|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-387 |
0e+00 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 771.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEHV 80
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANAGPDRSILRPASWDIDLPDQFTAAERIAKRRGI 160
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPRPDSWDIDMPNQFEAAERIAKRRGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 161 TREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPALDENKQPTSERVTISRDQGLRETTLSGLSALKPVLEGGIHTAGT 240
Cdd:PRK07850 161 TREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEGQPTGETRLVTRDQGLRDTTMEGLAGLKPVLEGGIHTAGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 241 SSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEINEAFASVVLS 320
Cdd:PRK07850 241 SSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAFASVVLS 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504194651 321 WARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIERI 387
Cdd:PRK07850 321 WAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIERI 387
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-387 |
4.93e-168 |
|
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: 474.94 E-value: 4.93e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGeQSNNISRVSWLVAGLPEHV 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPESV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRV---------GLGANAGPDRSILRPASWD-IDLPDQFTA 150
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRApmllpkarwGYRMNAKLVDPMINPGLTDpYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 151 AERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPALDENkqptserVTISRDQGLR-ETTLSGLSALKP 229
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-------VVVDRDEGPRpDTTLEKLAKLKP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 230 VL-EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLV 308
Cdd:COG0183 233 AFkKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLI 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504194651 309 EINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIERI 387
Cdd:COG0183 313 EINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-386 |
1.02e-162 |
|
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: 461.56 E-value: 1.02e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 5 VIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEqSNNISRVSWLVAGLPEHVGAMT 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPATT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 85 VDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANAGP---------DRSILRPASWDID-LPDQFTAAERI 154
Cdd:cd00751 80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARrggrlglntLDGMLDDGLTDPFtGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 155 AKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPALdenkqptSERVTISRDQGLRE-TTLSGLSALKPVL-E 232
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGR-------KGPVVVDRDEGPRPdTTLEKLAKLKPAFkK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 233 GGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEINE 312
Cdd:cd00751 233 DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504194651 313 AFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIER 386
Cdd:cd00751 313 AFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-387 |
3.47e-137 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 396.38 E-value: 3.47e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEHV 80
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGAN--AGPDRSILRPAS----WDI---DLP-DQFTA 150
Cdd:PRK07801 81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAmtAGEQLGFTSPFAeskgWLHrygDQEvSQFRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 151 AERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEApaldenkqptservtISRDQGLRETTLSGLSALKPV 230
Cdd:PRK07801 161 AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------------VTVDEGPRETSLEKMAGLKPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 231 LEGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEI 310
Cdd:PRK07801 226 VEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEI 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504194651 311 NEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIERI 387
Cdd:PRK07801 306 NEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIERL 382
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-385 |
1.15e-133 |
|
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: 387.74 E-value: 1.15e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 6 IVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQsNNISRVSWLVAGLPEHVGAMTV 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAYTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 86 DCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANAG------PDRSILRPASWDiDLPDQFTA------AER 153
Cdd:TIGR01930 80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlrwgvkPGNAELEDARLK-DLTDANTGlpmgvtAEN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 154 IAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPaldenkqPTSERVTISRDQGLR-ETTLSGLSALKPVL- 231
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVK-------GRKGPVTVSSDEGIRpNTTLEKLAKLKPAFd 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 232 EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEIN 311
Cdd:TIGR01930 232 PDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEIN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504194651 312 EAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIE 385
Cdd:TIGR01930 312 EAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-387 |
6.61e-121 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 355.19 E-value: 6.61e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEHV 80
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANA--------GPDRSILRPASWDIDLPDQFTAAE 152
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPStlpaknglGHYKSPGMEERYPGIQFSQFTGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 153 RIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEApaldenKQPTSERVTISRDQGLR-ETTLSGLSALKPVL 231
Cdd:PRK06504 161 MMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEI------TRADGSGEMHTVDEGIRfDATLEGIAGVKLIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 232 EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEIN 311
Cdd:PRK06504 235 EGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVN 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504194651 312 EAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIERI 387
Cdd:PRK06504 315 EAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL 390
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-387 |
7.28e-119 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 350.22 E-value: 7.28e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGeQSNNISRVSWLVAGLPEHV 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAG-AGQNPARQAALKAGLPVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSR---VGLGANAG---PDRSILRPASWDiDLPDQFT----- 149
Cdd:PRK05790 80 PALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQaphVLPGSRWGqkmGDVELVDTMIHD-GLTDAFNgyhmg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 150 -AAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPaldenkQPTSERVTISRDQGLR-ETTLSGLSAL 227
Cdd:PRK05790 159 iTAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIK------QRKGDPVVVDTDEHPRpDTTAESLAKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 228 KPVL-EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDID 306
Cdd:PRK05790 233 RPAFdKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 307 LVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIER 386
Cdd:PRK05790 313 LIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
.
gi 504194651 387 I 387
Cdd:PRK05790 393 P 393
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-387 |
1.36e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 339.55 E-value: 1.36e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSP--IGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPE 78
Cdd:PRK08242 1 MTEAYIYDAVRTPrgKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 79 HVGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANAGPdrsilrpasWDID----LPDQFT----A 150
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGA---------WAMDpstnFPTYFVpqgiS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 151 AERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEapalDENKQptserVTISRDQGLR-ETTLSGLSALKP 229
Cdd:PRK08242 152 ADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK----DQNGL-----TILDHDEHMRpGTTMESLAKLKP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 230 VLE-----GG-----------------IHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGP 287
Cdd:PRK08242 223 SFAmmgemGGfdavalqkypeverinhVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 288 VQSTAKVLEKAGMKMGDIDLVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTT 367
Cdd:PRK08242 303 VPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRT 382
|
410 420
....*....|....*....|
gi 504194651 368 ALITMCAGGALSTGTIIERI 387
Cdd:PRK08242 383 ALITLCVGGGMGIATIIERV 402
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-387 |
4.22e-100 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 302.27 E-value: 4.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGK-RNGWLSGLHATELLGAVQKALVEK-AGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPE 78
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRsKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 79 HVGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRV----GLGANAGPDRSILRpASWDIDLpdqftAAERI 154
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVpmnhGVDFHPGLSKNVAK-AAGMMGL-----TAEML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 155 AKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPalDENKQPTservTISRDQGLR-ETTLSGLSALKPVLE- 232
Cdd:PRK08947 155 GKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGH--DADGVLK----LFDYDEVIRpETTVEALAALRPAFDp 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 233 -GGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEIN 311
Cdd:PRK08947 229 vNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 312 EAFASVVLS-------WARVHEpdmaRVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTII 384
Cdd:PRK08947 309 EAFAAQSLPclkdlglLDKMDE----KVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVF 384
|
...
