTYFVPQgiSADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK---DQNGLTILDHDEHMRPgTTMESLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 236 KLKG---------------------VVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVM 294
Cdd:PRK08242 219 KLKPsfammgemggfdavalqkypeVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 295 GIGPAPASQKLLKQLGLSIDQLDVIELNEAFAAQGLAVTRQLGLRDDdpRVNPNGGAIALGHPLGMSGARLVTTAMYQLQ 374
Cdd:PRK08242 299 LTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHD--KVNVNGGAIAMGHPLGATGAMILGTVLDELE 376
|
410 420
....*....|....*....|....*.
gi 1777068256 375 RTGGRYALCTMCIGVGQGIALVIERV 400
Cdd:PRK08242 377 RRGKRTALITLCVGGGMGIATIIERV 402
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-400 |
1.46e-119 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 352.09 E-value: 1.46e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPDS 80
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRT-GIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSRDAAIYDTTIGWRfinplmkAQYGV 160
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGFTSPFAESKGWL-------HRYGD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 161 DSMPE--TAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVtipqkkGDaivVSRDEHPRATTMEALAKLK 238
Cdd:PRK07801 153 QEVSQfrGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV------GG---VTVDEGPRETSLEKMAGLK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 239 gVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDV 318
Cdd:PRK07801 224 -PLVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 319 IELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIE 398
Cdd:PRK07801 303 VEINEAFAPVVLAWLKETGA--DPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380
|
..
gi 1777068256 399 RV 400
Cdd:PRK07801 381 RL 382
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
6-400 |
4.70e-117 |
|
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: 345.77 E-value: 4.70e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 6 ICDAIRTPIGRY-GGSLSAVRADDLGAVPLKALMARNPQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPDSVPGS 84
Cdd:TIGR02445 4 IVDFGRTPMGRSkGGAFRNTRAEDLSAHLMSKLLARNPKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTSAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 85 TINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMG-KAASAFSRDAAiydttigwrfinplmKAQygvDSM 163
Cdd:TIGR02445 84 TVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMHGvDFHPGMSLHVA---------------KAA---GMM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 164 PETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVVSRDEHPRA-TTMEALAKLKGVVR 242
Cdd:TIGR02445 146 GLTAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPeTTVESLAALRPAFD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 243 P-DGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVIEL 321
Cdd:TIGR02445 226 PkNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 322 NEAFAAQGLAVTRQLGLRDD-DPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIERV 400
Cdd:TIGR02445 306 NEAFAAQALPCLKDLGLLDKmDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFERV 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-398 |
3.31e-116 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 344.00 E-value: 3.31e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARnpqVDWSA--IDDVIFGCANQAGEdNRNVARMSSLLAGLP 78
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALER---ANVSAedVEEVIMGTVLQGGQ-GQIPSRQAARAAGIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 79 DSVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKA------ASAFSRDAAIYDTtigwrfinp 152
Cdd:PRK08235 77 WEVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGArwgyrmGDNEVIDLMVADG--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 153 LMKAQYGVdSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVVSRDEHPRA-TTM 231
Cdd:PRK08235 148 LTCAFSGV-HMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKdTTI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 232 EALAKLKGVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGL 311
Cdd:PRK08235 227 EKLAKLKPVFDKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 312 SIDQLDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQ 391
Cdd:PRK08235 307 TVEDIDLFEINEAFAAVALASTEIAGI--DPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQ 384
|
....*..
gi 1777068256 392 GIALVIE 398
Cdd:PRK08235 385 GDAVLIE 391
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-400 |
4.24e-115 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 340.96 E-value: 4.24e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYG-GSLSAVRADDLGAVPLKALMARNPQVDwSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPD 79
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYE-GPIDDLIIGCAMPEAEQGLNMARNIGALAGLPY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 80 SVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPfVMGKAASAfsrDAAIYDTTIGWRFinplmkaqyg 159
Cdd:PRK07661 80 TVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVP-MMGHVVRP---NPRLVEAAPEYYM---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 160 vdSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDA--------IVVSRDEHPRA-TT 230
Cdd:PRK07661 146 --GMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGEnnklqeetITFSQDEGVRAdTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 231 MEALAKLKGVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLG 310
Cdd:PRK07661 224 LEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 311 LSIDQLDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVG 390
Cdd:PRK07661 304 LELSDIGLFELNEAFASQSIQVIRELGL--DEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGG 381
|
410
....*....|
gi 1777068256 391 QGIALVIERV 400
Cdd:PRK07661 382 MGAAGVFELL 391
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-399 |
1.06e-113 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 337.63 E-value: 1.06e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGEdNRNVARMSSLLAGLPDS 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQT-GLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLPHS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSR-DAAIYDTTIG---WRFINPLmka 156
Cdd:PRK05656 79 VPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMgHAQLVDSMITdglWDAFNDY--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 157 qygvdSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVVSRDEHPRA-TTMEALA 235
Cdd:PRK05656 156 -----HMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAgTTAESLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 236 KLKGVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQ 315
Cdd:PRK05656 231 KLKPAFKKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 316 LDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIAL 395
Cdd:PRK05656 311 LDLIEANEAFAAQSLAVGKELGW--DAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVAL 388
|
....
