|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
1-333 |
5.54e-156 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 446.13 E-value: 5.54e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 1 MHRLQVVLGHLAGRSESSSALQAAPCSAGFPQASAS------DVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQ 74
Cdd:PLN02287 5 INRQRVLLRHLRPSSSEPSSLSASACAAGDSAAYHRttafgdDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 75 DVKLKPECLGDISVGNVLQPGAGAAMA-RIAQFLSGIPETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESM 153
Cdd:PLN02287 85 KTGLNPSEVGDIVVGTVLAPGSQRANEcRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 154 TLSERGNPGNISSRLLENEKARDCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDD 233
Cdd:PLN02287 165 TTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 234 K-GDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGV 312
Cdd:PLN02287 245 KtGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGV 324
|
330 340
....*....|....*....|.
gi 1958797581 313 PPDIMGIGPAYAIPAALQKAG 333
Cdd:PLN02287 325 DPAVMGIGPAVAIPAAVKAAG 345
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
39-333 |
5.40e-135 |
|
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: 390.30 E-value: 5.40e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 39 VVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSA 118
Cdd:cd00751 1 VIVSAVRTPIGRFG-GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEK----------ARDCLIPMGITSENV 188
Cdd:cd00751 80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTldgmlddgltDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 189 AERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTtvlddKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGG 268
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEV-----PGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:cd00751 235 TVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAG 299
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
36-333 |
1.89e-122 |
|
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: 358.61 E-value: 1.89e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVP 115
Cdd:COG0183 2 REVVIVDAVRTPFGRFG-GALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 116 LSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLS----------ERGNPGNISSRLLENEKARDCLIPMGITS 185
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRApmllpkarwgYRMNAKLVDPMINPGLTDPYTGLSMGETA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTtvlddKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFK 265
Cdd:COG0183 161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEV-----PDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958797581 266 DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:COG0183 236 KDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAG 303
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
40-333 |
2.75e-113 |
|
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: 335.35 E-value: 2.75e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 40 VVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSAV 119
Cdd:TIGR01930 1 IVAAARTPIGKFG-GSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 120 NRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT----LSERGNPGNISSRLLENEKAR-------DCLIPMGITSENV 188
Cdd:TIGR01930 80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSrvpyGVPRSLRWGVKPGNAELEDARlkdltdaNTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 189 AERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttvldDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGG 268
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVT-----VKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:TIGR01930 235 TVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAG 299
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
36-333 |
7.15e-109 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 324.03 E-value: 7.15e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVP 115
Cdd:PRK05790 2 KDVVIVSAARTPIGKFG-GALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 116 LSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLI-----------PMGIT 184
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIhdgltdafngyHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 185 SENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttVLDDKGDrkTITVSQDEGVRPSTTMEGLAKLKPAF 264
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVT--IKQRKGD--PVVVDTDEHPRPDTTAESLAKLRPAF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958797581 265 KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK05790 237 DKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAG 305
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
38-291 |
9.33e-104 |
|
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: 306.15 E-value: 9.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 38 VVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLS 117
Cdd:pfam00108 1 VVIVSAARTPFGSFG-GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 118 AVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGN-ISSRLLENEKARDCLIP-----------MGITS 185
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDaRSGLKHGDEKKHDLLIPdgltdafngyhMGLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGdrktiTVSQDEGVRPSTTMEGLAKLKPAFK 265
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-----TVDKDEGIRPPTTAEPLAKLKPAFD 234
|
250 260
....*....|....*....|....*.
