|
Name |
Accession |
Description |
Interval |
E-value |
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-377 |
1.23e-160 |
|
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: 455.92 E-value: 1.23e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 6 IIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTVGNGG--NLARKSLLEAGLDFKIPGITID 83
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEqqNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 84 RQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIKRpqSVYESEFPQFFERAPF-----AREGEDPSMIEAAEN 158
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPR--SLRWGVKPGNAELEDArlkdlTDANTGLPMGVTAEN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 159 VAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVKG----EYFNQDESIKPQLTLKTLGRLKPLLNE-GTVTV 233
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGrkgpVTVSSDEGIRPNTTLEKLAKLKPAFDPdGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 234 GNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELNEAFSSQV 313
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488404731 314 IASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRLFYMKHQF---RTIATMGIGGGIGNAALFE 377
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRggrYGLATMCIGGGQGAAVILE 385
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-378 |
3.96e-137 |
|
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: 396.08 E-value: 3.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 5 VIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTV--GNGGNLARKSLLEAGLDFKIPGITI 82
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLqaGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 83 DRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIKRPQSVYESEFPQF--FERAPFAREGEDPSMIEAAENVA 160
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLdgMLDDGLTDPFTGLSMGITAENVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 161 KKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVKGEY----FNQDESIKPQLTLKTLGRLKPLL-NEGTVTVGN 235
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKgpvvVDRDEGPRPDTTLEKLAKLKPAFkKDGTVTAGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 236 SCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELNEAFSSQVIA 315
Cdd:cd00751 241 ASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488404731 316 SQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRLFY-MKHQF--RTIATMGIGGGIGNAALFER 378
Cdd:cd00751 321 CLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHeLKRRGgrYGLATMCIGGGQGAAMVIER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-353 |
1.28e-134 |
|
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: 389.81 E-value: 1.28e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTV--GNGGNLARKSLLEAGLDFKIP 78
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLqaGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 79 GITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAP-------WKIKRPQSVYESEFPQFFErAPFAregeDPS 151
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPmllpkarWGYRMNAKLVDPMINPGLT-DPYT----GLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 152 MIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKV---KGEY-FNQDESIKPQLTLKTLGRLKPLLN 227
Cdd:COG0183 156 MGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVpdrKGEVvVDRDEGPRPDTTLEKLAKLKPAFK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 228 E-GTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELN 306
Cdd:COG0183 236 KdGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEIN 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 488404731 307 EAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRLFY 353
Cdd:COG0183 316 EAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLH 362
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-353 |
5.73e-126 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 367.17 E-value: 5.73e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 3 QPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVmslLDDVILGNTVGNGGNLARKSLLEAGLDFKIPGITI 82
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFLSKGMERE---IDDVILGNVVGPGGNVARLSALEAGLGLHIPGVTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 83 DRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPwkikrpqsvyesefpqFFERAPFAREG-EDPSMIEAAENVAK 161
Cdd:PRK06690 79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSP----------------FQNRARFSPETiGDPDMGVAAEYVAE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 162 KYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFkvkGEYfnQDESIKPQLTL-KTLGRLKP-LLNEGTVTVGNSCKK 239
Cdd:PRK06690 143 RYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF---NGL--LDESIKKEMNYeRIIKRTKPaFLHNGTVTAGNSCGV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 240 NDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELNEAFSSQVIASQQQ 319
Cdd:PRK06690 218 NDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAKE 297
|
330 340 350
....*....|....*....|....*....|....
gi 488404731 320 LNIPLNKLNCWGGAIATGHPYGASGAALVTRLFY 353
Cdd:PRK06690 298 LQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFY 331
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-355 |
4.47e-100 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 302.07 E-value: 4.47e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESL-------------LEPlfnhftdqypkvmSLLDDVILGN--TVGNGGNLAR 65
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELgaivikaaleragVPP-------------EQVDEVIMGQvlQAGAGQNPAR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 66 KSLLEAGLDFKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIKRPQSVYESEFPQFFERapFAR 145
Cdd:PRK05790 68 QAALKAGLPVEVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDT--MIH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 146 EG-----EDPSMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKV---KGEY--FNQDESIKPQLT 215
Cdd:PRK05790 146 DGltdafNGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIkqrKGDPvvVDTDEHPRPDTT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 216 LKTLGRLKPLLN-EGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQER 294
Cdd:PRK05790 226 AESLAKLRPAFDkDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAG 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488404731 295 LTINDINAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGA-ALVTRLFYMK 355
Cdd:PRK05790 306 WSLADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGArILVTLLHEMK 367
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-378 |
1.58e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 293.43 E-value: 1.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTVGNGGN--LARKSLLEAGLDFKIP 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEApaIGRVAALDAGLPVTVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 79 GITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAP-------WKIKRPQSvyesefpQFFERAPFAREGEDPS 151
Cdd:PRK06205 81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEfyttdmrWGVRGGGV-------QLHDRLARGRETAGGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 152 -------MIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKV---KGEY--FNQDESIKPQLTLKTL 219
Cdd:PRK06205 154 rfpvpggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVpqrKGDPtvVDRDEHPRADTTLESL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 220 GRLKPLLN----EGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERL 295
Cdd:PRK06205 234 AKLRPIMGkqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 296 TINDINAVELNEAFSSQVIASQQQLNIP---LNKLNCWGGAIATGHPYGASGAALVTRLFYMKHQFRT---IATMGIGGG 369
Cdd:PRK06205 314 TLDDIDLIELNEAFAAQVLAVLKEWGFGaddEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQArygLETMCIGGG 393
|
....*....