gi 1777068256 396 VIER 399
Cdd:PRK05656 389 AIER 392
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-400 |
1.27e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 329.76 E-value: 1.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGS------LSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGEDNRNVARMSSLL 74
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKT-GIKPEEIDDIITGCALQVGENWLYGGRHPIFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 75 AGLPDSVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPfvMG-----KAASAFSRDAAI--YDTTIGW 147
Cdd:PRK06445 80 ARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP--MGdnphiEPNPKLLTDPKYieYDLTTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 148 rfinplmkaqygvdSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIpQKKGDAIVVSRDEHPR 227
Cdd:PRK06445 158 --------------VMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-EVEGKKKVVDVDQSVR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 228 A-TTMEALAKLKGVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLL 306
Cdd:PRK06445 223 PdTSLEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 307 KQLGLSIDQLDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMC 386
Cdd:PRK06445 303 EKAGLSVKDIDLWEINEAFAVVVLYAIKELGL--DPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLC 380
|
410
....*....|....
gi 1777068256 387 IGVGQGIALVIERV 400
Cdd:PRK06445 381 VGGGQGGAVVLERV 394
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-400 |
8.51e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 307.04 E-value: 8.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPDS 80
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRS-GADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPfvMGKAASAFSRDA-AIYDTtigwrfinPLMKAQYG 159
Cdd:PRK06504 80 VPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP--MGSPSTLPAKNGlGHYKS--------PGMEERYP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 160 VD--SMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVVSRDEHPRA-TTMEALAK 236
Cdd:PRK06504 150 GIqfSQFTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFdATLEGIAG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 237 LKgVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQL 316
Cdd:PRK06504 230 VK-LIAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 317 DVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALV 396
Cdd:PRK06504 309 DLYEVNEAFASVPLAWLKATGA--DPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTI 386
|
....
gi 1777068256 397 IERV 400
Cdd:PRK06504 387 VERL 390
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-400 |
4.40e-101 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 305.11 E-value: 4.40e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARnPQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPDS 80
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDR-AGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSRDAAIYDTTigwrfinplMKAQYgv 160
Cdd:PRK07850 80 VGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPRPDSWDID---------MPNQF-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 161 dsmpETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIP------QKKGDAIVVSRDEHPRATTMEAL 234
Cdd:PRK07850 149 ----EAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPvldeegQPTGETRLVTRDQGLRDTTMEGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 235 AKLKGVVrPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSID 314
Cdd:PRK07850 225 AGLKPVL-EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 315 QLDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIA 394
Cdd:PRK07850 304 DIDLVEINEAFASVVLSWAQVHEP--DMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTG 381
|
....*.
gi 1777068256 395 LVIERV 400
Cdd:PRK07850 382 TIIERI 387
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-398 |
9.03e-99 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 299.38 E-value: 9.03e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGR-YGGSLSAVRADDLGAVPLKALMARnPQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPD 79
Cdd:PRK07108 1 MTEAVIVSTARTPLAKsWRGAFNMTHGATLGGHVVQHAVER-AKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 80 SVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKaasafsrdaaiYDTTIGWrfinpLMKAQYG 159
Cdd:PRK07108 80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNR-----------HMLREGW-----LVEHKPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 160 VD-SMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDA---------IVVSRDEHPRA- 228
Cdd:PRK07108 144 IYwSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKatgrlftkeVTVSADEGIRPd 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 229 TTMEALAKLKGVVrPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQ 308
Cdd:PRK07108 224 TTLEGVSKIRSAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 309 LGLSIDQLDVIELNEAFAAQGLAVTRQLGLRDDdpRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIG 388
Cdd:PRK07108 303 AGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMD--RLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIG 380
|
410
....*....|
gi 1777068256 389 VGQGIALVIE 398
Cdd:PRK07108 381 GGQGAAGLFE 390
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
3-400 |
5.23e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 297.71 E-value: 5.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 3 EAFICDAIRTPIGRYGGSLSAVRADDLgAVPLKALMARNPQVDWSAIDDVIFGCANQAGEDnRNVARMSSLLAGLPDSVP 82
Cdd:PRK06633 4 PVYITHAKRTAFGSFMGSLSTTPAPML-AAHLIKDILQNSKIDPALVNEVILGQVITGGSG-QNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 83 GSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMS---RAPFVmgKAASAFSR----DAAIYDTtigwrfinpLMK 155
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI--RAGAKFGDikmvDLMQYDG---------LTD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 156 AQYGVdSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVvSRDEHPRA-TTMEAL 234
Cdd:PRK06633 151 VFSGV-FMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLF-DHDETVRPdTSLEIL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 235 AKLKGVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSID 314
Cdd:PRK06633 229 SKLRPAFDKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 315 QLDVIELNEAFAAQGLAVTRQlgLRDDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIA 394
Cdd:PRK06633 309 DLEVIEVNEAFAAQSIYVNRE--MKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMA 386
|
....*.
