|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
2-403 |
0e+00 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 802.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 2 SEEAFIYEAIRTPRGK-QKNGSLHEVKPLSLVVGLIDELRKRHpDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMP 80
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKgKKDGSLHEVKPVRLAAGLLEALRDRN-GLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 81 VTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGGAMGLDPATNYDVMFVPQSIGADLIATIE 160
Cdd:PRK08242 80 ETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 161 GFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQNGLLILDHDEHMRPDTTKEGLAKLKPAFEGLAALGGFDDVALQ 240
Cdd:PRK08242 160 GFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMGGFDAVALQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 241 KYHWVEKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRKVLDRAGLTVDD 320
Cdd:PRK08242 240 KYPEVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 321 IDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGGGMGVATII 400
Cdd:PRK08242 320 IDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATII 399
|
...
gi 2085608637 401 ERV 403
Cdd:PRK08242 400 ERV 402
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
3-403 |
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: 520.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 3 EEAFIYEAIRTPRGKQkNGSLHEVKPLSLVVGLIDELRKRHpDLDENLISDVILGCVSPVGdQGGDIARAAVLASGMPVT 82
Cdd:COG0183 2 REVVIVDAVRTPFGRF-GGALADVRADDLGAAVIKALLERA-GLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 83 SGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGGAMGLD-PATNYDVM----------FVPQSI 151
Cdd:COG0183 79 VPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRmNAKLVDPMinpgltdpytGLSMGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 152 GADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPV--RDQNGLLILDHDEHMRPDTTKEGLAKLKPAFEGla 229
Cdd:COG0183 159 TAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVevPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKK-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 230 alGGfddvalqkyhwvekinhVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRK 309
Cdd:COG0183 237 --DG-----------------TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 310 VLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLC 389
Cdd:COG0183 298 ALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMC 377
|
410
....*....|....
gi 2085608637 390 IGGGMGVATIIERV 403
Cdd:COG0183 378 IGGGQGIALIIERV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
6-402 |
6.16e-171 |
|
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: 482.75 E-value: 6.16e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 6 FIYEAIRTPRGKqKNGSLHEVKPLSLVVGLIDELRKRHPdLDENLISDVILGCVSPVGdQGGDIARAAVLASGMPVTSGG 85
Cdd:cd00751 1 VIVSAVRTPIGR-FGGALKDVSADDLGAAVIKALLERAG-LDPEEVDDVIMGNVLQAG-EGQNPARQAALLAGLPESVPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 86 VQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGGAMGLDPATNYDVMFV-----------PQSIGAD 154
Cdd:cd00751 78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLddgltdpftglSMGITAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 155 LIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQN--GLLILDHDEHMRPDTTKEGLAKLKPAFEGlaalg 232
Cdd:cd00751 158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGrkGPVVVDRDEGPRPDTTLEKLAKLKPAFKK----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 233 gfddvalqkyhwvekiNHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRKVLD 312
Cdd:cd00751 233 ----------------DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 313 RAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGG 392
Cdd:cd00751 297 RAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGG 376
|
410
....*....|
gi 2085608637 393 GMGVATIIER 402
Cdd:cd00751 377 GQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
7-401 |
1.31e-152 |
|
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: 436.27 E-value: 1.31e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 7 IYEAIRTPRGKQkNGSLHEVKPLSLVVGLIDELRKRHPdLDENLISDVILGCVSPVGDQGgDIARAAVLASGMPVTSGGV 86
Cdd:TIGR01930 1 IVAAARTPIGKF-GGSLKDVSAEDLGAAVIKELLERNP-LDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 87 QLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMG-SDGGAMGLDP--ATNYDVM---------FVPQSIGAD 154
Cdd:TIGR01930 78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGvPRSLRWGVKPgnAELEDARlkdltdantGLPMGVTAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 155 LIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQ--NGLLILDHDEHMRPDTTKEGLAKLKPAFEGlaalg 232
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKgrKGPVTVSSDEGIRPNTTLEKLAKLKPAFDP----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 233 gfddvalqkyhwvekiNHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRKVLD 312
Cdd:TIGR01930 233 ----------------DGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 313 RAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGG 392
Cdd:TIGR01930 297 KAGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGG 376
|
....*....
gi 2085608637 393 GMGVATIIE 401
Cdd:TIGR01930 377 GQGAAVILE 385
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
4-403 |
2.08e-144 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 416.87 E-value: 2.08e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRG--KQKNGSLHEVKPLSLVVGLIDELRKRHpDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPV 81
Cdd:PRK06025 3 EAYIIDAVRTPRGigKVGKGALAHLHPQHLAATVLKALAERN-GLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 82 TSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMS-RVPMGSDGGAMGLDP----ATNYDVMFV-PQS---IG 152
Cdd:PRK06025 82 KASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGKPPlgmgSGNLRLRALhPQShqgVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 153 ADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQNGLLILDHDEHMRPDTTKEGLAKLKPAFEGLAAL- 231
Cdd:PRK06025 162 GDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGSVALDHEEFPRPQTTAEGLAALKPAFTAIADYp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 232 ---GG--FDDVALQKYHWVEkINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPA 306
Cdd:PRK06025 242 lddKGttYRGLINQKYPDLE-IKHVHHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 307 TRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALI 386
Cdd:PRK06025 321 AKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGLV 400
|
410
....*....|....*..
gi 2085608637 387 TLCIGGGMGVATIIERV 403
Cdd:PRK06025 401 TMCAAGGMAPAIIIERV 417
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
3-403 |
1.10e-127 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 373.33 E-value: 1.10e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 3 EEAFIYEAIRTPRGKQkNGSLHEVKPLSLVVGLIDELRKRhPDLDENLISDVILGCVSPVGdQGGDIARAAVLASGMPVT 82
Cdd:PRK05790 2 KDVVIVSAARTPIGKF-GGALKDVSAVELGAIVIKAALER-AGVPPEQVDEVIMGQVLQAG-AGQNPARQAALKAGLPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 83 SGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVP---MGS-DGGAMG---LDPATNYDVM---FVPQSIG 152
Cdd:PRK05790 79 VPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvlPGSrWGQKMGdveLVDTMIHDGLtdaFNGYHMG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 153 --ADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVR--DQNG-LLILDHDEHMRPDTTKEGLAKLKPAFeg 227
Cdd:PRK05790 159 itAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTikQRKGdPVVVDTDEHPRPDTTAESLAKLRPAF-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 228 laalggfddvalqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPAT 307
Cdd:PRK05790 237 -------------------DKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 308 RKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALIT 387
Cdd:PRK05790 298 RKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLAT 377
|
410
....*....|....*.