gi 504194651 385 ERI 387
Cdd:PRK08947 385 ERV 387
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-387 |
1.12e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 293.82 E-value: 1.12e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEqSNNISRVSWLVAGLPEHV 80
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGE-APAIGRVAALDAGLPVTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGL-------GANAGP-------DRSILRPASWDIDLPD 146
Cdd:PRK06205 80 PGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFyttdmrwGVRGGGvqlhdrlARGRETAGGRRFPVPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 147 -QFTAAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPaldenkQPTSERVTISRDQGLR-ETTLSGL 224
Cdd:PRK06205 160 gMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVP------QRKGDPTVVDRDEHPRaDTTLESL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 225 SALKPVL----EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGM 300
Cdd:PRK06205 234 AKLRPIMgkqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 301 KMGDIDLVEINEAFASVVLSWAR---VHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGA 377
Cdd:PRK06205 314 TLDDIDLIELNEAFAAQVLAVLKewgFGADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGG 393
|
410
....*....|
gi 504194651 378 LSTGTIIERI 387
Cdd:PRK06205 394 QGLAAVFERV 403
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
5-387 |
4.16e-94 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 286.86 E-value: 4.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 5 VIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEHVGAMT 84
Cdd:PRK09051 6 VVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQETPAFN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 85 VDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGL-------GANAGPDRSilrpaswdID-----LPDQF---- 148
Cdd:PRK09051 86 VNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYllpaarwGARMGDAKL--------VDmmvgaLHDPFgtih 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 149 --TAAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPAldenkqpTSERVTISRDQGLR-ETTLSGLS 225
Cdd:PRK09051 158 mgVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKT-------RKGEVVFDTDEHVRaDTTLEDLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 226 ALKPVL--EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMG 303
Cdd:PRK09051 231 KLKPVFkkENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 304 DIDLVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTI 383
Cdd:PRK09051 311 DLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAI 390
|
....
gi 504194651 384 IERI 387
Cdd:PRK09051 391 FERL 394
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-387 |
1.35e-93 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 285.85 E-value: 1.35e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGK--RN----GWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVA 74
Cdd:PRK06445 1 LEDVYLVDFARTAFSRfrPKdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIFLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 75 GLPEHVGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANA--GPDRSIL-RPASWDIDLPDQFT-- 149
Cdd:PRK06445 81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPhiEPNPKLLtDPKYIEYDLTTGYVmg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 150 -AAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEApaldenkQPTSERVTISRDQGLR-ETTLSGLSAL 227
Cdd:PRK06445 161 lTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-------EVEGKKKVVDVDQSVRpDTSLEKLAKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 228 KPVLE-GGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDID 306
Cdd:PRK06445 234 PPAFKpDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDID 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 307 LVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIER 386
Cdd:PRK06445 314 LWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLER 393
|
.
gi 504194651 387 I 387
Cdd:PRK06445 394 V 394
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-387 |
8.15e-93 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 283.77 E-value: 8.15e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELlGAVQ-KALVEK-AGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPE 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDL-GAVPlKALMARnPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 79 HVGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSR---VGLGANAGPDRSI--------------LRPASWD 141
Cdd:PRK09050 80 SVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRapfVMGKADSAFSRQAeifdttigwrfvnpLMKAQYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 142 IDLPDQftAAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPaldenkQPTSERVTISRDQGLR-ETT 220
Cdd:PRK09050 160 VDSMPE--TAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIP------QKKGDPVVVDRDEHPRpETT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 221 LSGLSALKPVL-EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAG 299
Cdd:PRK09050 232 LEALAKLKPVFrPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 300 MKMGDIDLVEINEAFASVVLSWAR---VHEpDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGG 376
Cdd:PRK09050 312 LTIDQFDVIELNEAFAAQGLAVLRqlgLAD-DDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGV 390
|
410
....*....|.