gi 1777068256 395 LVIERV 400
Cdd:PRK06633 387 MCVEAV 392
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
5-400 |
6.47e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 298.47 E-value: 6.47e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 5 FICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNPqVDWSAIDDVIFGCANQaGEDNRNVARMSSLLAGLPDSVPGS 84
Cdd:PRK08170 6 YIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQP-FAPDDLDEVILGCAMP-SPDEANIARVVALRLGCGEKVPAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 85 TINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFV-----------MGKAASAFSRDAAIydTTIGWRFINPL 153
Cdd:PRK08170 84 TVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLfsekmvrwlagWYAAKSIGQKLAAL--GKLRPSYLAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 154 MKAQYGVD------SMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAqEITPVTIPQKKgdaiVVSRDEHPR 227
Cdd:PRK08170 162 IGLLRGLTdpvvglNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDRDGK----FYDHDDGVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 228 A-TTMEALAKLKGVV-RPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKL 305
Cdd:PRK08170 237 PdSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 306 LKQLGLSIDQLDVIELNEAFAAQGLAVTR----------QLGL-----RDDDPRVNPNGGAIALGHPLGMSGARLVTTAM 370
Cdd:PRK08170 317 LQRHGLTLEDLDLWEINEAFAAQVLACLAawadeeycreQLGLdgalgELDRERLNVDGGAIALGHPVGASGARIVLHLL 396
|
410 420 430
....*....|....*....|....*....|
gi 1777068256 371 YQLQRTGGRYALCTMCIGVGQGIALVIERV 400
Cdd:PRK08170 397 HALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
6-399 |
2.02e-97 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 297.83 E-value: 2.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 6 ICDAIRTPIGRYG-GSLSAVRADDLGAVPLKALMARNPqVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGLPDSVPGS 84
Cdd:PLN02287 50 IVAAYRTPICKAKrGGFKDTYPDDLLAPVLKAVVEKTG-LNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 85 TINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPfvmgkaasafsrdaaiydttIGWRF-INPLMK----AQYG 159
Cdd:PLN02287 129 TVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNP--------------------MAWEGgVNPRVEsfsqAQDC 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 160 VDSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPV---TIPQKKGD--AIVVSRDEHPR-ATTMEA 233
Cdd:PLN02287 189 LLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkIVDPKTGEekPIVISVDDGIRpNTTLAD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 234 LAKLKGVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSI 313
Cdd:PLN02287 269 LAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLEL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 314 DQLDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTG--GRYALCTMCIGVGQ 391
Cdd:PLN02287 349 DDIDLFEINEAFASQFVYCCKKLGL--DPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGM 426
|
....*...
gi 1777068256 392 GIALVIER 399
Cdd:PLN02287 427 GAAAVFER 434
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-400 |
1.18e-93 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 286.22 E-value: 1.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 2 TEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNPqVDWSAIDDVIFG---CAN--QAGednrnvARMSSLLAG 76
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAG-VDPALVQEVFFGnvlSANlgQAP------ARQAALGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 77 LPDSVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAfSR--DAAIYDTTIGWRFINPlm 154
Cdd:PLN02644 74 LPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKG-SRlgHDTVVDGMLKDGLWDV-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 155 kaqYGVDSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGD-AIVVSRDEHPRATTMEA 233
Cdd:PLN02644 151 ---YNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRpSVIVDKDEGLGKFDPAK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 234 LAKLKGVVRPD-GTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLS 312
Cdd:PLN02644 228 LRKLRPSFKEDgGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 313 IDQLDVIELNEAFAAQGLAVTRQLGLRDDdpRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQG 392
Cdd:PLN02644 308 ASQVDYYEINEAFSVVALANQKLLGLDPE--KVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGA 385
|
....*...
gi 1777068256 393 IALVIERV 400
Cdd:PLN02644 386 SAIVVELM 393
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-400 |
5.74e-90 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 276.89 E-value: 5.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMaRNPQVDWSAIDDVIFGCANQAGeDNRNVARMSSLLAGLPDS 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVI-DDAKLDPALVQEVIMGNVIQAG-VGQNPAGQAAYHAGLPFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 81 VPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGK-----AASAFSRDAAIYDTTIgwrfINPLMK 155
Cdd:PRK06366 79 VTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSdlrwgPKHLLHKNYKIDDAML----VDGLID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 156 AQYgVDSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTipqkkgdaiVVSRDEHPRATTMEALA 235
Cdd:PRK06366 155 AFY-FEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------DLDRDEGIRKTTMEDLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 236 KLKGVVRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQ 315
Cdd:PRK06366 225 KLPPAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 316 LDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIAL 395
Cdd:PRK06366 305 YDLVEHNEAFSIASIIVRDQLKI--DNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTL 382
|
....*
gi 1777068256 396 VIERV 400
Cdd:PRK06366 383 TLEMV 387
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-400 |
8.37e-86 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 265.09 E-value: 8.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 3 EAFICDAIRTPIGRYGGSLSAVRADDLGAvPLKALMARNPQvdwSAIDDVIFGCANQAGEdnrNVARMSSLLAGLPDSVP 82