gi 2085608637 388 LCIGGGMGVATIIERV 403
Cdd:PRK05790 378 LCIGGGQGVALIVERP 393
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
4-403 |
8.14e-125 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 366.20 E-value: 8.14e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKQkNGSLHEVKPLSLVVGLIDELRKRHPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPVTS 83
Cdd:PRK09050 3 EAFICDAIRTPIGRY-GGALSSVRADDLGAVPLKALMARNPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVP--MGSDGGA-----------MG---LDPA--TNYDVM 145
Cdd:PRK09050 82 PGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPfvMGKADSAfsrqaeifdttIGwrfVNPLmkAQYGVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 146 FVPQSigADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPV---RDQNGLLILDHDEHMRPDTTKEGLAKLK 222
Cdd:PRK09050 162 SMPET--AENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVtipQKKGDPVVVDRDEHPRPETTLEALAKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 223 PAFeglaalggfddvalqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTG 302
Cdd:PRK09050 240 PVF---------------------RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 303 PTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPD--EKLNVNGGAIAMGHPLGATGAMILGTMVDELERRN 380
Cdd:PRK09050 299 PAPATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLADddARVNPNGGAIALGHPLGMSGARLVLTALHQLERTG 378
|
410 420
....*....|....*....|...
gi 2085608637 381 ARRALITLCIGGGMGVATIIERV 403
Cdd:PRK09050 379 GRYALCTMCIGVGQGIALAIERV 401
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
4-403 |
9.38e-121 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 355.17 E-value: 9.38e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKqKNGSLHEVKPLSLVVGLIDELRKRHpDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPVTS 83
Cdd:PRK07801 3 EAYIVDAVRTPVGK-RKGGLAGVHPADLGAHVLKGLVDRT-GIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSD---GGAMGLDPATNYDVMF--------VPQSIG 152
Cdd:PRK07801 81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAmtaGEQLGFTSPFAESKGWlhrygdqeVSQFRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 153 ADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDqnglliLDHDEHMRpDTTKEGLAKLKPAFEGLAAlg 232
Cdd:PRK07801 161 AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG------VTVDEGPR-ETSLEKMAGLKPLVEGGRL-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 233 gfddvalqkyhwvekinhvhTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRKVLD 312
Cdd:PRK07801 232 --------------------TAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 313 RAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGG 392
Cdd:PRK07801 292 KTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGG 371
|
410
....*....|.
gi 2085608637 393 GMGVATIIERV 403
Cdd:PRK07801 372 GTANVTIIERL 382
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
3-403 |
4.13e-120 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 353.89 E-value: 4.13e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 3 EEAFIYEAIRTPRGKQKNGSLHEVKPLSLVVGLIDELRKRHPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPVT 82
Cdd:PRK08947 2 EDVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPHS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 83 SGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPM--GSDggamgLDPATNYDVMFVPQSIG--ADLIAT 158
Cdd:PRK08947 82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMnhGVD-----FHPGLSKNVAKAAGMMGltAEMLGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 159 IEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVR--DQNGLLIL-DHDEHMRPDTTKEGLAKLKPAFEglaalggfd 235
Cdd:PRK08947 157 MHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEghDADGVLKLfDYDEVIRPETTVEALAALRPAFD--------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 236 dvalqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRKVLDRAG 315
Cdd:PRK08947 228 -----------PVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 316 LTVDDIDLFELNEAFASVVLKFQKDLNI---PDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGG 392
Cdd:PRK08947 297 LSISDIDVFELNEAFAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGL 376
|
410
....*....|.
gi 2085608637 393 GMGVATIIERV 403
Cdd:PRK08947 377 GQGIATVFERV 387
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
4-403 |
7.82e-116 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 342.86 E-value: 7.82e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKqKNGSLHEVKPLSLVVGLIDELRKRhPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPVTS 83
Cdd:PRK07850 3 NPVIVEAVRTPIGK-RNGWLSGLHAAELLGAVQRAVLDR-AGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGGA-MGLDPATNYDVMFVPQSIGADLIATIEGF 162
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPgRGLPRPDSWDIDMPNQFEAAERIAKRRGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 163 SREDVDAYALRSQQKAAEAWSGGYFAKSVV----PVRDQNG-----LLILDHDEHMRpDTTKEGLAKLKPAFEGlaalgg 233
Cdd:PRK07850 161 TREDVDAFGLRSQRRAAQAWAEGRFDREISpvqaPVLDEEGqptgeTRLVTRDQGLR-DTTMEGLAGLKPVLEG------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 234 fddvalqkyhwvekinHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRKVLDR 313
Cdd:PRK07850 234 ----------------GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 314 AGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGGG 393
Cdd:PRK07850 298 AGMKIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGA 377
|
410
....*....|
gi 2085608637 394 MGVATIIERV 403
Cdd:PRK07850 378 LSTGTIIERI 387
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
4-403 |
2.03e-115 |
|
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.
Pssm-ID: 131483 Cd Length: 400 Bit Score: 342.53 E-value: 2.03e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKQkNGSLHEVKPLSLVVGLIDELRKRHPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPVTS 83
Cdd:TIGR02430 2 EAYICDAIRTPIGRY-GGSLSSVRADDLAAVPIKALLARNPQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVP--MGSDGGAMG--------------LDP--ATNYDVM 145
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPfvMGKADSAFSrsakiedttigwrfINPlmKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 146 FVPQSigADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPV---RDQNGLLILDHDEHMRPDTTKEGLAKLK 222
Cdd:TIGR02430 161 SMPET--AENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVvipQKKGEPTVVDQDEHPRPETTLEGLAKLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 223 PAFeglaalggfddvalqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTG 302
Cdd:TIGR02430 239 PVV---------------------RPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 303 PTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPD--EKLNVNGGAIAMGHPLGATGAMILGTMVDELERRN 380
Cdd:TIGR02430 298 PVPATQKLLARAGLSIDQFDVIELNEAFAAQALAVLRELGLADddARVNPNGGAIALGHPLGASGARLVLTALRQLERSG 377
|
410 420
....*....|....*....|...
gi 2085608637 381 ARRALITLCIGGGMGVATIIERV 403
Cdd:TIGR02430 378 GRYALCTMCIGVGQGIALAIERV 400
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-403 |
1.85e-110 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 329.66 E-value: 1.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 1 MSEEAFIYEAIRTPRGKQKNGSLHEVKPLSLVVGLIDELRKRHPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMP 80
Cdd:PRK09052 4 QLQDAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 81 VTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGsdGGAMGLDPAT-----NYDVMFvPQSIGADL 155
Cdd:PRK09052 84 NSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMM--GNKPSMSPAIfardeNVGIAY-GMGLTAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 156 IATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQNGLL------------ILDHDEHMRPDTTKEGLAKLKP 223
Cdd:PRK09052 161 VAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPdlatgevdvktrTVDLDEGPRADTSLEGLAKLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 224 AFeglAALGGFddvalqkyhwvekinhvhTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGP 303
Cdd:PRK09052 241 VF---ANKGSV------------------TAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 304 TPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARR 383
Cdd:PRK09052 300 IEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKY 379
|
410 420
....*....|....*....|
gi 2085608637 384 ALITLCIGGGMGVATIIERV 403
Cdd:PRK09052 380 GMVTMCVGTGMGAAGIFERL 399
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
4-403 |
1.49e-109 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 327.07 E-value: 1.49e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKqKNGSLHEVKPLSLVVGLIDELRKRhPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPVTS 83
Cdd:PRK06504 3 EAYIVAAARTAGGR-KGGRLAGWHPADLAAQVLDALVDR-SGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGS-------DGGAMGLDPATN--YDVMFVPQSIGAD 154
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSpstlpakNGLGHYKSPGMEerYPGIQFSQFTGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 155 LIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVP--VRDQNGLLILDH-DEHMRPDTTKEGLAKLKPAFEGlaal 231
Cdd:PRK06504 161 MMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPleITRADGSGEMHTvDEGIRFDATLEGIAGVKLIAEG---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 232 ggfddvalqkyhwvekinHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRKVL 311
Cdd:PRK06504 237 ------------------GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 312 DRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIG 391
Cdd:PRK06504 299 KKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEG 378
|
410
....*....|..