gi 504194651 377 ALSTGTIIERI 387
Cdd:PRK09050 391 GQGIALAIERV 401
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
5-386 |
4.16e-92 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 283.96 E-value: 4.16e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 5 VIVEATRSPIGK-RNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEHVGAM 83
Cdd:PLN02287 49 VIVAAYRTPICKaKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 84 TVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANAG-PDRSILRPASWDIDLPDQFTaAERIAKRRGITR 162
Cdd:PLN02287 129 TVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGvNPRVESFSQAQDCLLPMGIT-SENVAERFGVTR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 163 EEIDEFGFNSQARAKQAWDEGRFDREISPIEAPALDEnKQPTSERVTISRDQGLRE-TTLSGLSALKPVL-EGGIHTAGT 240
Cdd:PLN02287 208 EEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDP-KTGEEKPIVISVDDGIRPnTTLADLAKLKPVFkKNGTTTAGN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 241 SSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEINEAFASVVLS 320
Cdd:PLN02287 287 SSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVY 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504194651 321 WARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELER--TDQTTALITMCAGGALSTGTIIER 386
Cdd:PLN02287 367 CCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgKDCRFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-387 |
5.52e-92 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 282.43 E-value: 5.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSP--IGKR-NGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLP 77
Cdd:PRK06025 1 MAEAYIIDAVRTPrgIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 78 EHVGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVG-------------LGANAGPDR-SILRPASwdid 143
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAamaaedmaagkppLGMGSGNLRlRALHPQS---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 144 lpDQFTAAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAP----ALDENKQPTSErvtisrdqglreT 219
Cdd:PRK06025 157 --HQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDdgsvALDHEEFPRPQ------------T 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 220 TLSGLSALKPVLEG---------------------------GIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVS 272
Cdd:PRK06025 223 TAEGLAALKPAFTAiadyplddkgttyrglinqkypdleikHVHHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 273 QALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRL 352
Cdd:PRK06025 303 MANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSIL 382
|
410 420 430
....*....|....*....|....*....|....*
gi 504194651 353 ITTALHELERTDQTTALITMCAGGALSTGTIIERI 387
Cdd:PRK06025 383 IGTVLDELERRGLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-387 |
9.25e-92 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 281.51 E-value: 9.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGK-RNGWLSGLHATELLG-AVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPe 78
Cdd:PRK07851 1 MPEAVIVSTARSPIGRaFKGSLKDMRPDDLAAqMVRAALDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 79 HVGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLG-ANAGPD-----------RSILRPAS----W-- 140
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGnSDSLPDtknplfaeaqaRTAARAEGgaeaWhd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 141 ---DIDLPDQFTA----AERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPaldenkqptsERVTISRD 213
Cdd:PRK07851 160 preDGLLPDVYIAmgqtAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP----------DGTVVSTD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 214 QGLRE-TTLSGLSALKPVL-EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQST 291
Cdd:PRK07851 230 DGPRAgTTYEKVSQLKPVFrPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEAS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 292 AKVLEKAGMKMGDIDLVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALIT 371
Cdd:PRK07851 310 KQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLET 389
|
410
....*....|....*.
gi 504194651 372 MCAGGALSTGTIIERI 387
Cdd:PRK07851 390 MCVGGGQGMAMVLERL 405
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-387 |
3.79e-89 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 274.32 E-value: 3.79e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGK-RNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEH 79
Cdd:PRK07661 1 MREAVIVAGARTPVGKaKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 80 VGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANagpdrsILRPASWDIDLPDQF-----TAAERI 154
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGH------VVRPNPRLVEAAPEYymgmgHTAEQV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 155 AKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAP--ALDENKQPTSERVTISRDQGLR-ETTLSGLSALKPVL 231
Cdd:PRK07661 155 AVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTlrTVGENNKLQEETITFSQDEGVRaDTTLEILGKLRPAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 232 E-GGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEI 310
Cdd:PRK07661 235 NvKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFEL 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504194651 311 NEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIERI 387
Cdd:PRK07661 315 NEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFELL 391
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
6-387 |
2.18e-88 |
|
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: 272.43 E-value: 2.18e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 6 IVEATRSPIGKRNGWLSGLHATELLGAVQKALVEK-AGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEHVGAMT 84
Cdd:TIGR02430 5 ICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVSVPGTT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 85 VDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVG--LGANAGP--------DRSI-------LRPASWDIDLPDQ 147
Cdd:TIGR02430 85 VNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPfvMGKADSAfsrsakieDTTIgwrfinpLMKALYGVDSMPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 148 ftAAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPaldenkQPTSERVTISRDQGLR-ETTLSGLSA 226
Cdd:TIGR02430 165 --TAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIP------QKKGEPTVVDQDEHPRpETTLEGLAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 227 LKPVL-EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDI 305
Cdd:TIGR02430 237 LKPVVrPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 306 DLVEINEAFASVVLSWARVH--EPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTI 383
Cdd:TIGR02430 317 DVIELNEAFAAQALAVLRELglADDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALA 396
|
....
gi 504194651 384 IERI 387
Cdd:TIGR02430 397 IERV 400
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-385 |
4.97e-87 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 268.95 E-value: 4.97e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKR-NGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEH 79
Cdd:PRK07108 1 MTEAVIVSTARTPLAKSwRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 80 VGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANagpdRSILRPASWDIDLPDQF----TAAERIA 155
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMN----RHMLREGWLVEHKPEIYwsmlQTAENVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 156 KRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPALDENK---QPTSERVTISRDQGLRE-TTLSGLSALKPVL 231
Cdd:PRK07108 157 KRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKatgRLFTKEVTVSADEGIRPdTTLEGVSKIRSAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 232 EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEIN 311
Cdd:PRK07108 237 PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELN 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504194651 312 EAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIE 385
Cdd:PRK07108 317 EAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
6-387 |
3.66e-86 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 266.87 E-value: 3.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 6 IVEATRSPIGK-RNGWLSGLHATELLGAVQKALVEKA-GIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEHVGAM 83
Cdd:PRK09052 10 IVAATRTPVGKaPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPNSVGGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 84 TVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANagpdRSILRPASWDIDlPDQFTA------AERIAKR 157
Cdd:PRK09052 90 TVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGN----KPSMSPAIFARD-ENVGIAygmgltAEKVAEQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 158 RGITREEIDEFGFNSQARAKQAWDEGRFDREISPIE----APALDENKQPTSERvTISRDQGLR-ETTLSGLSALKPVLE 232
Cdd:PRK09052 165 WKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEiterFPDLATGEVDVKTR-TVDLDEGPRaDTSLEGLAKLKPVFA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 233 -GGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEIN 311
Cdd:PRK09052 244 nKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIELN 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504194651 312 EAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIERI 387
Cdd:PRK09052 324 EAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFERL 399
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-385 |
1.68e-85 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 265.04 E-value: 1.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGeQSNNISRVSWLVAGLPEHV 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGG-QGQIPSRQAARAAGIPWEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSrvglgaNAgPdrSILRPASW----------DIDLPDQFTA 150
Cdd:PRK08235 80 QTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMS------NA-P--YILPGARWgyrmgdneviDLMVADGLTC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 151 A----------ERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPaldenkQPTSERVTISRDQGLRE-T 219
Cdd:PRK08235 151 AfsgvhmgvygGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIP------QRKGDPIVVAKDEAPRKdT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 220 TLSGLSALKPVL--EGGIhTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEK 297
Cdd:PRK08235 225 TIEKLAKLKPVFdkTGTI-TAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 298 AGMKMGDIDLVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGA 377
Cdd:PRK08235 304 TGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGG 383
|
....*...