gi 488404731 370 IGNAALFER 378
Cdd:PRK06205 394 QGLAAVFER 402
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-364 |
1.12e-92 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 283.38 E-value: 1.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKV-MSLLDDVILG--NTVG-NGGNLARKSLLEAGLDFK 76
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNPGVdWEAVDDVIYGcaNQAGeDNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 77 IPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKI-------KRPQSVYESEFP-QFFERAPFAREGE 148
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMgkadsafSRQAEIFDTTIGwRFVNPLMKAQYGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 149 DpSMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKV---KGE--YFNQDESIKPQLTLKTLGRLK 223
Cdd:PRK09050 161 D-SMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIpqkKGDpvVVDRDEHPRPETTLEALAKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 224 PLL-NEGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINA 302
Cdd:PRK09050 240 PVFrPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDV 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488404731 303 VELNEAFSSQVIASQQQLNIPLN--KLNCWGGAIATGHPYGASGAALVTRLFYMKHQF---RTIATM 364
Cdd:PRK09050 320 IELNEAFAAQGLAVLRQLGLADDdaRVNPNGGAIALGHPLGMSGARLVLTALHQLERTggrYALCTM 386
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-348 |
3.56e-87 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 269.34 E-value: 3.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTVGNGG---NLARKSLLEAGLDFKI 77
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdsrNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 78 PGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIKRPQSVYESEFPQF----FERAP----FAREGED 149
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFdttiGARFPnpkiVAQYGND 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 150 pSMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVKG------EYFNQDESIKPQLTLKTLGRLK 223
Cdd:PRK08131 161 -SMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgrklppKLVAEDEHPRPSSTVEALTKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 224 PLLNEGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAV 303
Cdd:PRK08131 240 PLFEGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDII 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 488404731 304 ELNEAFSSQVIASQQQLNIPLN--KLNCWGGAIATGHPYGASGAALV 348
Cdd:PRK08131 320 EINEAFASQVLGCLKGLGVDFDdpRVNPNGGAIAVGHPLGASGARLA 366
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-351 |
2.13e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 252.23 E-value: 2.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYG-GRLKHLEPESLLEPLFNHFTDQYPKV-MSLLDDVILGntVG-----NGGNLARKSLLEAGL 73
Cdd:PRK07851 1 MPEAVIVSTARSPIGRAFkGSLKDMRPDDLAAQMVRAALDKVPALdPTDIDDLMLG--CGlpggeQGFNMARVVAVLLGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 74 DFkIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKikRPQSVYESEFPQFFE---RAPFAREGE-- 148
Cdd:PRK07851 79 DF-LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKG--NSDSLPDTKNPLFAEaqaRTAARAEGGae 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 149 ---DP-----------SMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVK-GEYFNQDESIKPQ 213
Cdd:PRK07851 156 awhDPredgllpdvyiAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPdGTVVSTDDGPRAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 214 LTLKTLGRLKPLLN-EGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQ 292
Cdd:PRK07851 236 TTYEKVSQLKPVFRpDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALAR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488404731 293 ERLTINDINAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRL 351
Cdd:PRK07851 316 AGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTL 374
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-378 |
5.29e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 240.42 E-value: 5.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYG-GRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTVG---NGGNLARKSLLEAGLDFK 76
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPeaeQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 77 IPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPW--KIKRPQSVYESEFPQFFErapfaregedpSMIE 154
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMmgHVVRPNPRLVEAAPEYYM-----------GMGH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 155 AAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVKGEY-------------FNQDESIKPQLTLKTLGR 221
Cdd:PRK07661 150 TAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgennklqeetitFSQDEGVRADTTLEILGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 222 LKPLLN-EGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDI 300
Cdd:PRK07661 230 LRPAFNvKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 301 NAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRLFY-MKH---QFrTIATMGIGGGIGNAALF 376
Cdd:PRK07661 310 GLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHeMKRrneQF-GIVTMCIGGGMGAAGVF 388
|
..