gi 2085608637 392 GGMGVATIIERV 403
Cdd:PRK06504 379 GGMANVTIVERL 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
4-403 |
6.76e-104 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 313.08 E-value: 6.76e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKQkNGSLHEVKPLSLVVGLIDELRKRhPDLDENLISDVILGCVSPVGDQGGdIARAAVLASGMPVTS 83
Cdd:PRK06205 3 DAVICEPVRTPVGRF-GGAFKDVPAEELAATVIRALVER-TGIDPARIDDVIFGQGYPNGEAPA-IGRVAALDAGLPVTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPM-------GSDGGAMGL-DPATNYDVMFVPQSIG--A 153
Cdd:PRK06205 80 PGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFyttdmrwGVRGGGVQLhDRLARGRETAGGRRFPvpG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 154 DLIATIE------GFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPV--RDQNG-LLILDHDEHMRPDTTKEGLAKLKPA 224
Cdd:PRK06205 160 GMIETAEnlrreyGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVtvPQRKGdPTVVDRDEHPRADTTLESLAKLRPI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 225 feglaaLGGFDDVAlqkyhwvekinhVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPT 304
Cdd:PRK06205 240 ------MGKQDPEA------------TVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 305 PATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPD---EKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNA 381
Cdd:PRK06205 302 PATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQA 381
|
410 420
....*....|....*....|..
gi 2085608637 382 RRALITLCIGGGMGVATIIERV 403
Cdd:PRK06205 382 RYGLETMCIGGGQGLAAVFERV 403
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
3-403 |
2.12e-103 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 311.27 E-value: 2.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 3 EEAFIYEAIRTP-----RGKQKNGSLHEVKPLSLVVGLIDELRKRhPDLDENLISDVILGCVSPVGDQ---GGdiaRAAV 74
Cdd:PRK06445 2 EDVYLVDFARTAfsrfrPKDPQKDVFNNIRPEELAAMLINRLIEK-TGIKPEEIDDIITGCALQVGENwlyGG---RHPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 75 LASGMPVTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSD---GGAMGL--DPA-TNYDvMFVP 148
Cdd:PRK06445 78 FLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphiEPNPKLltDPKyIEYD-LTTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 149 QSIG--ADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQNG--LLILDHDEHMRPDTTKEGLAKLKPA 224
Cdd:PRK06445 157 YVMGltAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEgkKKVVDVDQSVRPDTSLEKLAKLPPA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 225 FeglaalggfddvalqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPT 304
Cdd:PRK06445 237 F---------------------KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 305 PATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRA 384
Cdd:PRK06445 296 PASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYG 375
|
410
....*....|....*....
gi 2085608637 385 LITLCIGGGMGVATIIERV 403
Cdd:PRK06445 376 VATLCVGGGQGGAVVLERV 394
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
4-403 |
3.61e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 308.22 E-value: 3.61e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKQKNGSLHEVKPLSLVVGLIDELRKRHPDLDENlISDVILGCVSPVGDQGGDIARAAVLASGMPVTS 83
Cdd:PRK07661 3 EAVIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYEGP-IDDLIIGCAMPEAEQGLNMARNIGALAGLPYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGsdGGAMGLDPATnydVMFVPQ---SIG--ADLIAT 158
Cdd:PRK07661 82 PAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--GHVVRPNPRL---VEAAPEyymGMGhtAEQVAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 159 IEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVR------DQNGLL-----ILDHDEHMRPDTTKEGLAKLKPAFeg 227
Cdd:PRK07661 157 KYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDvtlrtvGENNKLqeetiTFSQDEGVRADTTLEILGKLRPAF-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 228 laalggfddvalqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPAT 307
Cdd:PRK07661 235 -------------------NVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 308 RKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALIT 387
Cdd:PRK07661 296 PKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVT 375
|
410
....*....|....*.
gi 2085608637 388 LCIGGGMGVATIIERV 403
Cdd:PRK07661 376 MCIGGGMGAAGVFELL 391
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
4-403 |
4.07e-102 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 308.24 E-value: 4.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKQkNGSLHEVKPLSLVVGLIDELRKRHPdLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPVTS 83
Cdd:PRK08131 3 DAYIYDGLRSPFGRH-AGALASVRPDDLAATVIRRLLEKSG-FPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVP--MGSDGGAMGLDpATNYDVMF--------------- 146
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPfvMGKAESAFSRD-AKVFDTTIgarfpnpkivaqygn 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 147 --VPQSigADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQNG----LLILDHDEHMRPDTTKEGLAK 220
Cdd:PRK08131 160 dsMPET--GDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGrklpPKLVAEDEHPRPSSTVEALTK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 221 LKPAFEGlaalggfddvalqkyhwvekinHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIML 300
Cdd:PRK08131 238 LKPLFEG----------------------GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 301 TGPTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIP--DEKLNVNGGAIAMGHPLGATGAMILGTMVDELER 378
Cdd:PRK08131 296 IGPVEAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVDfdDPRVNPNGGAIAVGHPLGASGARLALTAARELQR 375
|
410 420
....*....|....*....|....*
gi 2085608637 379 RNARRALITLCIGGGMGVATIIERV 403
Cdd:PRK08131 376 RGKRYAVVSLCIGVGQGLAMVIERV 400
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
7-403 |
1.12e-100 |
|
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: 304.17 E-value: 1.12e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 7 IYEAIRTPRGKQKNGSLHEVKPLSLVVGLIDELRKRHPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPVTSGGV 86
Cdd:TIGR02445 4 IVDFGRTPMGRSKGGAFRNTRAEDLSAHLMSKLLARNPKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTSAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 87 QLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMgsdggAMGLDPATNYDvMFVPQSIG-----ADLIATIEG 161
Cdd:TIGR02445 84 TVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPM-----MHGVDFHPGMS-LHVAKAAGmmgltAEMLGKMHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 162 FSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVR--DQNGLL-ILDHDEHMRPDTTKEGLAKLKPAFEglaalggfddva 238
Cdd:TIGR02445 158 ISREQQDAFAARSHARAHAATQEGKFKNEIIPTQghDADGFLkQFDYDEVIRPETTVESLAALRPAFD------------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 239 lqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRKVLDRAGLTV 318
Cdd:TIGR02445 226 --------PKNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 319 DDIDLFELNEAFASVVLKFQKDLNI---PDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGGGMG 395
Cdd:TIGR02445 298 SDIDVFELNEAFAAQALPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQG 377
|
....*...