gi 504194651 378 LSTGTIIE 385
Cdd:PRK08235 384 QGDAVLIE 391
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-387 |
7.85e-82 |
|
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: 255.25 E-value: 7.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 3 NPVIVEATRSPIGKRNGWLSGLHATELLGA--VQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEHV 80
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTRAEDLSAhlMSKLLARNPKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRV----GLGANAGPDRSILRPASWdidlpdQFTAAERIAK 156
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVpmmhGVDFHPGMSLHVAKAAGM------MGLTAEMLGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 157 RRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPALDENKQptservTISRDQGLR-ETTLSGLSALKPVLE--G 233
Cdd:TIGR02445 155 MHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLK------QFDYDEVIRpETTVESLAALRPAFDpkN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 234 GIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEINEA 313
Cdd:TIGR02445 229 GTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504194651 314 FASVVLSWAR---VHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIERI 387
Cdd:TIGR02445 309 FAAQALPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFERV 385
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-387 |
7.36e-80 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 250.85 E-value: 7.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWLVAGLPEHV 80
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLgANAGPDRSILRPAS-WDIDLPDQFT---------- 149
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPF-VMGKAESAFSRDAKvFDTTIGARFPnpkivaqygn 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 150 -----AAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPAldENKQPTserVTISRDQGLR-ETTLSG 223
Cdd:PRK08131 160 dsmpeTGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQ--GRKLPP---KLVAEDEHPRpSSTVEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 224 LSALKPVLEGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMG 303
Cdd:PRK08131 235 LTKLKPLFEGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 304 DIDLVEINEAFASVVLSWARVHEPDM--ARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTG 381
Cdd:PRK08131 315 DMDIIEINEAFASQVLGCLKGLGVDFddPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLA 394
|
....*.
gi 504194651 382 TIIERI 387
Cdd:PRK08131 395 MVIERV 400
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
5-386 |
1.28e-77 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 245.66 E-value: 1.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 5 VIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEqSNNISRVSWLVAGLPEHVGAMT 84
Cdd:PRK08963 8 AIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPE-APNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 85 VDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANAgPDRSILRPASWDIDLPDQFT--------------- 149
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSK-KLARALVDLNKARTLGQRLKlfsrlrlrdllpvpp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 150 -------------AAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPALDEnkqptservTISRDQGL 216
Cdd:PRK08963 166 avaeystglrmgdTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ---------PLEEDNNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 217 RE-TTLSGLSALKPVL--EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYH-LDGPVQSTA 292
Cdd:PRK08963 237 RGdSTLEDYAKLRPAFdrKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQDmLLGPAYATP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 293 KVLEKAGMKMGDIDLVEINEAFASVVLS---------WAR--------VHEPDMARVNVNGGAIALGHPVGSTGSRLITT 355
Cdd:PRK08963 317 LALERAGLTLADLTLIDMHEAFAAQTLAnlqmfaserFAReklgrsqaIGEVDMSKFNVLGGSIAYGHPFAATGARMITQ 396
|
410 420 430
....*....|....*....|....*....|.
gi 504194651 356 ALHELERTDQTTALITMCAGGALSTGTIIER 386
Cdd:PRK08963 397 TLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-386 |
1.44e-77 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 244.41 E-value: 1.44e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGeQSNNISRVSWLVAGLPEHV 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAG-AGQNPARQAAIKAGLPHSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMS---------RVGLG-ANAGPDRSILRPASWDI--DLPDQF 148
Cdd:PRK05656 80 PAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSlapyvlpgaRTGLRmGHAQLVDSMITDGLWDAfnDYHMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 149 TAaERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPaldenkQPTSERVTISRDQGLR-ETTLSGLSAL 227
Cdd:PRK05656 160 TA-ENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIP------QRKGEPLAFATDEQPRaGTTAESLAKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 228 KPVL-EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDID 306
Cdd:PRK05656 233 KPAFkKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 307 LVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIER 386
Cdd:PRK05656 313 LIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-387 |
2.69e-69 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 222.33 E-value: 2.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 3 NPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALveKAGIEAgDVEQVIGGCVTQYGeqsNNISRVSWLVAGLPEHVGA 82
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGMER-EIDDVILGNVVGPG---GNVARLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 83 MTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRvglganaGPDRSILRPASWDIDLPDQFTAAERIAKRRGITR 162
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTST-------SPFQNRARFSPETIGDPDMGVAAEYVAERYNITR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 163 EEIDEFGFNSQARAKQAWDEGRFDREISPIEApALDENKQPTSERVTIsrdqglrettlsgLSALKPV-LEGGIHTAGTS 241
Cdd:PRK06690 149 EMQDEYACLSYKRTLQALEKGYIHEEILSFNG-LLDESIKKEMNYERI-------------IKRTKPAfLHNGTVTAGNS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 242 SQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEINEAFASVVLSW 321
Cdd:PRK06690 215 CGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVVAC 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504194651 322 ARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIERI 387
Cdd:PRK06690 295 AKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-376 |
9.15e-69 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 221.81 E-value: 9.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSWlVAGLPEHV 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAY-HAGLPFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 81 GAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANA----GPDRSILRpaSWDID-------LPDQF- 148
Cdd:PRK06366 80 TKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSdlrwGPKHLLHK--NYKIDdamlvdgLIDAFy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 149 -----TAAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEapaldenkqptservTISRDQGLRETTLSG 223