gi 488404731 377 ER 378
Cdd:PRK07661 389 EL 390
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-378 |
2.49e-73 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 233.31 E-value: 2.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESL-------------LEPlfnhftDQypkvmslLDDVILGNTVGNGGN---LA 64
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLgatvvrealaragVDP------DQ-------VGHVVFGHVIPTEPRdmyLS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 65 RKSLLEAGLDFKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKikrpqsvyesefpqfferAPFA 144
Cdd:PRK09051 69 RVAAINAGVPQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYL------------------LPAA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 145 REGE---DPSMIEA-----------------AENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKV---KG 201
Cdd:PRK09051 131 RWGArmgDAKLVDMmvgalhdpfgtihmgvtAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIktrKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 202 EY-FNQDESIKPQLTLKTLGRLKPLL--NEGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYL 278
Cdd:PRK09051 211 EVvFDTDEHVRADTTLEDLAKLKPVFkkENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYM 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 279 GVGPVPAVNQLLAQERLTINDINAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRLFYMKHqf 358
Cdd:PRK09051 291 GIGPVPATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQ-- 368
|
410 420
....*....|....*....|....*
gi 488404731 359 RT-----IATMGIGGGIGNAALFER 378
Cdd:PRK09051 369 RIggryaLVTMCIGGGQGIAAIFER 393
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-378 |
2.61e-73 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 233.32 E-value: 2.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKY-GGRLKHLEPESLLEPLFNHFTDQYPKV-MSLLDDVILG---NTVGNGGNLARKSLLEAGLDF 75
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNPALdPAEIDDIIWGcvqQTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 76 KIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPwkikrpqsvyesefpqfferapfAREGEDP----- 150
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP-----------------------MNHGVDFhpgls 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 151 --------SMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPfkVKGE-------YFNQDESIKPQLT 215
Cdd:PRK08947 138 knvakaagMMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIP--TEGHdadgvlkLFDYDEVIRPETT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 216 LKTLGRLKPLLN--EGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQE 293
Cdd:PRK08947 216 VEALAALRPAFDpvNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 294 RLTINDINAVELNEAFSSQVIASQQQLNIpLN----KLNCWGGAIATGHPYGASGAALVTRLF-YMKHQFRTI--ATMGI 366
Cdd:PRK08947 296 GLSISDIDVFELNEAFAAQSLPCLKDLGL-LDkmdeKVNLNGGAIALGHPLGCSGARISTTLLnLMERKDAQFglATMCI 374
|
410
....*....|..
gi 488404731 367 GGGIGNAALFER 378
Cdd:PRK08947 375 GLGQGIATVFER 386
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
48-348 |
4.96e-70 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 225.03 E-value: 4.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 48 LDDVILG--NTVG-NGGNLARKSLLEAGLDFKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESIS------- 117
Cdd:PRK07108 49 VEDVIMGcaNPEGaTGANIARQIALRAGLPVTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIScvqnemn 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 118 ----RAPWKIKRPQSVYESefpqfferapfaregedpsMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQE 193
Cdd:PRK07108 129 rhmlREGWLVEHKPEIYWS-------------------MLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 194 ILPF--------KVKGEYF------NQDESIKPQLTLKTLGRLKPLLNEGTVTVGNSCKKNDGAVLLIVMEENRARQLGF 259
Cdd:PRK07108 190 IVPItvtagvadKATGRLFtkevtvSADEGIRPDTTLEGVSKIRSALPGGVITAGNASQFSDGASACVVMNAKVAEREGL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 260 TEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHP 339
Cdd:PRK07108 270 QPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHP 349
|
....*....
gi 488404731 340 YGASGAALV 348
Cdd:PRK07108 350 YGVSGARLT 358
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-353 |
8.30e-70 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 224.52 E-value: 8.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTV--GNGGNLARKSLLEAGLDFKIP 78
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVItgGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 79 GITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESIS--------RAPWKIKRPQSVYESEFPQFFE--RAPFarege 148
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmhgsyiRAGAKFGDIKMVDLMQYDGLTDvfSGVF----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 149 dpsMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKV----KGEYFNQDESIKPQLTLKTLGRLKP 224
Cdd:PRK06633 157 ---MGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVtikkTTSLFDHDETVRPDTSLEILSKLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 225 LLNE-GTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAV 303
Cdd:PRK06633 234 AFDKnGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVI 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 488404731 304 ELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRLFY 353
Cdd:PRK06633 314 EVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIH 363
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
6-378 |
1.24e-69 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 224.11 E-value: 1.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 6 IIAAKRIAFGKY-GGRLKHLEPESLLEPLFNHFTDQYPKV-MSLLDDVILGNTV---GNGGNLARKSLLEAGLDFKIPGI 80
Cdd:PRK09052 10 IVAATRTPVGKApRGMFKNTRPDDLLAHVLRSAVAQVPGLdPKLIEDAIVGCAMpeaEQGLNVARIGALLAGLPNSVGGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 81 TIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIKRPQsvyesefpqfFERAPFAREgEDPS----MIEAA 156
Cdd:PRK09052 90 TVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPS----------MSPAIFARD-ENVGiaygMGLTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 157 ENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVKgEYF---------------NQDESIKPQLTLKTLGR 221
Cdd:PRK09052 159 EKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEIT-ERFpdlatgevdvktrtvDLDEGPRADTSLEGLAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 222 LKPLL-NEGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDI 300
Cdd:PRK09052 238 LKPVFaNKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 301 NAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRLFY--MKHQFR-TIATMGIGGGIGNAALFE 377
Cdd:PRK09052 318 DWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHglRRTNLKyGMVTMCVGTGMGAAGIFE 397
|
.