gi 1958797581 266 DGGSTTAGNSSQVSDGAAAVLLARRS 291
Cdd:pfam00108 235 KEGTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
37-333 |
4.37e-95 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 289.21 E-value: 4.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 37 DVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVK-LKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPETV 114
Cdd:PRK09052 7 DAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPgLDPKLIEDAIVGCAMPEAEqGLNVARIGALLAGLPNSV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 115 PLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSE-RGNPGNISSRLLENEKARDCLIPMGITSENVAERFG 193
Cdd:PRK09052 87 GGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPmMGNKPSMSPAIFARDENVGIAYGMGLTAEKVAEQWK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 194 ISRQKQDAFALASQQKAASAQSKGCFRAEIVP--VTTTVLDDKG---DRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGG 268
Cdd:PRK09052 167 VSREDQDAFALESHQKAIAAQQAGEFKDEITPyeITERFPDLATgevDVKTRTVDLDEGPRADTSLEGLAKLKPVFANKG 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK09052 247 SVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAG 311
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
39-333 |
6.25e-88 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 270.47 E-value: 6.25e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 39 VVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLqPGA--GAAMARIAQFLSGIPETVPL 116
Cdd:PRK07661 5 VIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAM-PEAeqGLNMARNIGALAGLPYTVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGnpGNI---SSRLLENekARDCLIPMGITSENVAERFG 193
Cdd:PRK07661 84 ITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--GHVvrpNPRLVEA--APEYYMGMGHTAEQVAVKYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 194 ISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVL----DDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGS 269
Cdd:PRK07661 160 ISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRtvgeNNKLQEETITFSQDEGVRADTTLEILGKLRPAFNVKGS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958797581 270 TTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK07661 240 VTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
34-333 |
1.34e-80 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 251.80 E-value: 1.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 34 SASDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPE 112
Cdd:PRK09051 1 MMREVVVVSGVRTAIGTFG-GSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPrDMYLSRVAAINAGVPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 113 TVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCL----------IPMG 182
Cdd:PRK09051 80 ETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMvgalhdpfgtIHMG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 183 ITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTtvlddKGDRKTITVSQDEGVRPSTTMEGLAKLKP 262
Cdd:PRK09051 160 VTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEI-----KTRKGEVVFDTDEHVRADTTLEDLAKLKP 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958797581 263 AF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK09051 235 VFkKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAG 306
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
36-333 |
1.96e-74 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 236.42 E-value: 1.96e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVP 115
Cdd:PRK06205 2 RDAVICEPVRTPVGRFG-GAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 116 LSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSE----------RGNPGNISSRLL---ENEKARDCLIPMG 182
Cdd:PRK06205 81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEfyttdmrwgvRGGGVQLHDRLArgrETAGGRRFPVPGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 183 I--TSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttVLDDKGDrkTITVSQDEGVRPSTTMEGLAKL 260
Cdd:PRK06205 161 MieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVT--VPQRKGD--PTVVDRDEHPRADTTLESLAKL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958797581 261 KP--AFKDGGST-TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06205 237 RPimGKQDPEATvTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAG 312
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
37-333 |
3.38e-71 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 227.68 E-value: 3.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 37 DVVVVHGRRTPIGRAG-----RGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMA-RIAQFLSGI 110
Cdd:PRK06445 3 DVYLVDFARTAFSRFRpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLYGgRHPIFLARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 111 PETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERG-NPG-NISSRLLENEKARDCLIP----MGIT 184
Cdd:PRK06445 83 PYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGdNPHiEPNPKLLTDPKYIEYDLTtgyvMGLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 185 SENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVlddkgDRKTITVSQDEGVRPSTTMEGLAKLKPAF 264
Cdd:PRK06445 163 AEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEV-----EGKKKVVDVDQSVRPDTSLEKLAKLPPAF 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958797581 265 KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06445 238 KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAG 306
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
36-333 |
2.91e-70 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 225.22 E-value: 2.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQ-DVKLKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPET 113
Cdd:PRK09050 2 TEAFICDAIRTPIGRYG-GALSSVRADDLGAVPLKALMArNPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 114 VPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSergnP---GNISSRLLENEKARDCLI----------- 179
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRA----PfvmGKADSAFSRQAEIFDTTIgwrfvnplmka 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 180 -----PMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVttTVLDDKGDrkTITVSQDEGVRPSTTM 254
Cdd:PRK09050 157 qygvdSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPV--TIPQKKGD--PVVVDRDEHPRPETTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 255 EGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGL-PILGVLrSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK09050 233 EALAKLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLtPRARIL-GMATAGVEPRIMGIGPAPATRKLLARLG 311