gi 2085608637 396 VATIIERV 403
Cdd:TIGR02445 378 IATVFERV 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-403 |
1.17e-100 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 304.57 E-value: 1.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 1 MSEEAFIYEAIRTPRGKqKNGSLHEVKPLSLVVGLIDELRKRhPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMP 80
Cdd:PRK09051 1 MMREVVVVSGVRTAIGT-FGGSLKDVAPTDLGATVVREALAR-AGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 81 VTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSD----GGAMGldPATNYDVMF---------V 147
Cdd:PRK09051 79 QETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPaarwGARMG--DAKLVDMMVgalhdpfgtI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 148 PQSIGADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPV--RDQNGLLILDHDEHMRPDTTKEGLAKLKPAF 225
Cdd:PRK09051 157 HMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVeiKTRKGEVVFDTDEHVRADTTLEDLAKLKPVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 226 EglaalggfddvalqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTP 305
Cdd:PRK09051 237 K--------------------KENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 306 ATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRAL 385
Cdd:PRK09051 297 ATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYAL 376
|
410
....*....|....*...
gi 2085608637 386 ITLCIGGGMGVATIIERV 403
Cdd:PRK09051 377 VTMCIGGGQGIAAIFERL 394
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
4-402 |
4.93e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 298.07 E-value: 4.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKQKNGSLHEVKPLSLVVGLIDELRKRHPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPvTS 83
Cdd:PRK07851 3 EAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD-FL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMG-SD-----------------------GGAMGLDPA 139
Cdd:PRK07851 82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGnSDslpdtknplfaeaqartaaraegGAEAWHDPR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 140 TNYDVMFVPQSIG--ADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQNGLLIlDHDEHMRPDTTKEG 217
Cdd:PRK07851 162 EDGLLPDVYIAMGqtAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDGTVV-STDDGPRAGTTYEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 218 LAKLKPAFeglaalggfddvalqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPV 297
Cdd:PRK07851 241 VSQLKPVF---------------------RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 298 IMLTGPTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELE 377
Cdd:PRK07851 300 IMGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQ 379
|
410 420
....*....|....*....|....*
gi 2085608637 378 RRNARRALITLCIGGGMGVATIIER 402
Cdd:PRK07851 380 THDKTFGLETMCVGGGQGMAMVLER 404
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-403 |
5.50e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 270.35 E-value: 5.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 1 MSEEAFIYEAIRTPRGKQKNGslheVKPLS---LVVGLIDELRKRHP----DLDEnlisdVILGCVSPVGDQGgDIARAA 73
Cdd:PRK08170 1 MARPVYIVDGARTPFLKARGG----PGPFSasdLAVAAGRALLNRQPfapdDLDE-----VILGCAMPSPDEA-NIARVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 74 VLASGMPVTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVP-------------------MGSDGGAM 134
Cdd:PRK08170 71 ALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPllfsekmvrwlagwyaaksIGQKLAAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 135 G-LDPATNYDVM---------FVPQSIG--ADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFaKSVVPVRDQNGLlI 202
Cdd:PRK08170 151 GkLRPSYLAPVIgllrgltdpVVGLNMGqtAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPLFDRDGK-F 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 203 LDHDEHMRPDTTKEGLAKLKPAFEglaalggfddvalQKYHWVekinhvhTGGNSSGIVDGAALVMIGSAAAGKLQGLTP 282
Cdd:PRK08170 229 YDHDDGVRPDSSMEKLAKLKPFFD-------------RPYGRV-------TAGNSSQITDGACWLLLASEEAVKKYGLPP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 283 RARIVATATSGADPVIMLTGPTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPD----------------- 345
Cdd:PRK08170 289 LGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWADEEycreqlgldgalgeldr 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2085608637 346 EKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGGGMGVATIIERV 403
Cdd:PRK08170 369 ERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
4-401 |
7.28e-86 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 266.25 E-value: 7.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKQKNGSLHEVKPLSLVVGLIDELRKRhPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPVTS 83
Cdd:PRK07108 3 EAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVER-AKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVP------MGSDGGAMGLDPATNYDVMfvpQSigADLIA 157
Cdd:PRK07108 82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQnemnrhMLREGWLVEHKPEIYWSML---QT--AENVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 158 TIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQNGL------------LILDHDEHMRPDTTKEGLAKLKPAF 225
Cdd:PRK07108 157 KRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVadkatgrlftkeVTVSADEGIRPDTTLEGVSKIRSAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 226 EGlaalggfddvalqkyhwvekinHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTP 305
Cdd:PRK07108 237 PG----------------------GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 306 ATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRAL 385
Cdd:PRK07108 295 AVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVV 374
|
410
....*....|....*.
gi 2085608637 386 ITLCIGGGMGVATIIE 401
Cdd:PRK07108 375 VTMCIGGGQGAAGLFE 390
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-403 |
4.01e-85 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 264.58 E-value: 4.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 1 MSEEAFIYEAIRTPRGKQKnGSLHEVKPLSLVVGLIDELRKrHPDLDENLISDVILGCVSpVGDQGGDIARAAVLASGMP 80
Cdd:PRK06633 1 MTKPVYITHAKRTAFGSFM-GSLSTTPAPMLAAHLIKDILQ-NSKIDPALVNEVILGQVI-TGGSGQNPARQTLIHAGIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 81 VTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMS------RVPMGSDGGAMGLDPATNYDVMF-----VPQ 149
Cdd:PRK06633 78 KEVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmhgsYIRAGAKFGDIKMVDLMQYDGLTdvfsgVFM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 150 SIGADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVR--DQNGLLILDHDEHMRPDTTKEGLAKLKPAFEG 227
Cdd:PRK06633 158 GITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEvtIKKTTSLFDHDETVRPDTSLEILSKLRPAFDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 228 laalggfddvalqkyhwvekiNHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPAT 307
Cdd:PRK06633 238 ---------------------NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 308 RKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALIT 387
Cdd:PRK06633 297 QKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVT 376
|
410
....*....|....*.