gi 488404731 378 R 378
Cdd:PRK09052 398 R 398
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-353 |
1.05e-68 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 221.51 E-value: 1.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTV--GNGGNLARKSLLEAGLDFKIP 78
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLqgGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 79 GITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIkrpqsvyesefpqfferaPFAREGE---DPSMIEA 155
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYIL------------------PGARWGYrmgDNEVIDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 156 ------------------AENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKV---KGE--YFNQDESIKP 212
Cdd:PRK08235 143 mvadgltcafsgvhmgvyGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIpqrKGDpiVVAKDEAPRK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 213 QLTLKTLGRLKPLLN-EGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLA 291
Cdd:PRK08235 223 DTTIEKLAKLKPVFDkTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLE 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488404731 292 QERLTINDINAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRLFY 353
Cdd:PRK08235 303 KTGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIH 364
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-357 |
1.78e-65 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 213.05 E-value: 1.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGnTVGNGG----NLARKSLLEAGLDFK 76
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMG-CVSQVGeqatNVARNAVLASKLPES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 77 IPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAP------WKIKRPQSVYESefPQFFERAPfareGEDP 150
Cdd:PRK06504 80 VPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPmgspstLPAKNGLGHYKS--PGMEERYP----GIQF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 151 SMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVK-----GEYFNQDESIKPQLTLKTLGRLKPL 225
Cdd:PRK06504 154 SQFTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITradgsGEMHTVDEGIRFDATLEGIAGVKLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 226 LNEGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVEL 305
Cdd:PRK06504 234 AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEV 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 488404731 306 NEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRLFYMKHQ 357
Cdd:PRK06504 314 NEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQ 365
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
15-348 |
6.47e-64 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 209.35 E-value: 6.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 15 GKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNT--VGN-GGNLARKSLLEAGLDFKIPGITIDRQCGSGLE 91
Cdd:PRK08242 17 GKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVtpVGDqGADIARTAVLAAGLPETVPGVQINRFCASGLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 92 AVIQACRMVQSGAGTIYIAGGVESISRAP-------WKIKrPQSVYESEF-PQFFerapfaregedpsmieAAENVAKKY 163
Cdd:PRK08242 97 AVNLAAAKVRSGWDDLVIAGGVESMSRVPmgsdggaWAMD-PSTNFPTYFvPQGI----------------SADLIATKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 164 HISRNEQDDFAYRSHQLSSKNMNNGNISQEILPfkVKGE----YFNQDESIKPQLTLKTLGRLKP--------------- 224
Cdd:PRK08242 160 GFSREDVDAYAVESQQRAAAAWAEGYFAKSVVP--VKDQngltILDHDEHMRPGTTMESLAKLKPsfammgemggfdava 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 225 LLNEGTV-------TVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTI 297
Cdd:PRK08242 238 LQKYPEVerinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488404731 298 NDINAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALV 348
Cdd:PRK08242 318 DDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMIL 368
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
5-378 |
2.09e-63 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 209.24 E-value: 2.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 5 VIIAAKRIAF--GKYGGrLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTVGNGGNLA---RKSLLEAGLDFKIPG 79
Cdd:PLN02287 49 VIVAAYRTPIckAKRGG-FKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnecRMAAFYAGFPETVPV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 80 ITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAP--WKIKRPQSVyeSEFPQfferapfAREGEDPsMIEAAE 157
Cdd:PLN02287 128 RTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPmaWEGGVNPRV--ESFSQ-------AQDCLLP-MGITSE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 158 NVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVK------GE----YFNQDESIKPQLTLKTLGRLKPLLN 227
Cdd:PLN02287 198 NVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKivdpktGEekpiVISVDDGIRPNTTLADLAKLKPVFK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 228 E-GTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELN 306
Cdd:PLN02287 278 KnGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEIN 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488404731 307 EAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALV-TRLFYMKHQFRT----IATMGIGGGIGNAALFER 378
Cdd:PLN02287 358 EAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVaTLLHEMKRRGKDcrfgVVSMCIGTGMGAAAVFER 434
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-378 |
2.21e-63 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 207.25 E-value: 2.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESL----LEPLFNHfTDQYPkvmSLLDDVILG--NTVG-NGGNLARKSLLEAGL 73
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLgahvLKGLVDR-TGIDP---AAVDDVIFGcvDTIGpQAGNIARTSWLAAGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 74 DFKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPwkIKRPQSVYEsefpQFFERAPFA-------RE 146
Cdd:PRK07801 77 PEEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTAGE----QLGFTSPFAeskgwlhRY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 147 GEDP-SMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFkvkgEYFNQDESIKpQLTLKTLGRLKPL 225
Cdd:PRK07801 151 GDQEvSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV----GGVTVDEGPR-ETSLEKMAGLKPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 226 LNEGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVEL 305