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAA-PLLTFLSKGME---REIDDVILGNVVGPGG---NVARLSALEAGLGLHIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 83 GSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFvmgKAASAFSRDaaiydtTIGwrfiNPlmkaqygvdS 162
Cdd:PRK06690 75 GVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF---QNRARFSPE------TIG----DP---------D 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 163 MPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEItpVTIPQKKGDAIVVSRDehprattMEAL-AKLKGVV 241
Cdd:PRK06690 133 MGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEI--LSFNGLLDESIKKEMN-------YERIiKRTKPAF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 242 RPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVIEL 321
Cdd:PRK06690 204 LHNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEI 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1777068256 322 NEAFAAQGLAVTRQLGLRDDdpRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIERV 400
Cdd:PRK06690 284 NEAFASKVVACAKELQIPYE--KLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
6-398 |
9.03e-86 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 266.37 E-value: 9.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 6 ICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARnPQVDWSAIDDVIFGCANQAGEdNRNVARMSSLLAGLPDSVPGST 85
Cdd:PRK06954 11 IASAARTPMAAFQGEFASLTAPQLGAAAIAAAVER-AGLKPEQIDEVVMGCVLPAGQ-GQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 86 INRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSR-DAAIYDTTigwrFINPLMKAQYGVDSMP 164
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMgHGQVLDHM----FLDGLEDAYDKGRLMG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 165 ETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAiVVSRDEHPRATTMEALAKLKGVVRPD 244
Cdd:PRK06954 165 TFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDT-VIDRDEQPFKANPEKIPTLKPAFSKT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 245 GTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVIELNEA 324
Cdd:PRK06954 244 GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEA 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777068256 325 FAAQGLAVTRQLGLRDDdpRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIE 398
Cdd:PRK06954 324 FAVVTMAAMKEHGLPHE--KVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-400 |
1.36e-85 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 266.64 E-value: 1.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 1 MTEAFICDAIRTP--IGRYG-GSLSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGEDNRNVARMSSLLAGL 77
Cdd:PRK06025 1 MAEAYIIDAVRTPrgIGKVGkGALAHLHPQHLAATVLKALAERN-GLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 78 PDSVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRApfvmgkAASAfSRDAAIYDTTIGWRFINPLMKAQ 157
Cdd:PRK06025 80 DIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYT------AAMA-AEDMAAGKPPLGMGSGNLRLRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 158 YGVDSMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQkkgDAIVVSRDEHPR-ATTMEALAK 236
Cdd:PRK06025 153 HPQSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDD---GSVALDHEEFPRpQTTAEGLAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 237 LK-------GVVRPDGTVT-------------------AGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVP 290
Cdd:PRK06025 230 LKpaftaiaDYPLDDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 291 PRVMGIGPAPASQKLLKQLGLSIDQLDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIALGHPLGMSGARLVTTAM 370
Cdd:PRK06025 310 PTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDL--DRDKVNVNGGAIALGHPIGATGSILIGTVL 387
|
410 420 430
....*....|....*....|....*....|
gi 1777068256 371 YQLQRTGGRYALCTMCIGVGQGIALVIERV 400
Cdd:PRK06025 388 DELERRGLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
5-268 |
1.99e-81 |
|
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: 250.30 E-value: 1.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 5 FICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNPqVDWSAIDDVIFGCANQAGEDnRNVARMSSLLAGLPDSVPGS 84
Cdd:pfam00108 2 VIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAG-VDPEDVDEVIVGNVLQAGEG-QNPARQAALKAGIPDSAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 85 TINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKA--ASAFSRDAAIYDTTIgwrfINPLMKAQYGVdS 162
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDarSGLKHGDEKKHDLLI----PDGLTDAFNGY-H 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 163 MPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDaIVVSRDEHPRA-TTMEALAKLKGVV 241
Cdd:pfam00108 155 MGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGK-PTVDKDEGIRPpTTAEPLAKLKPAF 233
|
250 260
....*....|....*....|....*..
gi 1777068256 242 RPDGTVTAGNASGVNDGACALLLANEE 268
Cdd:pfam00108 234 DKEGTVTAGNASPINDGAAAVLLMSES 260
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
6-399 |
1.65e-73 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 235.65 E-value: 1.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 6 ICDAIRTPIGRYGGSLSAVRADDLGAVPLKALMARNpQVDWSAIDDVIFGCANQAGEdNRNVARMSSLLAGLPDSVPGST 85
Cdd:PRK08963 9 IVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARS-EIDPELIEQLVFGQVVQMPE-APNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 86 INRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSRDAAiYDTTIGWRF-------INPLMK--- 155
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLN-KARTLGQRLklfsrlrLRDLLPvpp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 156 --AQYGVD-SMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGdaiVVSRDEHPRA-TTM 231
Cdd:PRK08963 166 avAEYSTGlRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ---PLEEDNNIRGdSTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 232 EALAKLKGVV-RPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRV-MGIGPAPASQKLLKQL 309