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
36-333 |
4.52e-70 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 224.65 E-value: 4.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 36 SDVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPETV 114
Cdd:PRK07108 2 TEAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 115 PLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLIPMGITSENVAERFGI 194
Cdd:PRK07108 82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHMLREGWLVEHKPEIYWSMLQTAENVAKRYGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 195 SRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTT--VLDDKGDR---KTITVSQDEGVRPSTTMEGLAKLKPAFKdGGS 269
Cdd:PRK07108 162 SKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTagVADKATGRlftKEVTVSADEGIRPDTTLEGVSKIRSALP-GGV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958797581 270 TTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK07108 241 ITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAG 304
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
37-333 |
9.33e-68 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 218.68 E-value: 9.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 37 DVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVL-QDVKLKPECLGDISVGNVLQPG-AGAAMARIAQFLSGIPETV 114
Cdd:PRK08947 3 DVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLaRNPALDPAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPHSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 115 PLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVE-----SMTLSERGNPGnissrlLENEKARDCLIpMGITSENVA 189
Cdd:PRK08947 83 PAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEhmghvPMNHGVDFHPG------LSKNVAKAAGM-MGLTAEMLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 190 ERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTvlDDKGDRKTITVsqDEGVRPSTTMEGLAKLKPAFKD-GG 268
Cdd:PRK08947 156 KMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGH--DADGVLKLFDY--DEVIRPETTVEALAALRPAFDPvNG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK08947 232 TVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAG 296
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
37-333 |
6.70e-67 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 216.68 E-value: 6.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 37 DVVVVHGRRTPIGrAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPL 116
Cdd:PRK05656 3 DVVIVAATRTAIG-SFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLIP-----------MGITS 185
Cdd:PRK05656 82 MTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITdglwdafndyhMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttVLDDKGDrkTITVSQDEGVRPSTTMEGLAKLKPAFK 265
Cdd:PRK05656 162 ENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIL--IPQRKGE--PLAFATDEQPRAGTTAESLAKLKPAFK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958797581 266 DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK05656 238 KDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAG 305
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
38-333 |
4.77e-61 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 201.41 E-value: 4.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 38 VVVVHGRRTPIGRAGrgGFKDTTPDELLSAVLTA-VLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPL 116
Cdd:PRK06633 5 VYITHAKRTAFGSFM--GSLSTTPAPMLAAHLIKdILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSR--------LLENEKARDCL--IPMGITSE 186
Cdd:PRK06633 83 YTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKfgdikmvdLMQYDGLTDVFsgVFMGITAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 187 NVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVlddkgDRKTITVSQDEGVRPSTTMEGLAKLKPAFKD 266
Cdd:PRK06633 163 NISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTI-----KKTTSLFDHDETVRPDTSLEILSKLRPAFDK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958797581 267 GGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06633 238 NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAG 304
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
37-333 |
6.11e-61 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 201.39 E-value: 6.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 37 DVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDV-KLKPECLGDISVGnVLQPG--AGAAMARIAQFLSGIPeT 113
Cdd:PRK07851 3 EAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLG-CGLPGgeQGFNMARVVAVLLGYD-F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 114 VPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSR---LLENEKAR--------------- 175
Cdd:PRK07851 81 LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLPDTknpLFAEAQARtaaraeggaeawhdp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 176 -------DCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTT---TVlddkgdrktitVSQD 245
Cdd:PRK07851 161 redgllpDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLpdgTV-----------VSTD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 246 EGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAI 325
Cdd:PRK07851 230 DGPRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEAS 309
|
....*...
gi 1958797581 326 PAALQKAG 333
Cdd:PRK07851 310 KQALARAG 317
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
37-333 |
2.05e-60 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 199.55 E-value: 2.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 37 DVVVVHGRRTPIGrAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPL 116
Cdd:PLN02644 2 DVCIVGVARTPIG-GFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLI-----------PMGITS 185
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLkdglwdvyndfGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVlddKGDRKTITVSQDEGVRpSTTMEGLAKLKPAFK 265
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPG---GRGRPSVIVDKDEGLG-KFDPAKLRKLRPSFK 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958797581 266 -DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PLN02644 237 eDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAG 305
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
39-333 |
5.23e-58 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 193.39 E-value: 5.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 39 VVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSA 118