Cdd:PRK07801 226 VEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEI 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488404731 306 NEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRLFymkHQF-RT-----IATMGIGGGIGNAALFER 378
Cdd:PRK07801 306 NEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLL---HELeRTggrygLQTMCEGGGTANVTIIER 381
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-354 |
3.67e-63 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 207.05 E-value: 3.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGN--TVGNGGNLARKSLLEAGLDFKIP 78
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQvlTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 79 GITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIKRPQSVYESEFPQFFERapFAREG-----EDPSMI 153
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDS--MITDGlwdafNDYHMG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 154 EAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKV---KGE--YFNQDESIKPQLTLKTLGRLKPLL-N 227
Cdd:PRK05656 159 ITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIpqrKGEplAFATDEQPRAGTTAESLAKLKPAFkK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 228 EGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELNE 307
Cdd:PRK05656 239 DGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 488404731 308 AFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGA-ALVTRLFYM 354
Cdd:PRK05656 319 AFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCrVLVTLLHEM 366
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-349 |
4.74e-62 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 204.19 E-value: 4.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVIlGNTVGNGG----NLARKSLLEAGLDFK 76
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVI-GGCVTQAGeqsnNITRTAWLHAGLPYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 77 IPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKikrpQSVYesefPQFFERAPFAREGEDPSMIEAA 156
Cdd:PRK07850 80 VGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLG----ANAG----PGRGLPRPDSWDIDMPNQFEAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 157 ENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKV---------KGEY--FNQDESIKpQLTLKTLGRLKPL 225
Cdd:PRK07850 152 ERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQApvldeegqpTGETrlVTRDQGLR-DTTMEGLAGLKPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 226 LNEGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVEL 305
Cdd:PRK07850 231 LEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEI 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 488404731 306 NEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVT 349
Cdd:PRK07850 311 NEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLIT 354
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-351 |
2.65e-60 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 199.56 E-value: 2.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYggRLKH--------LEPESLLEPLFNHFTDQY---PKVmslLDDVILGNTVGNGGNLA---RK 66
Cdd:PRK06445 1 LEDVYLVDFARTAFSRF--RPKDpqkdvfnnIRPEELAAMLINRLIEKTgikPEE---IDDIITGCALQVGENWLyggRH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 67 SLLEAGLDFKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPwkikrpqsVYESEF----PQFFERAP 142
Cdd:PRK06445 76 PIFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP--------MGDNPHiepnPKLLTDPK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 143 FAREGEDP--SMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVKGE----YFNQDESIKPQLTL 216
Cdd:PRK06445 148 YIEYDLTTgyVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEgkkkVVDVDQSVRPDTSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 217 KTLGRLKPLLN-EGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERL 295
Cdd:PRK06445 228 EKLAKLPPAFKpDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGL 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 488404731 296 TINDINAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRL 351
Cdd:PRK06445 308 SVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTL 363
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
48-363 |
7.32e-60 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 199.47 E-value: 7.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 48 LDDVILG--NTVGNGGNLARKSLLEAGLDFKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIKR 125
Cdd:PRK08170 49 LDEVILGcaMPSPDEANIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 126 PQSVYESEF-----------------PQFFerAP---FAREGEDP----SMIEAAENVAKKYHISRNEQDDFAYRSHQLS 181
Cdd:PRK08170 129 KMVRWLAGWyaaksigqklaalgklrPSYL--APvigLLRGLTDPvvglNMGQTAEVLAHRFGITREQMDAYAARSHQRL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 182 SKNMNNGNISqEILP-FKVKGEYFNQDESIKPQLTLKTLGRLKPLLNE--GTVTVGNSCKKNDGAVLLIVMEENRARQLG 258
Cdd:PRK08170 207 AAAQAEGRLK-EVVPlFDRDGKFYDHDDGVRPDSSMEKLAKLKPFFDRpyGRVTAGNSSQITDGACWLLLASEEAVKKYG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 259 FTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELNEAFSSQVIASQ----------QQLNIP----- 323
Cdd:PRK08170 286 LPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLaawadeeycrEQLGLDgalge 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 488404731 324 --LNKLNCWGGAIATGHPYGASGAALVTRLFYMKHQF---RTIAT 363
Cdd:PRK08170 366 ldRERLNVDGGAIALGHPVGASGARIVLHLLHALKRRgtkRGIAA 410
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
5-251 |
3.94e-59 |
|
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: 192.52 E-value: 3.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 5 VIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGN--TVGNGGNLARKSLLEAGLDFKIPGITI 82
Cdd:pfam00108 2 VIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNvlQAGEGQNPARQAALKAGIPDSAPAVTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 83 DRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAP--------WKIKRPQ------SVYESEFPQFferapfaregE 148
Cdd:pfam00108 82 NKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPyalptdarSGLKHGDekkhdlLIPDGLTDAF----------N 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 149 DPSMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVKGE----YFNQDESIKPQLTLKTLGRLKP 224
Cdd:pfam00108 152 GYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRkgkpTVDKDEGIRPPTTAEPLAKLKP 231
|
250 260
....*....|....*....|....*...