Cdd:PRK08963 243 EDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQdMLLGPAYATPLALERA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 310 GLSIDQLDVIELNEAFAAQGLAVTRQLGLRD---------------DDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQ 374
Cdd:PRK08963 323 GLTLADLTLIDMHEAFAAQTLANLQMFASERfareklgrsqaigevDMSKFNVLGGSIAYGHPFAATGARMITQTLHELR 402
|
410 420
....*....|....*....|....*
gi 1777068256 375 RTGGRYALCTMCIGVGQGIALVIER 399
Cdd:PRK08963 403 RRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
9-398 |
7.19e-59 |
|
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: 196.56 E-value: 7.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 9 AIRTPIGRYGGSLSAVR---ADDLGAVPLKALMARnPQVDWSAIDDVIFGCANQAGEdNRNVARMSSLLAGLPDSVPGST 85
Cdd:cd00826 3 AAMTAFGKFGGENGADAndlAHEAGAKAIAAALEP-AGVAAGAVEEACLGQVLGAGE-GQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 86 INRLCGSGMDATGTAARAIRSGETALMIAGGVESMSrapfvmgkaasafsrdaaiydttigwrfinplmkaqygvdsmpE 165
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME-------------------------------------------T 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 166 TAENVATDYNIN--------REDQDRFAVRSQASAARAQEDGTLAQEITPVTIPQKKGDAIVVSRD--EHPRATTMEALA 235
Cdd:cd00826 118 SAENNAKEKHIDvlinkygmRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEyiQFGDEASLDEIA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 236 KLKGVVRPDGTVTAGNASGVNDGACALLLANEESA-------KRFGLTPRARIVGMATAGVPPR----VMGIGPAPASQK 304
Cdd:cd00826 198 KLRPAFDKEDFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 305 LLKQLGLSIDQLDVIELNEAFAAQGLAVTRQLGL-----------RDDDPR-----VNPNGGAIALGHPLGMSGARLVTT 368
Cdd:cd00826 278 ALEKAGLGIGDLDLIEAHDAFAANACATNEALGLcpegqggalvdRGDNTYggksiINPNGGAIAIGHPIGASGAAICAE 357
|
410 420 430
....*....|....*....|....*....|....*
gi 1777068256 369 AMYQLQRTGG-----RYALCTMCIGVGQGIALVIE 398
Cdd:cd00826 358 LCFELKGEAGkrqgaGAGLALLCIGGGGGAAMCIE 392
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
275-399 |
1.90e-57 |
|
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: 183.61 E-value: 1.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 275 LTPRARIVGMATAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVIELNEAFAAQGLAVTRQLGLrdDDPRVNPNGGAIAL 354
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGI--DPEKVNVNGGAIAL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1777068256 355 GHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIER 399
Cdd:pfam02803 79 GHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
66-399 |
2.34e-48 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 169.70 E-value: 2.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 66 NVARMSSLLAGLPDSVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSRDAAIYDTTI 145
Cdd:PRK09268 69 NLTRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLELNRAKTTG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 146 G-WRFINPLMKAQYGVD-----------SMPETAENVATDYNINREDQDRFAVRSQASAARAQEDGTLAQEITPVtipqk 213
Cdd:PRK09268 149 DrLKALGKLRPKHLAPEiprngeprtglSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF----- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 214 KGdaivVSRDEHPRA-TTMEALAKLKGV--VRPDGTVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVP 290
Cdd:PRK09268 224 LG----LTRDNNLRPdSSLEKLAKLKPVfgKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 291 pRVMG-----IGPAPASQKLLKQLGLSIDQLDVIELNEAFAAQGLAVTR----------QLGL-----RDDDPRVNPNGG 350
Cdd:PRK09268 300 -FVHGkegllMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKawedeeycreRLGLdaplgSIDRSKLNVNGS 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1777068256 351 AIALGHPLGMSGARLVTTAMYQLQRTGGRYALCTMCIGVGQGIALVIER 399
Cdd:PRK09268 379 SLAAGHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
12-380 |
1.69e-22 |
|
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: 97.72 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 12 TPIGRYGGslsaVRADDLGAVPLKALMARNPqVDWSAIDDVIFGCANqAGEDNRNVARMSSLLAGLPDsVPGSTINRLCG 91
Cdd:cd00829 6 TPFGRRSD----RSPLELAAEAARAALDDAG-LEPADIDAVVVGNAA-GGRFQSFPGALIAEYLGLLG-KPATRVEAAGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 92 SGMDATGTAARAIRSGETALMIAGGVESMSRAPFVMGKAASAFSRDAAIYDTTIGWRFInplmkAQYGvdsmpetaeNVA 171
Cdd:cd00829 79 SGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPPGGLTPP-----ALYA---------LAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 172 T----DYNINREDQDRFAVRSQASAARaqedgtlaqeitpvtipqkkgdaivvsrdeHPRA-----TTMEALAKLKGVVR 242
Cdd:cd00829 145 RrymhRYGTTREDLAKVAVKNHRNAAR------------------------------NPYAqfrkpITVEDVLNSRMIAD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 243 PdgtVTAGNASGVNDGACALLLANEESAKRFGLTPrARIVGMATAGVPP----RVMGIGPAP---ASQKLLKQLGLSIDQ 315
Cdd:cd00829 195 P---LRLLDCCPVSDGAAAVVLASEERARELTDRP-VWILGVGAASDTPslseRDDFLSLDAarlAARRAYKMAGITPDD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 316 LDVIELNEAFAAQGLAVTRQLGL----------------RDDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGR 379
Cdd:cd00829 271 IDVAELYDCFTIAELLALEDLGFcekgeggklvregdtaIGGDLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGA 350
|
.
gi 1777068256 380 Y 380
Cdd:cd00829 351 R 351
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
249-397 |
4.82e-22 |
|
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: 94.43 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 249 AGNASGVNDGACALLLANEESAKRFGLTPRARIVGMAT----AGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVIELNEA 324
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAAtfdgASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 325 FAAQGLAVTRQLGLRDDDPR-VNPNGGAIALGHPLGMSGARLVTTAMYQLQ-------RTGGRYALCTMCIGVGQGIALV 396
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVRsPAVSATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVV 253
|
.