Cdd:PRK06366 158 fehmgVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------------DLDRDEGIRKTTMED 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 224 LSALKPVLE-GGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKM 302
Cdd:PRK06366 223 LAKLPPAFDkNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSI 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504194651 303 GDIDLVEINEAF--ASVVLSwARVHePDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGG 376
Cdd:PRK06366 303 DYYDLVEHNEAFsiASIIVR-DQLK-IDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGG 376
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
5-385 |
1.08e-68 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 221.69 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 5 VIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGeQSNNISRVSWLVAGLPEHVGAMT 84
Cdd:PRK06954 10 VIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAG-QGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 85 VDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMS---------RVGLGANAGpdrSILRPASWDiDLPDQF------- 148
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTnapyllpkaRGGMRMGHG---QVLDHMFLD-GLEDAYdkgrlmg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 149 TAAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPAldenkqpTSERVTISRDQGLRETTLSGLSALK 228
Cdd:PRK06954 165 TFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAG-------KKGDTVIDRDEQPFKANPEKIPTLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 229 PVL-EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDL 307
Cdd:PRK06954 238 PAFsKTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDL 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504194651 308 VEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIE 385
Cdd:PRK06954 318 FEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-387 |
1.93e-67 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 218.36 E-value: 1.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPV-IVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQyGEQSNNISRVSWLVAGLPEH 79
Cdd:PRK06633 1 MTKPVyITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVIT-GGSGQNPARQTLIHAGIPKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 80 VGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMS------RVGLGANAGpDRSILRPASWDiDLPDQFTA--- 150
Cdd:PRK06633 80 VPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmhgsYIRAGAKFG-DIKMVDLMQYD-GLTDVFSGvfm 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 151 ---AERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPAldenKQPTServTISRDQGLR-ETTLSGLSA 226
Cdd:PRK06633 158 gitAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTI----KKTTS---LFDHDETVRpDTSLEILSK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 227 LKPVLE-GGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDI 305
Cdd:PRK06633 231 LRPAFDkNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 306 DLVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIE 385
Cdd:PRK06633 311 EVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
..
gi 504194651 386 RI 387
Cdd:PRK06633 391 AV 392
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-387 |
3.17e-65 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 213.73 E-value: 3.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPV-IVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQyGEQSNNISRVSWLVAGLPEH 79
Cdd:PRK08170 1 MARPVyIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMP-SPDEANIARVVALRLGCGEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 80 VGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRV-------------GLGANAGPDRSI-----LRPASWD 141
Cdd:PRK08170 80 VPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHApllfsekmvrwlaGWYAAKSIGQKLaalgkLRPSYLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 142 --IDLPDQFT----------AAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFdREISPIeapaLDENKQptservT 209
Cdd:PRK08170 160 pvIGLLRGLTdpvvglnmgqTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPL----FDRDGK------F 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 210 ISRDQGLR-ETTLSGLSALKPVLEG--GIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDG 286
Cdd:PRK08170 229 YDHDDGVRpDSSMEKLAKLKPFFDRpyGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 287 PVQSTAKVLEKAGMKMGDIDLVEINEAFASVVL----SWA-----RVH--------EPDMARVNVNGGAIALGHPVGSTG 349
Cdd:PRK08170 309 PVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLaclaAWAdeeycREQlgldgalgELDRERLNVDGGAIALGHPVGASG 388
|
410 420 430
....*....|....*....|....*....|....*...
gi 504194651 350 SRLITTALHELERTDQTTALITMCAGGALSTGTIIERI 387
Cdd:PRK08170 389 ARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
3-387 |
5.78e-65 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 211.88 E-value: 5.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 3 NPVIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTqygeqSNNI----SRVSWLVAGLPE 78
Cdd:PLN02644 2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVL-----SANLgqapARQAALGAGLPP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 79 HVGAMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMS---------RVG--LGANAGPDrSILRPASWDI--DLP 145
Cdd:PLN02644 77 STICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSnapkylpeaRKGsrLGHDTVVD-GMLKDGLWDVynDFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 146 dQFTAAERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPAlDENKQPTservTISRDQGLRETTLSGLS 225
Cdd:PLN02644 156 -MGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPG-GRGRPSV----IVDKDEGLGKFDPAKLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 226 ALKPVLE--GGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMG 303
Cdd:PLN02644 230 KLRPSFKedGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEAS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 304 DIDLVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTI 383
Cdd:PLN02644 310 QVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIV 389
|
....
gi 504194651 384 IERI 387
Cdd:PLN02644 390 VELM 393
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
5-257 |
4.23e-62 |
|
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: 200.22 E-value: 4.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 5 VIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNnISRVSWLVAGLPEHVGAMT 84
Cdd:pfam00108 2 VIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQN-PARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 85 VDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGLGANAGPDRSILRPASW--DIDLPDQFT----------AAE 152
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKHGDEKkhDLLIPDGLTdafngyhmglTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 153 RIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEAPalDENKQPtservTISRDQGLR-ETTLSGLSALKPVL 231
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVK--GRKGKP-----TVDKDEGIRpPTTAEPLAKLKPAF 233
|
250 260
....*....|....*....|....*..