gi 488404731 225 LLN-EGTVTVGNSCKKNDGAVLLIVMEE 251
Cdd:pfam00108 232 AFDkEGTVTAGNASPINDGAAAVLLMSE 259
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-357 |
3.64e-50 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 172.97 E-value: 3.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 2 KQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTV--GNGGNLARKSLLEAGLDFKIPG 79
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLsaNLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 80 ITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIkrPQSVYESEFPQFFERAPFAREG-----EDPSMIE 154
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYL--PEARKGSRLGHDTVVDGMLKDGlwdvyNDFGMGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 155 AAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVKGE------YFNQDESIKpQLTLKTLGRLKPLLNE 228
Cdd:PLN02644 159 CAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGrgrpsvIVDKDEGLG-KFDPAKLRKLRPSFKE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 229 --GTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELN 306
Cdd:PLN02644 238 dgGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEIN 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 488404731 307 EAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGA-ALVTRLFYMKHQ 357
Cdd:PLN02644 318 EAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGArILVTLLGVLRSK 369
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
62-349 |
7.57e-49 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 170.55 E-value: 7.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 62 NLARKSLLEAGLDFKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIKRP-----------QSVY 130
Cdd:PRK08963 67 NIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKlaralvdlnkaRTLG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 131 ES-------EFPQFFERAPFARE---GEdpSMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEIL----- 195
Cdd:PRK08963 147 QRlklfsrlRLRDLLPVPPAVAEystGL--RMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMtahvp 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 196 PFKvkgEYFNQDESIKPQLTLKTLGRLKPLLNE--GTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEgIKFVNS---AT 270
Cdd:PRK08963 225 PYK---QPLEEDNNIRGDSTLEDYAKLRPAFDRkhGTVTAANSTPLTDGAAAVLLMSESRAKALGLTP-LGYLRSyafAA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 271 VGVQPQYLgVGPVPAVNQLLAQERLTINDINAVELNEAFSSQVIA----------SQQQLN-------IPLNKLNCWGGA 333
Cdd:PRK08963 301 IDVWQDML-LGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLGrsqaigeVDMSKFNVLGGS 379
|
330
....*....|....*.
gi 488404731 334 IATGHPYGASGAALVT 349
Cdd:PRK08963 380 IAYGHPFAATGARMIT 395
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-357 |
2.31e-48 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 168.26 E-value: 2.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTV--GNGGNLARKSLLEAGLDFKIP 78
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIqaGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 79 GITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIKR-----PQSVYESEFPqfFERAPFAREGEDPSMI 153
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSdlrwgPKHLLHKNYK--IDDAMLVDGLIDAFYF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 154 E----AAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFkvkgEYFNQDESIKpQLTLKTLGRLKPLLNE- 228
Cdd:PRK06366 159 EhmgvSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPF----NDLDRDEGIR-KTTMEDLAKLPPAFDKn 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 229 GTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELNEA 308
Cdd:PRK06366 234 GILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNEA 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 488404731 309 FSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGA-ALVTRLFYMKHQ 357
Cdd:PRK06366 314 FSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSrIIVTLINALKTR 363
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
48-351 |
8.49e-45 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 158.90 E-value: 8.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 48 LDDVILGNTV--GNGGNLARKSLLEAGLDFKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPWKIKR 125
Cdd:PRK06954 53 IDEVVMGCVLpaGQGQAPARQAALGAGLPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 126 PQSVYESEFPQFFERApFAREGEDP-----SMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVK 200
Cdd:PRK06954 133 ARGGMRMGHGQVLDHM-FLDGLEDAydkgrLMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 201 GE----YFNQDESIKpQLTLKTLGRLKPLLNE-GTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQP 275
Cdd:PRK06954 212 GKkgdtVIDRDEQPF-KANPEKIPTLKPAFSKtGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAP 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488404731 276 QYLGVGPVPAVNQLLAQERLTINDINAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGASGAALVTRL 351
Cdd:PRK06954 291 SKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTL 366
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-348 |
3.40e-43 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 155.32 E-value: 3.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 1 MKQPVIIAAKRI--AFGKYG-GRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTVGNG---GNLARKSLLEAGLD 74
Cdd:PRK06025 1 MAEAYIIDAVRTprGIGKVGkGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGkqgGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 75 FKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISrapwkikrpqsvYESEFPqfferAPFAREGEDPSMIE 154
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMS------------YTAAMA-----AEDMAAGKPPLGMG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 155 AAENVAKKYH-----------------ISRNEQDDFAYRSHQLSSKNMNNGNISQEILP-FKVKGEY-FNQDESIKPQLT 215
Cdd:PRK06025 144 SGNLRLRALHpqshqgvcgdaiatmegITREALDALGLESQRRAARAIKEGRFDKSLVPvYRDDGSVaLDHEEFPRPQTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 216 LKTLGRLKPL--------LNEGTVT-------------------VGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNS 268
Cdd:PRK06025 224 AEGLAALKPAftaiadypLDDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAM 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 269 ATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELNEAFSsqVIASQ--QQLNIPLNKLNCWGGAIATGHPYGASGAA 346
Cdd:PRK06025 304 ANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFA--VVAEKfiRDLDLDRDKVNVNGGAIALGHPIGATGSI 381
|
..