gi 1777068256 397 I 397
Cdd:cd00327 254 L 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
90-373 |
8.78e-14 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 72.24 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 90 CGSGMDATGTAARAIRSGETALMIAGGVESMSRAPF-----VMGKAASAFsrdaaiYDTTIGWRFinPLMKAQYGVDSMP 164
Cdd:PRK06064 85 CASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTpdateAIARAGDYE------WEEFFGATF--PGLYALIARRYMH 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 165 EtaenvatdYNINREDQDRFAVRSQASAAR---AQedgtlaqeitpvtipqkkgdaivvsrdeHPRATTMEALAKLKGVV 241
Cdd:PRK06064 157 K--------YGTTEEDLALVAVKNHYNGSKnpyAQ----------------------------FQKEITVEQVLNSPPVA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 242 RPdgtVTAGNASGVNDGACALLLANEESAKRFGLTPrARIVGMA----TAGVPPR--VMGIGPAP-ASQKLLKQLGLSID 314
Cdd:PRK06064 201 DP---LKLLDCSPITDGAAAVILASEEKAKEYTDTP-VWIKASGqasdTIALHDRkdFTTLDAAVvAAEKAYKMAGIEPK 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777068256 315 QLDVIELNEAFAAQGLAVTRQLGL----------------RDDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQL 373
Cdd:PRK06064 277 DIDVAEVHDCFTIAEILAYEDLGFakkgeggklaregqtyIGGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQL 351
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
86-362 |
2.16e-09 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 58.76 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 86 INRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRapfvmGKAASAFSRDAAIYDttigwRFInPLMKAQYGVDSMPE 165
Cdd:PRK08256 76 VNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQP-----GALGSVWDDRPSPLE-----RFD-KALAELQGFDPAPP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 166 TA-------ENVATDYNINREDQDRFAVRSQASAARaqedGTLAQEITPVTIpqkkgDAIVVSRDEHPRATTMEAlaklk 238
Cdd:PRK08256 145 ALrmfggagREHMEKYGTTAETFAKIGVKARRHAAN----NPYAQFRDEYTL-----EDVLASPMIWGPLTRLQC----- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 239 gvvrpdgtvtagnaSGVNDGACALLLANEESAKRFGLTPRARIVG--MAT-------AGVPPRVMGIG-PAPASQKLLKQ 308
Cdd:PRK08256 211 --------------CPPTCGAAAAIVCSEEFARKHGLDRAVEIVAqaMTTdtpstfdGRSMIDLVGYDmTRAAAQQVYEQ 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 309 LGLSIDQLDVIELNEAFAAQGLAVTRQLGL----------RDDDPR------VNPNGGAIALGHPLGMSG 362
Cdd:PRK08256 277 AGIGPEDIDVVELHDCFSANELLTYEALGLcpegeaekfiDDGDNTyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
79-380 |
3.84e-08 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 54.69 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 79 DSVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMSRAPfvmGKAASAFSRDAAIYDTTI-GWRFINPLMKAQ 157
Cdd:PRK06289 79 WGVPASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVP---GDVAAEHLGAAAWTGHEGqDARFPWPSMFAR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 158 ygvdsmpeTAENVATDYNINREDQDRFAVRSQASAARaqedgtlaqeitpvtipqkkgdaivvsrdeHPRATTM-----E 232
Cdd:PRK06289 156 --------VADEYDRRYGLDEEHLRAIAEINFANARR------------------------------NPNAQTRgwafpD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 233 ALAKLKGVVRP--DGTVTAGNASGVNDGACALLLANEESAKRF-GLTPRARIvgmatAGVPPRVMGIGPAP--------- 300
Cdd:PRK06289 198 EATNDDDATNPvvEGRLRRQDCSQVTDGGAGVVLASDAYLRDYaDARPIPRI-----KGWGHRTAPLGLEQkldrsagdp 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 301 --------ASQKLLKQLGLSIDQLDVIELNEAFAAQGLAVTRQLGLR--------------DDDPR--VNPNGGAIALGH 356
Cdd:PRK06289 273 yvlphvrqAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHIGLTgpgeswkaiengeiAIGGRlpINPSGGLIGGGH 352
|
330 340
....*....|....*....|....
gi 1777068256 357 PLGMSGARLVTTAMYQLQRTGGRY 380
Cdd:PRK06289 353 PVGASGVRMLLDAAKQVTGTAGDY 376
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
253-382 |
4.77e-08 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 54.51 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 253 SGVNDGACALLLANEESAKRFGLTPR-ARIVGMATAGV--------PPRVMGIGPA-PASQKLLKQLGLSIDQLDVIELN 322
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEIKSLACasgnlyedPPDATRMFTSrAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777068256 323 EAFAAQGLAVTRQLG----------------LRDDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGRYAL 382
Cdd:PTZ00455 336 DCFTIAELLMYEALGiaeyghakdlirngatALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQM 411
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
77-379 |
6.13e-06 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 48.10 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 77 LPDsVPGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESM-----------SRAPF-----VMGKAASAFSRDAAI 140
Cdd:PRK06157 76 LPN-IPVTRVENFCATGSEAFRGAVYAVASGAYDIALALGVEKLkdtgygglpvaNPGTLadmtmPNVTAPGNFAQLASA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 141 YdttigwrfinplmKAQYGVdSMPETAENVAtdyninredqdRFAVRSQASAARaqedgtlaqeitpvtipqkkgdaivv 220
Cdd:PRK06157 155 Y-------------AAKYGV-SREDLKRAMA-----------HVSVKSHANGAR-------------------------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 221 srdeHPRA-----TTMEALAKLKGVVRPDGTVtagNASGVNDGACALLLANEESAKRFGLTPRARIVGMATAGVPPRVMG 295
Cdd:PRK06157 184 ----NPKAhlrkaVTEEQVLKAPMIAGPLGLF---DCCGVSDGAAAAIVTTPEIARALGKKDPVYVKALQLAVSNGWELQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 296 IG---------PAPASQKLLKQLGLS--IDQLDVIELNEAFAAQGLAVTRQLGL----------------RDDDPRVNPN 348
Cdd:PRK06157 257 YNgwdgsyfptTRIAARKAYREAGITdpREELSMAEVHDCFSITELVTMEDLGLsergqawrdvldgffdADGGLPCQID 336
|
330 340 350
....*....|....*....|....*....|..