gi 2085608637 388 LCIGGGMGVATIIERV 403
Cdd:PRK06633 377 LCIGGGMGMAMCVEAV 392
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
4-401 |
2.63e-81 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 254.64 E-value: 2.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKQkNGSLHEVKPLSLVVGLIDELRKRhPDLDENLISDVILGCVSPVGdQGGDIARAAVLASGMPVTS 83
Cdd:PRK08235 3 KTVIVSAARTPFGKF-GGSLKDVKATELGGIAIKEALER-ANVSAEDVEEVIMGTVLQGG-QGQIPSRQAARAAGIPWEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGGAMGL--DPATNYDVMF----------VPQSI 151
Cdd:PRK08235 80 QTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYrmGDNEVIDLMVadgltcafsgVHMGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 152 GADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQN---GLLILDHDEHMRPDTTKEGLAKLKPAFEGL 228
Cdd:PRK08235 160 YGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQrkgDPIVVAKDEAPRKDTTIEKLAKLKPVFDKT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 229 AALggfddvalqkyhwvekinhvhTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATR 308
Cdd:PRK08235 240 GTI---------------------TAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAIN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 309 KVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITL 388
Cdd:PRK08235 299 ALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAI 378
|
410
....*....|...
gi 2085608637 389 CIGGGMGVATIIE 401
Cdd:PRK08235 379 CSGGGQGDAVLIE 391
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
2-402 |
3.16e-81 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 256.23 E-value: 3.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 2 SEEAFIYEAIRTPRGKQKNGSLHEVKPLSLVVGLIDELRKRHPdLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPV 81
Cdd:PLN02287 45 GDDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVEKTG-LNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 82 TSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGGamgLDPATNYDVM----FVPQSIGADLIA 157
Cdd:PLN02287 124 TVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGG---VNPRVESFSQaqdcLLPMGITSENVA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 158 TIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQ--------NGLLILDHDEHMRPDTTKEGLAKLKPAFegla 229
Cdd:PLN02287 201 ERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKivdpktgeEKPIVISVDDGIRPNTTLADLAKLKPVF---- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 230 alggfddvalqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRK 309
Cdd:PLN02287 277 -----------------KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 310 VLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRN--ARRALIT 387
Cdd:PLN02287 340 AVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVS 419
|
410
....*....|....*
gi 2085608637 388 LCIGGGMGVATIIER 402
Cdd:PLN02287 420 MCIGTGMGAAAVFER 434
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
3-402 |
7.45e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 250.96 E-value: 7.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 3 EEAFIYEAIRTPRGKQKnGSLHEVKPLSLVVGLIDELRKRhPDLDENLISDVILGCVSPVGdQGGDIARAAVLASGMPVT 82
Cdd:PRK05656 2 QDVVIVAATRTAIGSFQ-GSLANIPAVELGAAVIRRLLEQ-TGLDPAQVDEVILGQVLTAG-AGQNPARQAAIKAGLPHS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 83 SGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGGAMGL--DPATNYDVMFVP----------QS 150
Cdd:PRK05656 79 VPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLrmGHAQLVDSMITDglwdafndyhMG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 151 IGADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPV---RDQNGLLILDHDEHMRPDTTKEGLAKLKPAFeg 227
Cdd:PRK05656 159 ITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIlipQRKGEPLAFATDEQPRAGTTAESLAKLKPAF-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 228 laalggfddvalqkyhwveKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPAT 307
Cdd:PRK05656 237 -------------------KKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSAT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 308 RKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALIT 387
Cdd:PRK05656 298 RRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLAT 377
|
410
....*....|....*
gi 2085608637 388 LCIGGGMGVATIIER 402
Cdd:PRK05656 378 LCIGGGQGVALAIER 392
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
4-403 |
1.26e-75 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 238.90 E-value: 1.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKqKNGSLHEVKPLSLVVGLIDELRKRHPDLdenlISDVILGCVspVGdQGGDIARAAVLASGMPVTS 83
Cdd:PRK06690 2 RAVIVEAKRTPIGK-KNGMLKDYEVQQLAAPLLTFLSKGMERE----IDDVILGNV--VG-PGGNVARLSALEAGLGLHI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 84 GGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGgamgldpatnydvMFVPQSIG-------ADLI 156
Cdd:PRK06690 74 PGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRA-------------RFSPETIGdpdmgvaAEYV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 157 ATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVrdqNGLLildhDEHMRPDTTKEGL-AKLKPAFEGlaalggfd 235
Cdd:PRK06690 141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF---NGLL----DESIKKEMNYERIiKRTKPAFLH-------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 236 dvalqkyhwvekiNHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRKVLDRAG 315
Cdd:PRK06690 206 -------------NGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 316 LTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGGGMG 395
Cdd:PRK06690 273 MKVEDIDYFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIG 352
|
....*...
gi 2085608637 396 VATIIERV 403
Cdd:PRK06690 353 LALLFEKV 360
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
3-403 |
2.57e-69 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 223.82 E-value: 2.57e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 3 EEAFIYEAIRTPRGKQkNGSLHEVKPLSLVVGLIDELRKRHPdLDENLISDVILGCVSPVGdQGGDIARAAVLASGMPVT 82
Cdd:PLN02644 1 RDVCIVGVARTPIGGF-LGSLSSLSATELGSIAIQAALERAG-VDPALVQEVFFGNVLSAN-LGQAPARQAALGAGLPPS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 83 SGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVP-----------MGSDG---GAM--GL-DPATNYdvm 145
Cdd:PLN02644 78 TICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPkylpearkgsrLGHDTvvdGMLkdGLwDVYNDF--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 146 fvPQSIGADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQNG----LLILDHDEHM-RPDTTKegLAK 220
Cdd:PLN02644 155 --GMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGrgrpSVIVDKDEGLgKFDPAK--LRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 221 LKPAFEglaalggfddvalqkyhwvEKINHVhTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIML 300
Cdd:PLN02644 231 LRPSFK-------------------EDGGSV-TAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 301 TGPTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRN 380
Cdd:PLN02644 291 TAPALAIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKN 370
|
410 420
....*....|....*....|...