gi 488404731 347 LV 348
Cdd:PRK06025 382 LI 383
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
5-357 |
2.41e-37 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 139.65 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 5 VIIAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTDQYPKVMSLLDDVILGNTVGNGG--NLARKSLLEAGLDFKIPGITI 82
Cdd:PRK09268 10 AILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRdfNLTRECVLGSALSPYTPAYDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 83 DRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPW---------------------KIK-----RPQSVyESEFPQ 136
Cdd:PRK09268 90 QQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIavneglrkillelnrakttgdRLKalgklRPKHL-APEIPR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 137 FFERapfaREGEdpSMIEAAENVAKKYHISRNEQDDFAYRSHQLSSKNMNNGNISQEILPFkvKGeyFNQDESIKPQLTL 216
Cdd:PRK09268 169 NGEP----RTGL--SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF--LG--LTRDNNLRPDSSL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 217 KTLGRLKPLL---NEGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATVGVQ----PQYLGVGPVPAVNQL 289
Cdd:PRK09268 239 EKLAKLKPVFgkgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhgKEGLLMAPAYAVPRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 290 LAQERLTINDINAVELNEAFSSQVIASQQQ------------LNIPL-----NKLNCWGGAIATGHPYGASGAALVTRLF 352
Cdd:PRK09268 319 LARNGLTLQDFDFYEIHEAFASQVLATLKAwedeeycrerlgLDAPLgsidrSKLNVNGSSLAAGHPFAATGGRIVATLA 398
|
....*
gi 488404731 353 YMKHQ 357
Cdd:PRK09268 399 KLLAE 403
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-355 |
2.75e-36 |
|
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: 136.08 E-value: 2.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 7 IAAKRIAFGKYGGRLKHLEPESLLEPLFNHFTD---QYPKVMSLLDDVILGNTV--GNGGNLARKSLLEAGLDFKIPGIT 81
Cdd:cd00826 1 AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAalePAGVAAGAVEEACLGQVLgaGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 82 IDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISrapwkikrpqsvyesefpqfferapfaregedpsmiEAAENVAK 161
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME------------------------------------TSAENNAK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 162 KYHI--------SRNEQDDFAYRSHQLSSKNMNNGNISQEILPFKVKGEYFNQ----DESIKPQL--TLKTLGRLKPLLN 227
Cdd:cd00826 125 EKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIhsdaDEYIQFGDeaSLDEIAKLRPAFD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 228 -EGTVTVGNSCKKNDGAVLLIVMEENRARQLGFTE---GI----KFVNSATVGVQPQYL----GVGPVPAVNQLLAQERL 295
Cdd:cd00826 205 kEDFLTAGNACGLNDGAAAAILMSEAEAQKHGLQSkarEIqaleMITDMASTFEDKKVIkmvgGDGPIEAARKALEKAGL 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488404731 296 TINDINAVELNEAFSSQVIASQQQLNI-PLNK-----------------LNCWGGAIATGHPYGASGAA-LVTRLFYMK 355
Cdd:cd00826 285 GIGDLDLIEAHDAFAANACATNEALGLcPEGQggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAiCAELCFELK 363
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
264-378 |
4.10e-31 |
|
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: 114.66 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 264 KFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDINAVELNEAFSSQVIASQQQLNIPLNKLNCWGGAIATGHPYGAS 343
Cdd:pfam02803 6 RIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHPLGAS 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 488404731 344 GA-ALVTRLFYMKHQFRTI--ATMGIGGGIGNAALFER 378
Cdd:pfam02803 86 GArILVTLLHELKRRGGKYglASLCIGGGQGVAMIIER 123
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
234-358 |
3.65e-09 |
|
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: 57.07 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 234 GNSCKKNDGAVLLIVMEENRARQLGFTEGIKFVNSATV----GVQPQYLGVGPVPAVNQLLAQERLTINDINAVELNEAF 309