gi 504194651 232 E-GGIHTAGTSSQISDGAAAVLWMDED 257
Cdd:pfam00108 234 DkEGTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
5-386 |
4.88e-52 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 178.94 E-value: 4.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 5 VIVEATRSPIGKRNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYgEQSNNISRVSWLVAGLPEHVGAMT 84
Cdd:PRK09268 10 AILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKH-SRDFNLTRECVLGSALSPYTPAYD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 85 VDCQCGSGQQANGLVAGLIAAGAIDIGIACGI-----------EAMSRVGLGANAG---PDR----SILRPASWDIDLP- 145
Cdd:PRK09268 89 LQQACGTGLEAAILVANKIALGQIDSGIAGGVdttsdapiavnEGLRKILLELNRAkttGDRlkalGKLRPKHLAPEIPr 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 146 --DQFTA------AERIAKRRGITREEIDEFGFNSQARAKQAWDEGRFDREISPIEApaldenkqptservtISRDQGLR 217
Cdd:PRK09268 169 ngEPRTGlsmgehAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLG---------------LTRDNNLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 218 -ETTLSGLSALKPVL---EGGIHTAGTSSQISDGAAAVLWMDEDKAKALGLRPRARIVSqALVGAEPYYH-----LDGPV 288
Cdd:PRK09268 234 pDSSLEKLAKLKPVFgkgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVD-AETAAVDFVHgkeglLMAPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 289 QSTAKVLEKAGMKMGDIDLVEINEAFASVVLS----W-------------ARVHEPDMARVNVNGGAIALGHPVGSTGSR 351
Cdd:PRK09268 313 YAVPRLLARNGLTLQDFDFYEIHEAFASQVLAtlkaWedeeycrerlgldAPLGSIDRSKLNVNGSSLAAGHPFAATGGR 392
|
410 420 430
....*....|....*....|....*....|....*
gi 504194651 352 LITTALHELERTDQTTALITMCAGGALSTGTIIER 386
Cdd:PRK09268 393 IVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-385 |
2.02e-40 |
|
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: 147.25 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 7 VEATRSPIGKRNGWLSGLH---ATELLGAVQKALVEKAGIEAGDVEQVIGGCVTQYGEQSNnISRVSWLVAGLPEHVGAM 83
Cdd:cd00826 1 AGAAMTAFGKFGGENGADAndlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQN-CAQQAAMHAGGLQEAPAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 84 TVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVglganagpDRSIlrPASWDIDlpdqftaaerIAKRRGITRE 163
Cdd:cd00826 80 GMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETS--------AENN--AKEKHID----------VLINKYGMRA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 164 EIDEFGFNSQARAKQAWDEGRFDREISPIEAPALDENKqpTSERVTISRDQGlrETTLSGLSALKPVLEG-GIHTAGTSS 242
Cdd:cd00826 140 CPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDI--HSDADEYIQFGD--EASLDEIAKLRPAFDKeDFLTAGNAC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 243 QISDGAAAVLWMDEDKA-------KALGLRPRARIVSQALVGAEPYYHL----DGPVQSTAKVLEKAGMKMGDIDLVEIN 311
Cdd:cd00826 216 GLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKmvggDGPIEAARKALEKAGLGIGDLDLIEAH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 312 EAFASVV------LSW-------ARVHEPDMAR-----VNVNGGAIALGHPVGSTGSRLITTALHELERTDQTTA----- 368
Cdd:cd00826 296 DAFAANAcatneaLGLcpegqggALVDRGDNTYggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQgagag 375
|
410
....*....|....*..
gi 504194651 369 LITMCAGGALSTGTIIE 385
Cdd:cd00826 376 LALLCIGGGGGAAMCIE 392
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
264-386 |
4.07e-40 |
|
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: 138.54 E-value: 4.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 264 LRPRARIVSQALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEINEAFASVVLSWARVHEPDMARVNVNGGAIALGH 343
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 504194651 344 PVGSTGSRLITTALHELERTDQTTALITMCAGGALSTGTIIER 386
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
32-360 |
2.33e-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: 88.47 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 32 AVQKALvEKAGIEAGDVEQVIGGCVTQYGEQSNNISRVSwLVAGLPeHVGAMTVDCQCGSGQQANGLVAGLIAAGAIDIG 111
Cdd:cd00829 23 AARAAL-DDAGLEPADIDAVVVGNAAGGRFQSFPGALIA-EYLGLL-GKPATRVEAAGASGSAAVRAAAAAIASGLADVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 112 IACGIEAMSRVGLGANAGPdrsILRPASWDI-DLPDQFT-------AAERIAKRRGITREEIDEFGFNSQARAkqawdeg 183
Cdd:cd00829 100 LVVGAEKMSDVPTGDEAGG---RASDLEWEGpEPPGGLTppalyalAARRYMHRYGTTREDLAKVAVKNHRNA------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 184 rfdreispieapALDENKQptsERVTISRDQGLRETTLSGlsalkPVleggihTAGTSSQISDGAAAVLWMDEDKAKALG 263
Cdd:cd00829 170 ------------ARNPYAQ---FRKPITVEDVLNSRMIAD-----PL------RLLDCCPVSDGAAAVVLASEERARELT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 264 LRPrARIVSQA-------LVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEINEAFASVVL-------------SWAR 323