gi 2085608637 381 ARRALITLCIGGGMGVATIIERV 403
Cdd:PLN02644 371 GKYGVAGICNGGGGASAIVVELM 393
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
7-402 |
2.19e-66 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 217.16 E-value: 2.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 7 IYEAIRTPRGKQKNgSLHEVKPLSLVVGLIDELRKRHpDLDENLISDVILGCVSPVgDQGGDIARAAVLASGMPVTSGGV 86
Cdd:PRK08963 9 IVSGLRTPFAKQAT-AFHGIPAVDLGKMVVGELLARS-EIDPELIEQLVFGQVVQM-PEAPNIAREIVLGTGMNVHTDAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 87 QLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMG-SDGGAMGLDPATN----------------YDVMFVPQ 149
Cdd:PRK08963 86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGvSKKLARALVDLNKartlgqrlklfsrlrlRDLLPVPP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 150 SIG-----------ADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSV----VPVRDQngllILDHDEHMRPDTT 214
Cdd:PRK08963 166 AVAeystglrmgdtAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVmtahVPPYKQ----PLEEDNNIRGDST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 215 KEGLAKLKPAFEglaalggfddvalQKYHWVekinhvhTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGA 294
Cdd:PRK08963 242 LEDYAKLRPAFD-------------RKHGTV-------TAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 295 DPVI-MLTGPTPATRKVLDRAGLTVDDIDLFELNEAFASVVL---------KF-QKDLN-------IPDEKLNVNGGAIA 356
Cdd:PRK08963 302 DVWQdMLLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLanlqmfaseRFaREKLGrsqaigeVDMSKFNVLGGSIA 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2085608637 357 MGHPLGATGAMILGTMVDELERRNARRALITLCIGGGMGVATIIER 402
Cdd:PRK08963 382 YGHPFAATGARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
4-403 |
3.31e-65 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 212.95 E-value: 3.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 4 EAFIYEAIRTPRGKQKNgSLHEVKPLSL----VVGLIDELRkrhpdLDENLISDVILGCVSPVGDqGGDIARAAVLASGM 79
Cdd:PRK06366 3 DVYIVSAKRTAIGKFGR-SFSKIKAPQLggaaIKAVIDDAK-----LDPALVQEVIMGNVIQAGV-GQNPAGQAAYHAGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 80 PVTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVP--MGSD---------------GGAM---GLDPA 139
Cdd:PRK06366 76 PFGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPflLPSDlrwgpkhllhknykiDDAMlvdGLIDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 140 TNYDVMfvpqSIGADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDqnglliLDHDEHMRpDTTKEGLA 219
Cdd:PRK06366 156 FYFEHM----GVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND------LDRDEGIR-KTTMEDLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 220 KLKPAFEGlaalggfddvalqkyhwvekiNHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIM 299
Cdd:PRK06366 225 KLPPAFDK---------------------NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 300 LTGPTPATRKVLDRAGLTVDDIDLFELNEAF--ASVVLKFQkdLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELE 377
Cdd:PRK06366 284 VEAPIPATRKLLEKQNKSIDYYDLVEHNEAFsiASIIVRDQ--LKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALK 361
|
410 420
....*....|....*....|....*.
gi 2085608637 378 RRNARRALITLCIGGGMGVATIIERV 403
Cdd:PRK06366 362 TRHMKTGLATLCHGGGGAHTLTLEMV 387
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
51-401 |
1.36e-62 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 206.28 E-value: 1.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 51 ISDVILGCVSPVGdQGGDIARAAVLASGMPVTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVP--MG 128
Cdd:PRK06954 53 IDEVVMGCVLPAG-QGQAPARQAALGAGLPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPylLP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 129 SDGGAMGLDPATNYDVMFVP---------QSIG--ADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVR-- 195
Cdd:PRK06954 132 KARGGMRMGHGQVLDHMFLDgledaydkgRLMGtfAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTva 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 196 DQNGLLILDHDEHMRPDTTkEGLAKLKPAFEGLAALggfddvalqkyhwvekinhvhTGGNSSGIVDGA-ALVMIGSAAA 274
Cdd:PRK06954 212 GKKGDTVIDRDEQPFKANP-EKIPTLKPAFSKTGTV---------------------TAANSSSISDGAaALVMMRASTA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 275 GKLqGLTPRARIVATATSGADPVIMLTGPTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGA 354
Cdd:PRK06954 270 KRL-GLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGA 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2085608637 355 IAMGHPLGATGAMILGTMVDELERRNARRALITLCIGGGMGVATIIE 401
Cdd:PRK06954 349 CALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
70-402 |
2.65e-57 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 193.19 E-value: 2.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 70 ARAAVLASGMPVTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMG-SDG----------------- 131
Cdd:PRK09268 71 TRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAvNEGlrkillelnrakttgdr 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 132 --GAMGLDPAtnydvMFVPQ-----------SIG--ADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRD 196
Cdd:PRK09268 151 lkALGKLRPK-----HLAPEiprngeprtglSMGehAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 197 qnglliLDHDEHMRPDTTKEGLAKLKPAFeglaalGGFDDVALqkyhwvekinhvhTGGNSSGIVDGAALVMIGSAAAGK 276
Cdd:PRK09268 226 ------LTRDNNLRPDSSLEKLAKLKPVF------GKGGRATM-------------TAGNSTPLTDGASVVLLASEEWAA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 277 LQGLTPRARIVATATSGADPVI----MLTGPTPATRKVLDRAGLTVDDIDLFELNEAFASVVL---------KFQKDL-- 341
Cdd:PRK09268 281 EHGLPVLAYLVDAETAAVDFVHgkegLLMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLatlkawedeEYCRERlg 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2085608637 342 ------NIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGGGMGVATIIER 402
Cdd:PRK09268 361 ldaplgSIDRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
280-402 |
7.14e-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: 182.46 E-value: 7.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 280 LTPRARIVATATSGADPVIMLTGPTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGH 359
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2085608637 360 PLGATGAMILGTMVDELERRNARRALITLCIGGGMGVATIIER 402
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
6-273 |
8.01e-53 |
|
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: 176.72 E-value: 8.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 6 FIYEAIRTPRGKqKNGSLHEVKPLSLVVGLIDELRKRHPdLDENLISDVILGCVSPVGdQGGDIARAAVLASGMPVTSGG 85
Cdd:pfam00108 2 VIVSAARTPFGS-FGGSLKDVSAVELGAEAIKAALERAG-VDPEDVDEVIVGNVLQAG-EGQNPARQAALKAGIPDSAPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 86 VQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGGAMG---LDPATNYDVM--------FVPQSIG-- 152
Cdd:pfam00108 79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSglkHGDEKKHDLLipdgltdaFNGYHMGlt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 153 ADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVR--DQNGLLILDHDEHMRPDTTKEGLAKLKPAFeglaa 230
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTvkGRKGKPTVDKDEGIRPPTTAEPLAKLKPAF----- 233
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2085608637 231 lggfddvalQKYHWVekinhvhTGGNSSGIVDGAALVMIGSAA 273
Cdd:pfam00108 234 ---------DKEGTV-------TAGNASPINDGAAAVLLMSES 260
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
51-401 |
2.29e-48 |
|
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: 169.21 E-value: 2.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 51 ISDVILGCVSPVGdQGGDIARAAVLASGMPVTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSrvpmgsd 130
Cdd:cd00826 45 VEEACLGQVLGAG-EGQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 131 ggamgldpatnYDVMFVPQSIGADLIATIEGfSREDVDAYALRSQQKAAEAWSGGYFAKSVVP--VRDQNGLLILDHDEH 208
Cdd:cd00826 117 -----------TSAENNAKEKHIDVLINKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKfgVKGRKGDIHSDADEY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 209 MR--PDTTKEGLAKLKPAFEGLAALggfddvalqkyhwvekinhvhTGGNSSGIVDGAALVMIGSAA-------AGKLQG 279
Cdd:cd00826 185 IQfgDEASLDEIAKLRPAFDKEDFL---------------------TAGNACGLNDGAAAAILMSEAeaqkhglQSKARE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 280 LTPRARIVATATSGADP----VIMLTGPTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEK-------- 347
Cdd:cd00826 244 IQALEMITDMASTFEDKkvikMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdr 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2085608637 348 ----------LNVNGGAIAMGHPLGATGAMILGTMVDELERRN-----ARRALITLCIGGGMGVATIIE 401
Cdd:cd00826 324 gdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAgkrqgAGAGLALLCIGGGGGAAMCIE 392
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
254-400 |
4.87e-20 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 88.66 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 254 GGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATAT----SGADPVIMLTGPTPATRKVLDRAGLTVDDIDLFELNEA 329
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAAtfdgASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 330 FASVVLKFQKDLNIPDEK---LNVNGGAIAMGHPLGATGAMILGTMVDELERRN-------ARRALITLCIGGGMGVATI 399
Cdd:cd00327 174 GTPIGDAVELALGLDPDGvrsPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFipptprePRTVLLLGFGLGGTNAAVV 253
|
.