Cdd:cd00327 95 SEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATfdgaSMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTG 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488404731 310 SSQVIASQQQLNIP---LNKLNCWGGAIATGHPYGASG-AALVTRLFYMKHQF 358
Cdd:cd00327 175 TPIGDAVELALGLDpdgVRSPAVSATLIMTGHPLGAAGlAILDELLLMLEHEF 227
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
49-352 |
1.74e-08 |
|
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: 55.73 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 49 DDVILGNTVGN--GGNLARKSLLEAGLDfKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRAPwkikRP 126
Cdd:cd00829 39 DAVVVGNAAGGrfQSFPGALIAEYLGLL-GKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVP----TG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 127 QSVYESEFPQFFErapFAREGEDPSMIEAAENVAK----KYHISRNEQDDFAYRSHQLSSKNMNngniSQEILPFKVkge 202
Cdd:cd00829 114 DEAGGRASDLEWE---GPEPPGGLTPPALYALAARrymhRYGTTREDLAKVAVKNHRNAARNPY----AQFRKPITV--- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 203 yfnqDESIK-PQLTLktlgrlkPLlnegtvTVGNSCKKNDGAVLLIVMEENRARQLGFT----EGIKFVN-SATVGVQPQ 276
Cdd:cd00829 184 ----EDVLNsRMIAD-------PL------RLLDCCPVSDGAAAVVLASEERARELTDRpvwiLGVGAASdTPSLSERDD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 277 YLGVGP-VPAVNQLLAQERLTINDINAVELNEAFSSQVIasqQQL------------------------NIPlnkLNCWG 331
Cdd:cd00829 247 FLSLDAaRLAARRAYKMAGITPDDIDVAELYDCFTIAEL---LALedlgfcekgeggklvregdtaiggDLP---VNTSG 320
|
330 340
....*....|....*....|.
gi 488404731 332 GAIATGHPYGASGAALVTRLF 352
Cdd:cd00829 321 GLLSKGHPLGATGLAQAVEAV 341
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
241-357 |
7.26e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 44.27 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 241 DGAVLLIVMEENRARQ---------LGFTegikFVNSATVGVQPQYLGVGPVPAVNQLLAQERLTINDIN-------AVE 304
Cdd:PRK05952 210 EGGAILVLESAELAQKrgakiygqiLGFG----LTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDyihahgtATR 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 488404731 305 LNEAFSSQVIAS--QQQLNIPLNKlncwgGAiaTGHPYGASGA-ALVTRLFYMKHQ 357
Cdd:PRK05952 286 LNDQREANLIQAlfPHRVAVSSTK-----GA--TGHTLGASGAlGVAFSLLALRHQ 334
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
72-348 |
7.31e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 44.45 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 72 GLDFKIPgITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISrapwKIKRPQSV--------YESEFPQFFERAP- 142
Cdd:PRK12578 69 GLTGKVP-LRVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMT----EVDTSTSLaiggrggnYQWEYHFYGTTFPt 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 143 -FAregedpsmIEAAENVAKkYHISRNEQDDFAYRSHQLSSKNmnngnisqeilpfkvKGEYFNQDESIKPQLTLKTLGR 221
Cdd:PRK12578 144 yYA--------LYATRHMAV-YGTTEEQMALVSVKAHKYGAMN---------------PKAHFQKPVTVEEVLKSRAISW 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404731 222 LKPLLNegtvtvgnSCKKNDGAVLLIVMEENRARQLG-----FTEGIKFVN-SATVGVQPQYLGV-GPVPAVNQLLAQER 294
Cdd:PRK12578 200 PIKLLD--------SCPISDGSATAIFASEEKVKELKidspvWITGIGYANdYAYVARRGEWVGFkATQLAARQAYNMAK 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488404731 295 LTINDINAVELNEAFSSQVIASQQQL---------------------NIPlnkLNCWGGAIATGHPYGASGAALV 348
Cdd:PRK12578 272 VTPNDIEVATVHDAFTIAEIMGYEDLgftekgkggkfieegqsekggKVG---VNLFGGLKAKGHPLGATGLSMI 343
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
76-119 |
1.23e-03 |
|
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: 40.12 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 488404731 76 KIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESISRA 119
Cdd:cd00327 58 GGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEFVFG 101
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
73-116 |
9.04e-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: 37.61 E-value: 9.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 488404731 73 LDFKIPGITIDRQCGSGLEAVIQACRMVQSGAGTIYIAGGVESI 116
Cdd:pfam00109 160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
|
|
| |