Cdd:cd00829 224 DRP-VWILGVGaasdtpsLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELlaledlgfcekgeGGKL 302
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 504194651 324 VHEPDMAR-----VNVNGGAIALGHPVGSTGSRLITTALHEL 360
Cdd:cd00829 303 VREGDTAIggdlpVNTSGGLLSKGHPLGATGLAQAVEAVRQL 344
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-360 |
7.46e-13 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 69.16 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 1 MGNPVIVEATRSPIGKRngWLSGLH--ATEllgAVQKALvEKAGIEAGDVEQVIGGCVT--QYGEQSNnISRVSWLVAGL 76
Cdd:PRK06064 1 MRDVAIIGVGQTKFGEL--WDVSLRdlAVE---AGLEAL-EDAGIDGKDIDAMYVGNMSagLFVSQEH-IAALIADYAGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 77 PeHVGAMTVDCQCGSGQQA--NGLVAglIAAGAIDIGIACGIEAMSRVGlgaNAGPDRSILRPAS--WDIDLPDQFTA-- 150
Cdd:PRK06064 74 A-PIPATRVEAACASGGAAlrQAYLA--VASGEADVVLAAGVEKMTDVP---TPDATEAIARAGDyeWEEFFGATFPGly 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 151 ---AERIAKRRGITREEIDEFGFNSQARAkqawdegrfdreispieapALDENKQPTSErvtISRDQGLRETTLSglSAL 227
Cdd:PRK06064 148 aliARRYMHKYGTTEEDLALVAVKNHYNG-------------------SKNPYAQFQKE---ITVEQVLNSPPVA--DPL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 228 KpVLEggihtagtSSQISDGAAAVLWMDEDKAKALGLRPrARIVSQ-------ALVGAEPYYHLDGPVQSTAKVLEKAGM 300
Cdd:PRK06064 204 K-LLD--------CSPITDGAAAVILASEEKAKEYTDTP-VWIKASgqasdtiALHDRKDFTTLDAAVVAAEKAYKMAGI 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504194651 301 KMGDIDLVEINEAF--ASVV----LSWARVHEP-DMAR-----------VNVNGGAIALGHPVGSTGSRLITTALHEL 360
Cdd:PRK06064 274 EPKDIDVAEVHDCFtiAEILayedLGFAKKGEGgKLARegqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQL 351
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
244-376 |
1.17e-10 |
|
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: 61.31 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 244 ISDGAAAVLWMDEDKAKALGLRPRARIVSQALVGAEPYYHL----DGPVQSTAKVLEKAGMKMGDIDLVEINEAFASVVL 319
Cdd:cd00327 100 FGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPavsgEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGD 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504194651 320 SWAR--VHEPDMAR-VNVNGGAIALGHPVGSTGSRLITTALHELER-----TDQ--TTALITMCAGG 376
Cdd:cd00327 180 AVELalGLDPDGVRsPAVSATLIMTGHPLGAAGLAILDELLLMLEHefippTPRepRTVLLLGFGLG 246
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
17-359 |
6.67e-09 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 57.01 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 17 RNGWLSGLHATELLGAVQKALVEKAGIEAGDVEQV-----IGGCVTQYGEQSNNISRVSWLVAGLP--EHVGAmtvdcqC 89
Cdd:PRK06289 17 RNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVhvgnfFGELFAGQGHLGAMPATVHPALWGVPasRHEAA------C 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 90 GSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGlGANAGpdrSILRPASW--------DIDLPDQFTA-AERIAKRRGI 160
Cdd:PRK06289 91 ASGSVATLAAMADLRAGRYDVALVVGVELMKTVP-GDVAA---EHLGAAAWtghegqdaRFPWPSMFARvADEYDRRYGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 161 TREEIDEFGFNSQARAKqawdegrfdreispieapaldenKQPTSErvtiSRDQGLRETTLSGLSALKPVLEGGIHTAgT 240
Cdd:PRK06289 167 DEEHLRAIAEINFANAR-----------------------RNPNAQ----TRGWAFPDEATNDDDATNPVVEGRLRRQ-D 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 241 SSQISDGAAAVLWMDEDKAKAL-GLRPRARI-----------VSQALVGA--EPYY--HLDGPVQSTakvLEKAGMKMGD 304
Cdd:PRK06289 219 CSQVTDGGAGVVLASDAYLRDYaDARPIPRIkgwghrtaplgLEQKLDRSagDPYVlpHVRQAVLDA---YRRAGVGLDD 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504194651 305 IDLVEINEAFASVVL-------------SWARVHEPDMA-----RVNVNGGAIALGHPVGSTGSRLITTALHE 359
Cdd:PRK06289 296 LDGFEVHDCFTPSEYlaidhigltgpgeSWKAIENGEIAiggrlPINPSGGLIGGGHPVGASGVRMLLDAAKQ 368
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
82-353 |
4.78e-08 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 54.51 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 82 AMTVDCQCGSGQQANGLVAGLIAAGAIDIGIACGIEAMSRVGlgANAGPDRsILRPASWDIDLP-DQFTAAERIAKRRGI 160
Cdd:PTZ00455 113 AMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVS--ARVGGDY-LARAADYRRQRKlDDFTFPCLFAKRMKY 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 161 TREEiDEFGFNSQAR-AKQAWDEGrfdreispieapaldeNKQPTSERVT--ISRDQGLRETTLS----GLSALKPVLEg 233
Cdd:PTZ00455 190 IQEH-GHFTMEDTARvAAKAYANG----------------NKNPLAHMHTrkLSLEFCTGASDKNpkflGNETYKPFLR- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 234 gihtAGTSSQISDGAAAVLWMDEDKAKALGLRPR-ARIVS-QALVGAEPYYHLDGP--------VQSTAKVLEKAGMKMG 303
Cdd:PTZ00455 252 ----MTDCSQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEiKSLACASGNLYEDPPdatrmftsRAAAQKALSMAGVKPS 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504194651 304 DIDLVEINEAFASV------VLSWARV-HEPDMAR-----------VNVNGGAIALGHPVGSTGSRLI 353