gi 2085608637 400 I 400
Cdd:cd00327 254 L 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
52-400 |
2.59e-14 |
|
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: 73.84 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 52 SDVILGCVSPVGDQGGDIARAAVLASGMPVT-SGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSD 130
Cdd:cd00829 36 ADIDAVVVGNAAGGRFQSFPGALIAEYLGLLgKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 131 GGAMGLDPATNYDVMFVPQSIGAdliatiegfsredvdAYALRSQQKAAE-AWSGGYFAKSVVPVRdQNGLLildHDE-H 208
Cdd:cd00829 116 AGGRASDLEWEGPEPPGGLTPPA---------------LYALAARRYMHRyGTTREDLAKVAVKNH-RNAAR---NPYaQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 209 MRPDTTKEGLAKLKPafeglaalggfddVA--LQKYHwvekinhvhtggnSSGIVDGAALVMIGSAAAGKLQGLTP---R 283
Cdd:cd00829 177 FRKPITVEDVLNSRM-------------IAdpLRLLD-------------CCPVSDGAAAVVLASEERARELTDRPvwiL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 284 ARIVATATSGADPVIMLTGPTP---ATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDL----------------NIP 344
Cdd:cd00829 231 GVGAASDTPSLSERDDFLSLDAarlAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLgfcekgeggklvregdTAI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085608637 345 DEKL--NVNGGAIAMGHPLGATGAMILGTMV-------DELERRNARRALiTLCIGGGMGVATII 400
Cdd:cd00829 311 GGDLpvNTSGGLLSKGHPLGATGLAQAVEAVrqlrgeaGARQVPGARVGL-AHNIGGTGSAAVVT 374
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
258-403 |
6.95e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 54.18 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 258 SGIVDGAA-LVMIGSAAAGKLQgltPRARIVATA-------TSGADPVIMlTGPTPATRKVLDRAGLTVDDIDLFELNEA 329
Cdd:PRK07516 213 SLVSDGAAaLVLADAETARALQ---RAVRFRARAhvndflpLSRRDPLAF-EGPRRAWQRALAQAGVTLDDLSFVETHDC 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 330 F-------------------ASVVLK--FQKDLNIPdekLNVNGGAIAMGHPLGATG-------AMILGTMVDELERRNA 381
Cdd:PRK07516 289 FtiaelieyeamglappgqgARAIREgwTAKDGKLP---VNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPGA 365
|
170 180
....*....|....*....|....*
gi 2085608637 382 RRALITLCigGGMGVA---TIIERV 403
Cdd:PRK07516 366 KLAGVFNM--GGAAVAnyvSILERV 388
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
92-365 |
1.52e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 49.90 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 92 CASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGGAMGldPATNYD----VMFVPQSIGAdLIATIE----GFS 163
Cdd:PRK06064 85 CASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIA--RAGDYEweefFGATFPGLYA-LIARRYmhkyGTT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 164 REDVDAYALRSQQKAAeawsggyfaksvvpvrdqnglliLDHDEHMRPDTTKEGLAKLKPafeglaalggfddVA--LQK 241
Cdd:PRK06064 162 EEDLALVAVKNHYNGS-----------------------KNPYAQFQKEITVEQVLNSPP-------------VAdpLKL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 242 YHwvekinhvhtggnSSGIVDGAALVMIGSAAAGKLQGLTP---RARIVATAT---SGADPVIMLTGPTPATRKVLDRAG 315
Cdd:PRK06064 206 LD-------------CSPITDGAAAVILASEEKAKEYTDTPvwiKASGQASDTialHDRKDFTTLDAAVVAAEKAYKMAG 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2085608637 316 LTVDDIDLFELNEAF--ASVV----LKFQK---------------DLNIPdekLNVNGGAIAMGHPLGATG 365
Cdd:PRK06064 273 IEPKDIDVAEVHDCFtiAEILayedLGFAKkgeggklaregqtyiGGDIP---VNPSGGLKAKGHPVGATG 340
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
306-401 |
2.61e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 46.06 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 306 ATRKVLDRAGLT--VDDIDLFELNEAFASVVLKFQKDLNI----------------PDEKLNVN--GGAIAMGHPLGATG 365
Cdd:PRK06365 298 AAKEAYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgkpeLPGKLPVNpsGGLLAAGHAVGATG 377
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2085608637 366 AM--------ILGTM-----VDELERRNARRALITLCIGGGMGV-ATIIE 401
Cdd:PRK06365 378 IMqavfmfwqLQGRIkkhfhDDYLQVKNAKRGLIHSHAGTGTYVtVTILE 427
|
|
| PRK08257 |
PRK08257 |
acetyl-CoA acetyltransferase; Validated |
261-387 |
4.92e-05 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 236204 [Multi-domain] Cd Length: 498 Bit Score: 45.29 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 261 VD-GAALVMIGSAAAGKLQglTPRARIV--ATATSGADPVIMLTGPTP--------ATRKVLDRAGLTVDDIDLFELNEA 329
Cdd:PRK08257 243 VDqGAAVLLTSVAKARRLG--VPEDRWVylHGGADAHDPYDILERPDLhrspairaAGRRALALAGLGIDDIDAFDLYSC 320
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2085608637 330 FASVVLKFQKDLNIPDEK---LNVNGGAIAMGHPLG--ATGAMIlgTMVDELERRNARRALIT 387
Cdd:PRK08257 321 FPSAVQVAARELGLDLDDprpLTVTGGLPFFGGPGNnyVTHAIA--EMVERLRANPGRRGLVT 381
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
258-392 |
6.81e-05 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 44.68 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 258 SGIVDGAALVMIGSAA-AGKLQGLTPRARIVA----TAT---------SGADPVIMltgptPATRK-VLD---RAGLTVD 319
Cdd:PRK06289 220 SQVTDGGAGVVLASDAyLRDYADARPIPRIKGwghrTAPlgleqkldrSAGDPYVL-----PHVRQaVLDayrRAGVGLD 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 320 DIDLFELNEAFASVVL---------------KFQKDLNI-PDEKLNVN--GGAIAMGHPLGATGA-MIL-------GTMV 373
Cdd:PRK06289 295 DLDGFEVHDCFTPSEYlaidhigltgpgeswKAIENGEIaIGGRLPINpsGGLIGGGHPVGASGVrMLLdaakqvtGTAG 374
|
170
....*....|....*....