gi 1777068256 349 GGAIALGHPLGMSGARLVTTAMYQLQ-RTGGR 379
Cdd:PRK06157 337 GGLKCFGHPIGASGLRMLYEMYLQLLgRAGER 368
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
90-378 |
7.80e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 47.53 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 90 CGSGMDATGTAARAIRSGETALMIAGGVESMSR----APFVMGKAASAFSRDAAIYDTTIgwrfinPLMKAQYGVDSMPE 165
Cdd:PRK12578 82 CATGLAASLTAYTAVASGLVDMAIAVGVDKMTEvdtsTSLAIGGRGGNYQWEYHFYGTTF------PTYYALYATRHMAV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 166 taenvatdYNINREDQDRFAVRSQASAARAQEdgtlAQEITPVTIpqkkgdaivvsrdehprattmEALAKLKGVVRPdg 245
Cdd:PRK12578 156 --------YGTTEEQMALVSVKAHKYGAMNPK----AHFQKPVTV---------------------EEVLKSRAISWP-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 246 tVTAGNASGVNDGACALLLANEESAKRFGLTPRARIVGMA----TAGVPPRVMGIG---PAPASQKLLKQLGLSIDQLDV 318
Cdd:PRK12578 201 -IKLLDSCPISDGSATAIFASEEKVKELKIDSPVWITGIGyandYAYVARRGEWVGfkaTQLAARQAYNMAKVTPNDIEV 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777068256 319 IELNEAFAAQGLAVTRQLG----------LRDDDPR------VNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGG 378
Cdd:PRK12578 280 ATVHDAFTIAEIMGYEDLGftekgkggkfIEEGQSEkggkvgVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAG 355
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
253-378 |
1.99e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 46.48 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 253 SGVNDGACALLLANEESAKRFgltPRA-RIVGMATAG--VPPRVMGI----GPAPASQKLLKQLGLSIDQLDVIELNEAF 325
Cdd:PRK07516 213 SLVSDGAAALVLADAETARAL---QRAvRFRARAHVNdfLPLSRRDPlafeGPRRAWQRALAQAGVTLDDLSFVETHDCF 289
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 326 A--------AQGLAVTRQ--------LGLRDDDPRVNPNGGAIALGHPLGMSGARL-VTTAMyQLQRTGG 378
Cdd:PRK07516 290 TiaelieyeAMGLAPPGQgarairegWTAKDGKLPVNPSGGLKAKGHPIGATGVSMhVLAAM-QLTGEAG 358
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
196-376 |
6.97e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 44.90 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 196 QEDGTLAQEITPVTIpQKKGDAIVVSRDEHPRATTMEALAKLKGVVRPdgtVTAGNASGVNDGACALLLANEESAKRFGL 275
Cdd:PRK06365 170 YEFGTTVEQLAKVSV-KNHGNAIHNPFAQSPMKITVEDVRKSPMVSYP---LTRLDVCAMSDGAACAILASEDKAFEITD 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 276 TP-RARIVGMATAGVPP--RVMGIGP-----APASQKLLKQLGLS---------------------IDQLDVIELNEAFA 326
Cdd:PRK06365 246 KPvLIKAIGTGSDTLRLadRPFGEVPllpneSPDDYKDLRYPGVHsfragrmaakeayemagitdpLNDLDLIELHDAYT 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777068256 327 AQGLAVTRQLGLR----------------DDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRT 376
Cdd:PRK06365 326 SSEIQTYEDLGLCkygeggqfiesgkpelPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQGR 391
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
255-362 |
8.76e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 44.29 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 255 VNDGACALLLANEESAKRFGLTPrARIVGMA----TAGVPPRVMGIGP--APASQKLLkqlGLSIDQLDVIELNEAFAAQ 328
Cdd:PRK07937 204 ITDGAAAVVLAAGDRARELRERP-AWITGIEhrieSPSLGARDLTRSPstALAAEAAT---GGDAGGVDVAELHAPFTHQ 279
|
90 100 110
....*....|....*....|....*....|....
gi 1777068256 329 GLAVTRQLGLrDDDPRVNPNGGAIAlGHPLGMSG 362
Cdd:PRK07937 280 ELILREALGL-GDKTKVNPSGGALA-ANPMFAAG 311
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
90-120 |
5.30e-04 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 42.00 E-value: 5.30e-04
10 20 30
....*....|....*....|....*....|.
gi 1777068256 90 CGSGMDATGTAARAIRSGETALMIAGGVESM 120
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAA 191
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
82-132 |
5.74e-04 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 41.70 E-value: 5.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1777068256 82 PGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVES----MSRAPFVMGKAAS 132
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAaitpLGIAGFAAARALS 208
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
258-363 |
5.78e-04 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 41.62 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 258 GACALLLANEESAKRFGLTPRARIVGMATAG-----VPPRVMGIGPAPASQKLLKQLGLSIDQLDVI-------ELNEAF 325
Cdd:COG0304 232 GAGVLVLEELEHAKARGAKIYAEVVGYGASSdayhiTAPAPDGEGAARAMRAALKDAGLSPEDIDYInahgtstPLGDAA 311
|
90 100 110
....*....|....*....|....*....|....*...