Cdd:PRK08235 5 VIVSAARTPFGKFG-GSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTET 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLI-----------PMGITSEN 187
Cdd:PRK08235 84 VNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVadgltcafsgvHMGVYGGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 188 VAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVttTVLDDKGDrkTITVSQDEGVRPSTTMEGLAKLKPAFKDG 267
Cdd:PRK08235 164 VAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPV--TIPQRKGD--PIVVAKDEAPRKDTTIEKLAKLKPVFDKT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958797581 268 GSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK08235 240 GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTG 305
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
39-333 |
1.05e-57 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 192.24 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 39 VVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPETVPLS 117
Cdd:PRK07850 5 VIVEAVRTPIGKRN-GWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 118 AVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTL--------SERGNPgnissrlleneKARDCLIPMG---ITSE 186
Cdd:PRK07850 84 TIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRvplganagPGRGLP-----------RPDSWDIDMPnqfEAAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 187 NVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDR--KTITVSQDEGVRpSTTMEGLAKLKPAF 264
Cdd:PRK07850 153 RIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEGQPtgETRLVTRDQGLR-DTTMEGLAGLKPVL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958797581 265 kDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK07850 232 -EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAG 299
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
45-333 |
4.64e-56 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 188.55 E-value: 4.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 45 RTPIGRAGRGG-FKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPG-AGAAMARIAQFLSGIPETVPLSAVNRQ 122
Cdd:PRK08242 11 RTPRGKGKKDGsLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPGVQINRF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 123 CSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPG---------NISSRllenekardcLIPMGITSENVAERFG 193
Cdd:PRK08242 91 CASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGgawamdpstNFPTY----------FVPQGISADLIATKYG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 194 ISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTT----TVLDdkgdrktitvsQDEGVRPSTTMEGLAKLKPAFKDGGS 269
Cdd:PRK08242 161 FSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDqnglTILD-----------HDEHMRPGTTMESLAKLKPSFAMMGE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 270 T---------------------TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAA 328
Cdd:PRK08242 230 MggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKA 309
|
....*
gi 1958797581 329 LQKAG 333
Cdd:PRK08242 310 LAKAG 314
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
37-333 |
1.89e-55 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 186.91 E-value: 1.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 37 DVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAA-MARIAQFLSGIPETVP 115
Cdd:PRK08131 3 DAYIYDGLRSPFGRHA-GALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRnVARNALLLAGLPVTVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 116 LSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSE--RGNPGNISSRLLeneKARDCLI-------------- 179
Cdd:PRK08131 82 GQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPfvMGKAESAFSRDA---KVFDTTIgarfpnpkivaqyg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 180 --PMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDRKtitVSQDEGVRPSTTMEGL 257
Cdd:PRK08131 159 ndSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLPPKL---VAEDEHPRPSSTVEAL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958797581 258 AKLKPAFkDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK08131 236 TKLKPLF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAG 310
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
38-333 |
2.67e-55 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 187.11 E-value: 2.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 38 VVVVHGRRTPIGRAGRGgFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLS 117
Cdd:PRK08963 7 IAIVSGLRTPFAKQATA-FHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 118 AVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDC--------------LIP--- 180
Cdd:PRK08963 86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLNKARTLgqrlklfsrlrlrdLLPvpp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 181 ----------MGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEivpVTTTVLDDKGDrktiTVSQDEGVRP 250
Cdd:PRK08963 166 avaeystglrMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDE---VMTAHVPPYKQ----PLEEDNNIRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 251 STTMEGLAKLKPAF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPP-DIMGIGPAYAIPAA 328
Cdd:PRK08963 239 DSTLEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLA 318
|
....*
gi 1958797581 329 LQKAG 333
Cdd:PRK08963 319 LERAG 323
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
37-333 |
3.24e-50 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 173.66 E-value: 3.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 37 DVVVVHGRRTPIGRAgRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPL 116
Cdd:PRK08170 4 PVYIVDGARTPFLKA-RGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT-----LSERG--------NPGNISSRLLENEKAR-DCLIP-- 180
Cdd:PRK08170 83 WTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMShapllFSEKMvrwlagwyAAKSIGQKLAALGKLRpSYLAPvi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 181 --------------MGITSENVAERFGISRQKQDAFALASQQKAASAQSKGcFRAEIVPVTttvlddkgDRKTITVSQDE 246
Cdd:PRK08170 163 gllrgltdpvvglnMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEG-RLKEVVPLF--------DRDGKFYDHDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 247 GVRPSTTMEGLAKLKPAF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAI 325
Cdd:PRK08170 234 GVRPDSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAA 313
|
....*...