gi 2085608637 374 DeLERRNARRALiTLCIGG 392
Cdd:PRK06289 375 D-YQVEGAKTFG-TLNIGG 391
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
78-399 |
6.12e-04 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 41.55 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 78 GMPVTsggvQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMsrvpmgSDGGAMGLDPAtnydvmfvpqSIGADLIA 157
Cdd:PRK06157 78 NIPVT----RVENFCATGSEAFRGAVYAVASGAYDIALALGVEKL------KDTGYGGLPVA----------NPGTLADM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 158 TiegfsREDVDAYALRSQqkaaeaWSGGYFAKSVVPVRD-------------QNGLliLDHDEHMRPDTTKEGLAKlKPA 224
Cdd:PRK06157 138 T-----MPNVTAPGNFAQ------LASAYAAKYGVSREDlkramahvsvkshANGA--RNPKAHLRKAVTEEQVLK-APM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 225 FEGlaALGGFDdvalqkyhwvekinhvhtggnSSGIVDGAALVMIGSAAAGKLQGLTPRARIVAT--ATSGADPVI---- 298
Cdd:PRK06157 204 IAG--PLGLFD---------------------CCGVSDGAAAAIVTTPEIARALGKKDPVYVKALqlAVSNGWELQyngw 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 299 -MLTGPTP--ATRKVLDRAGLT--VDDIDLFELNEAFASVVLKFQKDLNIP----------------DEKL--NVNGGAI 355
Cdd:PRK06157 261 dGSYFPTTriAARKAYREAGITdpREELSMAEVHDCFSITELVTMEDLGLSergqawrdvldgffdaDGGLpcQIDGGLK 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2085608637 356 AMGHPLGATGAMILGTM-------VDELERRNARRALiTLCIGG--GMGVATI 399
Cdd:PRK06157 341 CFGHPIGASGLRMLYEMylqllgrAGERQLKNPRLAL-THNLGGapGQNVCSV 392
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
16-365 |
6.93e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 41.42 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 16 GKQKNGSLHEVkplsLVVGLIDELRKRHPDLDENLISDVILG-----CVSpvgdQGGDIARAAVLASGMPVTSGG----- 85
Cdd:PTZ00455 41 GKKENKTLEEL----LATAIQGTLENTGLDGKAALVDKVVVGnflgeLFS----SQGHLGPAAVGSLGQSGASNAllykp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 86 -VQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVpmGSDGGAMGLDPATNY------DVMFVPQSIGADLIAT 158
Cdd:PTZ00455 113 aMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTV--SARVGGDYLARAADYrrqrklDDFTFPCLFAKRMKYI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 159 IEG--FSREDVdayalrsQQKAAEAWSGGyfaksvvpvrDQNGLlildhdEHMRPDttkeglaklKPAFEGLAAlggfDD 236
Cdd:PTZ00455 191 QEHghFTMEDT-------ARVAAKAYANG----------NKNPL------AHMHTR---------KLSLEFCTG----AS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 237 VALQKYHWVEKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPR-ARIVATATSGA----------DPVIMLTGpTP 305
Cdd:PTZ00455 235 DKNPKFLGNETYKPFLRMTDCSQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEIKSLACasgnlyedppDATRMFTS-RA 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2085608637 306 ATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDE------------------KLNVNGGAIAMGHPLGATG 365
Cdd:PTZ00455 314 AAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYghakdlirngatalegriPVNTGGGLLSFGHPVGATG 391
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
77-403 |
8.41e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 41.42 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 77 SGMPVtsggVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRvpmGSDGGAMG--------LDPATNYDVMFVP 148
Cdd:PRK08256 69 TGIPI----VNVNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQP---GALGSVWDdrpsplerFDKALAELQGFDP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 149 QSIGADLIAtieGFSREDVDAYALRSQQkaaeawsggyFAKSVVPVRD--QNGLLILDHDEHmrpdTTKEGLAKlKPAFE 226
Cdd:PRK08256 142 APPALRMFG---GAGREHMEKYGTTAET----------FAKIGVKARRhaANNPYAQFRDEY----TLEDVLAS-PMIWG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 227 GLAALggfddvalqkyhwvekinhvhtggNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATA-------TSGADPVIM 299
Cdd:PRK08256 204 PLTRL------------------------QCCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQAmttdtpsTFDGRSMID 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 300 LTG---PTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNI-PD---EKL--------------NVNGGAIAMG 358
Cdd:PRK08256 260 LVGydmTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLcPEgeaEKFiddgdntyggrwvvNPSGGLLSKG 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2085608637 359 HPLGATGAMILGTMVDEL----ERR---NARRAL---ITLcigGGMGVATIIERV 403
Cdd:PRK08256 340 HPLGATGLAQCAELTWQLrgtaGARqveGARLALqhnLGL---GGACVVTLYQRA 391
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
92-136 |
1.84e-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: 39.54 E-value: 1.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2085608637 92 CASGLEAVNTAAQKVRSGWDDLVLAGGVESMSrVPMGSDG-GAMGL 136
Cdd:pfam00109 173 CSSSLVAIHAAVQSIRSGEADVALAGGVNLLL-TPLGFAGfSAAGM 217
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
92-123 |
3.96e-03 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 39.06 E-value: 3.96e-03
10 20 30
....*....|....*....|....*....|..
gi 2085608637 92 CASGLEAVNTAAQKVRSGWDDLVLAGGVESMS 123
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALI 192
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
262-377 |
4.27e-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: 38.77 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 262 DGAALVMIGSAAAGKLQGLTPRARIVATA-----TSGADPVIMLTGPTPATRKVLDRAGLTVDDIDLFE---LNEAFASV 333
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAatidgAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVahgTGTPIGDV 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2085608637 334 VLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELE 377
Cdd:cd00825 241 KELKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
262-367 |
6.24e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 38.49 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085608637 262 DGAALVMIGSAAAGKLQGLTPRARIV-----ATATSGADPVIMLTGPTPATRKVLDRAGLTVDDIDLF-------ELNEA 329
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILgfgltCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQ 289
|
90 100 110
....*....|....*....|....*....|....*...
gi 2085608637 330 FASVVLKfqkdlNIPDEKLNVNGGAIAMGHPLGATGAM 367
Cdd:PRK05952 290 REANLIQ-----ALFPHRVAVSSTKGATGHTLGASGAL 322
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
304-351 |
6.75e-03 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 38.29 E-value: 6.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2085608637 304 TPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVN 351
Cdd:cd00830 226 PESIEEALEKAGLTPDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVN 273
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
311-351 |
7.76e-03 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 35.55 E-value: 7.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2085608637 311 LDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVN 351
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVN 41
|
|
| |