gi 1777068256 326 AAQglAVTRQLGLRDDDPRVNPNGGAIalGHPLGMSGA 363
Cdd:COG0304 312 ETK--AIKRVFGDHAYKVPVSSTKSMT--GHLLGAAGA 345
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
82-121 |
6.03e-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: 6.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1777068256 82 PGSTINRLCGSGMDATGTAARAIRSGETALMIAGGVESMS 121
Cdd:cd00834 153 PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALI 192
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
258-375 |
6.74e-04 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 41.66 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 258 GACALLLANEESAKRFGLTPRARIVGMATA--GVPPRVMGIGPAPAS--QKLLKQLGLSIDQLDVIEL-----NEAFAAQ 328
Cdd:cd00828 232 GAGVLVLERAELALARGAPIYGRVAGTASTtdGAGRSVPAGGKGIARaiRTALAKAGLSLDDLDVISAhgtstPANDVAE 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1777068256 329 GLAVTRQLGLRDDDPRVNPNGGAIalGHPLGMSGARLVTTAMYQLQR 375
Cdd:cd00828 312 SRAIAEVAGALGAPLPVTAQKALF--GHSKGAAGALQLIGALQSLEH 356
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
258-363 |
7.51e-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: 41.37 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 258 GACALLLANEESAKRFGLTPRARIVGMATAG-----VPPRVMGIGPAPASQKLLKQLGLSIDQLDVI-------ELNEaf 325
Cdd:cd00834 232 GAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDYInahgtstPLND-- 309
|
90 100 110
....*....|....*....|....*....|....*...
gi 1777068256 326 AAQGLAVTRQLGLRDDDPRVNPNGGAIalGHPLGMSGA 363
Cdd:cd00834 310 AAESKAIKRVFGEHAKKVPVSSTKSMT--GHLLGAAGA 345
|
|
| PRK08257 |
PRK08257 |
acetyl-CoA acetyltransferase; Validated |
255-344 |
8.41e-04 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 236204 [Multi-domain] Cd Length: 498 Bit Score: 41.44 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 255 VNDGAcALLLANEESAKRFGLtPRARIV---GMATAGVPPRVM---GIGPAPAS----QKLLKQLGLSIDQLDVIELNEA 324
Cdd:PRK08257 243 VDQGA-AVLLTSVAKARRLGV-PEDRWVylhGGADAHDPYDILerpDLHRSPAIraagRRALALAGLGIDDIDAFDLYSC 320
|
90 100
....*....|....*....|
gi 1777068256 325 FAAQGLAVTRQLGLRDDDPR 344
Cdd:PRK08257 321 FPSAVQVAARELGLDLDDPR 340
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
257-380 |
1.05e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 40.87 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 257 DGACALLLANEESAKRFGLTPRARIVG-------MATAG---VPPRvmgiGPAPASQKLLKQLGLS--IDQLDVIELNEA 324
Cdd:PRK08313 210 DGACAVVIGDEEAADAAAGRPVAWIHGtamrtepLAFAGrdqVNPQ----AGRDAAAALWKAAGITdpRDEIDVAEIYVP 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777068256 325 FAAQGLAVTRQLGLRDD----------------DPRVNPNGGAIAlGHPLGMSGARLVTTAMYQLQRTGGRY 380
Cdd:PRK08313 286 FSWFEPMWLENLGFAPEgegwklteagetaiggRLPVNPSGGVLS-SNPIGASGMIRFAEAALQVMGKAGEH 356
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
257-379 |
1.33e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 40.51 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 257 DGACALLLANEESAKRFGLTPR-ARIVGMATAGVPPRVMGIGPAP----ASQKLLKQLGLSIDQLDV--IELNEAFAAQG 329
Cdd:PRK06066 212 DGAIVVVLASEEVAKKLTDDPVwIKGIGWSTESSNLETAELGKANymriAADMAYKMAGIESPRKEVdaAEVDDRYSYKE 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777068256 330 LAVTRQLGL----------------RDDDPRVNPNGGAIALGHPLGMSGARLVTTAMYQLQRTGGR 379
Cdd:PRK06066 292 LQHIEALRLseepekdsllregnfdPQGELPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGA 357
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
257-370 |
1.33e-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: 40.31 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068256 257 DGACALLLANEESAKRFGLTPRARIVGMA-----TAGVPPRVMGIGPAPASQKLLKQLGLSIDQLDVIELNEAFAAQGLA 331
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAatidgAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDV 240
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1777068256 332 VTRQLGLRDDDPRVNPNGGAIA-LGHPLGMSGARLVTTAM 370
Cdd:cd00825 241 KELKLLRSEFGDKSPAVSATKAmTGNLSSAAVVLAVDEAV 280
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
90-137 |
2.44e-03 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 39.16 E-value: 2.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1777068256 90 CGSGMDATGTAARAIRSGETALMIAGGVESM-SRAPFVMGKAASAFSRD 137
Cdd:pfam00109 173 CSSSLVAIHAAVQSIRSGEADVALAGGVNLLlTPLGFAGFSAAGMLSPD 221
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
90-138 |
8.33e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 38.06 E-value: 8.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1777068256 90 CGSGMDATGTAARAIRSGETALMIAGGVES----MSRAPFVMGKAASAFSRDA 138
Cdd:PRK06333 173 CAAGVQAIGDAARLIRSGEADVAVCGGTEAaidrVSLAGFAAARALSTRFNDA 225
|
|
| |