gi 1958797581 326 PAALQKAG 333
Cdd:PRK08170 314 TPLLQRHG 321
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
37-333 |
2.33e-47 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 165.18 E-value: 2.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 37 DVVVVHGRRTPIGRAGRGGFKDTTPdELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPL 116
Cdd:PRK06366 3 DVYIVSAKRTAIGKFGRSFSKIKAP-QLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSE-------RGNPGNIssrLLENEKARDCLIP--------- 180
Cdd:PRK06366 82 YTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPfllpsdlRWGPKHL---LHKNYKIDDAMLVdglidafyf 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 181 --MGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttvlddkgdrktiTVSQDEGVRpSTTMEGLA 258
Cdd:PRK06366 159 ehMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN-------------DLDRDEGIR-KTTMEDLA 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 259 KLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06366 225 KLPPAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQN 299
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
40-333 |
1.93e-44 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 157.58 E-value: 1.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 40 VVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGA-AMARIAQFLSGIPETVPLSA 118
Cdd:PRK06504 6 IVAAARTAGGRKG-GRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQAtNVARNAVLASKLPESVPGTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNP---------GNISSRLLEnEKARDCLIPMGITSENVA 189
Cdd:PRK06504 85 IDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPstlpaknglGHYKSPGME-ERYPGIQFSQFTGAEMMA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 190 ERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDRKTItvsqDEGVRPSTTMEGLAKLKPaFKDGGS 269
Cdd:PRK06504 164 KKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTV----DEGIRFDATLEGIAGVKL-IAEGGR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958797581 270 TTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06504 239 LTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAG 302
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
39-325 |
1.37e-42 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 151.84 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 39 VVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVklkPECLGDISVGNVLqpGAGAAMARIAQFLSGIPETVPLSA 118
Cdd:PRK06690 4 VIVEAKRTPIGKKN-GMLKDYEVQQLAAPLLTFLSKGM---EREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKardclipMGITSENVAERFGISRQK 198
Cdd:PRK06690 78 IDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSPETIGDPD-------MGVAAEYVAERYNITREM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 199 QDAFALASQQKAASAQSKGCFRAEIVPVTTTVlddkgdrktitvsqDEGVRPSTTMEGL-AKLKPAFKDGGSTTAGNSSQ 277
Cdd:PRK06690 151 QDEYACLSYKRTLQALEKGYIHEEILSFNGLL--------------DESIKKEMNYERIiKRTKPAFLHNGTVTAGNSCG 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958797581 278 VSDGAAAVLLARRSKAEELGL-PILGVLRSyAVVGVPPDIMGIGPAYAI 325
Cdd:PRK06690 217 VNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAV 264
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
38-333 |
4.70e-42 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 151.58 E-value: 4.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 38 VVVVHGRRTPIGrAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLS 117
Cdd:PRK06954 9 IVIASAARTPMA-AFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 118 AVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSE----------RGNPGNISSRLLEN--EKARDCLIPMGITS 185
Cdd:PRK06954 88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPyllpkarggmRMGHGQVLDHMFLDglEDAYDKGRLMGTFA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVttTVLDDKGDrktITVSQDEGVRpSTTMEGLAKLKPAFK 265
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPV--TVAGKKGD---TVIDRDEQPF-KANPEKIPTLKPAFS 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958797581 266 DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06954 242 KTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNG 309
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
36-333 |
1.62e-41 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 149.47 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAA-MARIAQFLSGIPETV 114
Cdd:PRK07801 2 AEAYIVDAVRTPVGKRK-GGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGnIARTSWLAAGLPEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 115 PLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTL----------SERGNPGNISSRLLENEKARDCLIPMGIT 184
Cdd:PRK07801 81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQipissamtagEQLGFTSPFAESKGWLHRYGDQEVSQFRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 185 SENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVtttvlddkGDrktitVSQDEGVRpSTTMEGLAKLKPaF 264
Cdd:PRK07801 161 AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV--------GG-----VTVDEGPR-ETSLEKMAGLKP-L 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958797581 265 KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK07801 226 VEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTG 294
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
31-333 |
1.58e-37 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 140.04 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 31 PQASASDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGI 110
Cdd:PRK09268 2 TMPTVRRVAILGGNRIPFARSN-GAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 111 PETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVES-----MTLSE-----------------------RGNPG 162
Cdd:PRK09268 81 SPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTtsdapIAVNEglrkillelnrakttgdrlkalgKLRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 163 NISSRLLENEKARDCLiPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVtttvlddKGdrktitV 242
Cdd:PRK09268 161 HLAPEIPRNGEPRTGL-SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-------LG------L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 243 SQDEGVRPSTTMEGLAKLKPAF--KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVP----PDI 316
Cdd:PRK09268 227 TRDNNLRPDSSLEKLAKLKPVFgkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhgKEG 306
|
330
....*....|....*..
gi 1958797581 317 MGIGPAYAIPAALQKAG 333
Cdd:PRK09268 307 LLMAPAYAVPRLLARNG 323
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
36-333 |
2.16e-35 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 133.75 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 36 SDVVVVHGRRTP--IGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPE 112
Cdd:PRK06025 2 AEAYIIDAVRTPrgIGKVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 113 TVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTL-----SERGNPGnISSRLLENEKAR-DCLIPM---GI 183
Cdd:PRK06025 82 KASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYtaamaAEDMAAG-KPPLGMGSGNLRlRALHPQshqGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 184 TSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVtttvLDDKGdrkTITVSQDEGVRPSTTMEGLAKLKPA 263
Cdd:PRK06025 161 CGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV----YRDDG---SVALDHEEFPRPQTTAEGLAALKPA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 264 FK--------DGGST------------------TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIM 317
Cdd:PRK06025 234 FTaiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLM 313
|
330
....*....|....*.