Cdd:PTZ00455 328 DLQVAEVHDCFTIAellmyeALGIAEYgHAKDLIRngatalegripVNTGGGLLSFGHPVGATGVKQI 395
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
242-349 |
1.00e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 50.33 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 242 SQISDGAAAVLWMDEDKAKALGLRPRARIVSQA-----LVGAEPyYHLDGPVQSTAKVLEKAGMKMGDIDLVEINEAFAS 316
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALQRAVRFRARAHVndflpLSRRDP-LAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTI 291
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504194651 317 VVL------------SWARVHEPDMAR------VNVNGGAIALGHPVGSTG 349
Cdd:PRK07516 292 AELieyeamglappgQGARAIREGWTAkdgklpVNPSGGLKAKGHPIGATG 342
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
32-349 |
1.18e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 46.82 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 32 AVQKALvEKAGIEAGDVEQVIGGCVtqYGEqSNNISRVSWlvaglpeHVGaMT------VDCQCGSGQQANGLVAGLIAA 105
Cdd:PRK08256 29 AGRAAL-ADAGIDYDAVQQAYVGYV--YGD-STSGQRALY-------EVG-MTgipivnVNNNCSTGSTALFLARQAVRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 106 GAIDIGIACGIEAMSRVGLGAnAGPDRSI----LRPASWDIDLPDQFTAAERIAKRRGitREEIDEFGFNSQARAKqawd 181
Cdd:PRK08256 97 GAADCALALGFEQMQPGALGS-VWDDRPSplerFDKALAELQGFDPAPPALRMFGGAG--REHMEKYGTTAETFAK---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 182 egrfdreispIEAPAldeNKQPTSERVTISRDqglrETTLSGLSALKPVLEGgiHTAGTSSQISDGAAAVLWMDEDKAKA 261
Cdd:PRK08256 170 ----------IGVKA---RRHAANNPYAQFRD----EYTLEDVLASPMIWGP--LTRLQCCPPTCGAAAAIVCSEEFARK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 262 LGLRPRARIVSQA----------------LVGAepyyhlDGPVQSTAKVLEKAGMKMGDIDLVEINEAFAS-VVLSWAR- 323
Cdd:PRK08256 231 HGLDRAVEIVAQAmttdtpstfdgrsmidLVGY------DMTRAAAQQVYEQAGIGPEDIDVVELHDCFSAnELLTYEAl 304
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 504194651 324 -----------VHEPDM---ARVNVN--GGAIALGHPVGSTG 349
Cdd:PRK08256 305 glcpegeaekfIDDGDNtygGRWVVNpsGGLLSKGHPLGATG 346
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
32-353 |
1.31e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 43.68 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 32 AVQKALvEKAGIEAGDVEQVIGGCVTQYGEQ---SNNISRVSWLVAGLPEHVGAMtvdcqCGSGQQANGLVAGLIAAGAI 108
Cdd:PRK12578 28 SIKEAL-NDAGVSQTDIELVVVGSTAYRGIElypAPIVAEYSGLTGKVPLRVEAM-----CATGLAASLTAYTAVASGLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 109 DIGIACGIEAMSRV------GLGANAGpdrsilrPASWDI-----DLPDQFTA-AERIAKRRGITREEIDEFGFNSQARA 176
Cdd:PRK12578 102 DMAIAVGVDKMTEVdtstslAIGGRGG-------NYQWEYhfygtTFPTYYALyATRHMAVYGTTEEQMALVSVKAHKYG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 177 KQAwDEGRFDREIspieapaldenkqpTSERVTISRdqglrettlsglsalkpVLEGGIHTAgTSSQISDGAAAVLWMDE 256
Cdd:PRK12578 175 AMN-PKAHFQKPV--------------TVEEVLKSR-----------------AISWPIKLL-DSCPISDGSATAIFASE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 257 DKAKALGLRPRARIVS-------QALVGAEPYYHLDGPVQSTAKVLEKAGMKMGDIDLVEINEAF--ASVV----LSWAR 323
Cdd:PRK12578 222 EKVKELKIDSPVWITGigyandyAYVARRGEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFtiAEIMgyedLGFTE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 504194651 324 -------VHEPDMAR-----VNVNGGAIALGHPVGSTGSRLI 353
Cdd:PRK12578 302 kgkggkfIEEGQSEKggkvgVNLFGGLKAKGHPLGATGLSMI 343
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
29-167 |
1.74e-03 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 40.01 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 29 LLGAVQKALVEkAGIEAGDVEQVIGGcvTQYGEQSNNISRVSWLVAGLPEHVGAMTVDCQCGSGQQANGLVAGLIAAGAI 108
Cdd:PRK06157 31 MVEAFLEALAD-AGIEPKDIDAAWFG--THYDEIGSGKSGTPLSRALRLPNIPVTRVENFCATGSEAFRGAVYAVASGAY 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504194651 109 DIGIACGIEAMSRVGLG----ANAGPDRSILRPaswDIDLPDQFT-AAERIAKRRGITREEIDE 167
Cdd:PRK06157 108 DIALALGVEKLKDTGYGglpvANPGTLADMTMP---NVTAPGNFAqLASAYAAKYGVSREDLKR 168
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
244-378 |
1.74e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 40.06 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504194651 244 ISDGAAAVLWMDEDKAKALGLRPrARIVSQAlvgaepyYHLDGPV---------QSTAKVLEKA-GMKMGDIDLVEINEA 313
Cdd:PRK07937 204 ITDGAAAVVLAAGDRARELRERP-AWITGIE-------HRIESPSlgardltrsPSTALAAEAAtGGDAGGVDVAELHAP 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504194651 314 FAS--VVLSWArVHEPDMARVNVNGGAIAlGHPVGSTGSRLITTALHELERTDQTTALITMCAGGAL 378
Cdd:PRK07937 276 FTHqeLILREA-LGLGDKTKVNPSGGALA-ANPMFAAGLERIGEAARHIWDGSARRALAHATSGPAL 340
|
|
| |