gi 1958797581 318 GIGPAYAIPAALQKAG 333
Cdd:PRK06025 314 LNAPVPAAKKVLAKAG 329
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
45-333 |
5.75e-29 |
|
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: 116.05 E-value: 5.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 45 RTPIGRAG--RGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSAVNRQ 122
Cdd:cd00826 5 MTAFGKFGgeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 123 CSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPgnissrlleNEKARDCLIpmgitsenvaERFGiSRQKQDAF 202
Cdd:cd00826 85 CGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNA---------KEKHIDVLI----------NKYG-MRACPDAF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 203 ALASQQKAASAQSKGCFRAEIVPVTTtvlddKGDRKTITVSQDEGVR--PSTTMEGLAKLKPAFKDGGSTTAGNSSQVSD 280
Cdd:cd00826 145 ALAGQAGAEAAEKDGRFKDEFAKFGV-----KGRKGDIHSDADEYIQfgDEASLDEIAKLRPAFDKEDFLTAGNACGLND 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958797581 281 GAAAVLLARRSKAEELGLPI-------LGVLRSYAVVGVPPD----IMGIGPAYAIPAALQKAG 333
Cdd:cd00826 220 GAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAG 283
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
298-333 |
6.62e-12 |
|
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: 61.89 E-value: 6.62e-12
10 20 30
....*....|....*....|....*....|....*.
gi 1958797581 298 LPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAG 36
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
46-333 |
4.81e-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: 54.19 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 46 TPIGRAGrggfkDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVL-QPGAGAAMARIAQFLSGIPetVPLSAVNRQCS 124
Cdd:cd00829 6 TPFGRRS-----DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAgGRFQSFPGALIAEYLGLLG--KPATRVEAAGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 125 SGLQAVANIAGGIRNGSYDIGMACGVESMtlSERGNPGNISSRLLENEKARDcLIPMGITSENVA--------ERFGISR 196
Cdd:cd00829 79 SGSAAVRAAAAAIASGLADVVLVVGAEKM--SDVPTGDEAGGRASDLEWEGP-EPPGGLTPPALYalaarrymHRYGTTR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 197 qkqDAFAL--ASQQKAASAQSKGCFRAEivpvtttvlddkgdrktITVSQDEGVRPSTTmeglaklkPafkdggsTTAGN 274
Cdd:cd00829 156 ---EDLAKvaVKNHRNAARNPYAQFRKP-----------------ITVEDVLNSRMIAD--------P-------LRLLD 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 275 SSQVSDGAAAVLLARRSKAEELGLP---ILGV---LRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:cd00829 201 CCPVSDGAAAVVLASEERARELTDRpvwILGVgaaSDTPSLSERDDFLSLDAARLAARRAYKMAG 265
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
63-297 |
2.51e-03 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 39.67 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 63 ELLSAVLTAVLQDVKLKPECLGDISVGNVlqpgAGAAMARIAQfLSGIPETV-------PLSAVNRQCSSGLQAVANIAG 135
Cdd:PRK06289 28 DLTREVVDGTLAAAGVDADDIEVVHVGNF----FGELFAGQGH-LGAMPATVhpalwgvPASRHEAACASGSVATLAAMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 136 GIRNGSYDIGMACGVESM-TLSERGNPGNISSRLLENEKARDCLIP----MGITSENVAERFGISRQKQDAFA---LASQ 207
Cdd:PRK06289 103 DLRAGRYDVALVVGVELMkTVPGDVAAEHLGAAAWTGHEGQDARFPwpsmFARVADEYDRRYGLDEEHLRAIAeinFANA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 208 QKAASAQSKGCFraeiVPVTTTVLDDkgdrktitvsqdegvrpsttmeglaKLKPAFkdGGSTTAGNSSQVSDGAAAVLL 287
Cdd:PRK06289 183 RRNPNAQTRGWA----FPDEATNDDD-------------------------ATNPVV--EGRLRRQDCSQVTDGGAGVVL 231
|
250
....*....|
gi 1958797581 288 ARRSKAEELG 297
Cdd:PRK06289 232 ASDAYLRDYA 241
|
|
|