|
Name |
Accession |
Description |
Interval |
E-value |
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
43-426 |
0e+00 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 546.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 43 VIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTI 122
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 123 NKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY-GGVKLEDLIVKDGLTDVYNKIHMGSCAENTA 201
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 202 KKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPdVVVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTA 280
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 281 ANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVV 360
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557237 361 LANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 426
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
40-427 |
0e+00 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 520.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 40 KEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPC 119
Cdd:COG0183 2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 120 TTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGG-VKLEDLIVKDGLTDVYNKIHMGSCAE 198
Cdd:COG0183 82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 199 NTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQpDVVVKEDEEYKR-VDFSKVPKLKTVFqKENGT 277
Cdd:COG0183 162 NVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKG-EVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 278 VTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFS 357
Cdd:COG0183 240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557237 358 LVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 427
Cdd:COG0183 320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
40-427 |
0e+00 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 518.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 40 KEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPC 119
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 120 TTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCA 197
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 198 ENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV-KGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENG 276
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 277 TVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAF 356
Cdd:PLN02644 241 SVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557237 357 SLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 427
Cdd:PLN02644 321 SVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
40-424 |
4.19e-168 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 476.95 E-value: 4.19e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 40 KEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPC 119
Cdd:PRK05790 2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 120 TTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN--RGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCA 197
Cdd:PRK05790 82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPgsRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 198 ENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDeEYKRVDFS--KVPKLKTVFqKEN 275
Cdd:PRK05790 162 ENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTD-EHPRPDTTaeSLAKLRPAF-DKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 276 GTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEA 355
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557237 356 FSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLI 424
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKrrGAKKGLATLCIGGGQGVALIV 390
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
44-425 |
3.24e-162 |
|
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: 461.70 E-value: 3.24e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 44 IVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTIN 123
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 124 KVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTP---YGGVKLEDLIVKDgLTDVYNKIHMGSCAENT 200
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 201 AKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTA 280
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 281 ANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVV 360
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557237 361 LANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 425
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
39-425 |
9.11e-153 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 437.99 E-value: 9.11e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTP 118
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 119 CTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY--GGVKLEDLIVKDGLTDVYNKIHMGSC 196
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYrmGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 197 AENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVT-VKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKEn 275
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPqRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKT- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 276 GTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEA 355
Cdd:PRK08235 240 GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557237 356 FSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 425
Cdd:PRK08235 320 FAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrgGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
41-425 |
1.61e-125 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 368.84 E-value: 1.61e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 41 EVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCT 120
Cdd:PRK06954 8 PIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 121 TINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKDGLTDVYNKIH-MGSCA 197
Cdd:PRK06954 88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpkARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 198 ENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQpDVVVKEDEEYKRVDFSKVPKLKTVFQKeNGT 277
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKG-DTVIDRDEQPFKANPEKIPTLKPAFSK-TGT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 278 VTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFS 357
Cdd:PRK06954 246 VTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFA 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 358 LVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 425
Cdd:PRK06954 326 VVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRArgGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
40-427 |
7.05e-117 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 346.56 E-value: 7.05e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 40 KEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLqggegqaPT--------RQAVLGA 111
Cdd:PRK09051 3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVI-------PTeprdmylsRVAAINA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 112 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKdGLTDVYN 189
Cdd:PRK09051 76 GVPQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpaARWGARMGDAKLVDMMVG-ALHDPFG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 190 KIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV-TVKGqpDVVVKEDEEYKR-VDFSKVPKL 267
Cdd:PRK09051 155 TIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIkTRKG--EVVFDTDEHVRAdTTLEDLAKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 268 KTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDI 347
Cdd:PRK09051 233 KPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 348 AMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLIQ 425
Cdd:PRK09051 313 DVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQriGGRYALVTMCIGGGQGIAAIFE 392
|
..
gi 4557237 426 KL 427
Cdd:PRK09051 393 RL 394
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
42-299 |
7.90e-117 |
|
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: 341.59 E-value: 7.90e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 42 VVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTT 121
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 122 INKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN---RGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAE 198
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 199 NTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKEnGTV 278
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTV 239
|
250 260
....*....|....*....|.
gi 4557237 279 TAANASTLNDGAAALVLMTAD 299
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
39-426 |
1.61e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 333.01 E-value: 1.61e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTP 118
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 119 CTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSC 196
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLpgARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 197 AENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV-TVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKEn 275
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIpQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 276 GTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEA 355
Cdd:PRK05656 240 GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557237 356 FSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQK 426
Cdd:PRK05656 320 FAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMirRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
39-425 |
7.87e-104 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 313.51 E-value: 7.87e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTP 118
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 119 CTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS---NVPYVmnRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGS 195
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI--RAGAKFGDIKMVDLMQYDGLTDVFSGVFMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 196 CAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKeN 275
Cdd:PRK06633 160 TAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDK-N 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 276 GTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEA 355
Cdd:PRK06633 239 GVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557237 356 FSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLIQ 425
Cdd:PRK06633 319 FAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRraKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
39-427 |
6.22e-102 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 308.81 E-value: 6.22e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEK-AGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPIS 116
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 117 TPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYG-GVKLEDL-----IVKDGLTDVYNK 190
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSrQAEIFDTtigwrFVNPLMKAQYGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 191 IHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEeYKRVDFS--KVPKLK 268
Cdd:PRK09050 161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDE-HPRPETTleALAKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 269 TVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIA 348
Cdd:PRK09050 240 PVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 349 MWEVNEAFSLVVLANIKMLEI--DPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLI 424
Cdd:PRK09050 319 VIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTMCIGVGQGIALAI 398
|
...
gi 4557237 425 QKL 427
Cdd:PRK09050 399 ERV 401
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
39-425 |
5.98e-101 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 305.78 E-value: 5.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTP 118
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 119 CTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNR------GSTPYGGVKLEDLIVKDGLTDVYNKIH 192
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSdlrwgpKHLLHKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 193 MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkgqpdvVVKEDEEYKRVDFSKVPKLKTVFQ 272
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------DLDRDEGIRKTTMEDLAKLPPAFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 273 KeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEV 352
Cdd:PRK06366 232 K-NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEH 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557237 353 NEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQG--EYGLASICNGGGGASAMLIQ 425
Cdd:PRK06366 311 NEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRhmKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
39-417 |
3.65e-99 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 301.91 E-value: 3.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTP 118
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 119 CTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN--RGSTPYGGVKLEDLIVKDGLT---DVYNKIH- 192
Cdd:PRK06205 81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQLHDRLARGRETaggRRFPVPGg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 193 MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYkRVDFS--KVPKLKTV 270
Cdd:PRK06205 161 MIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHP-RADTTleSLAKLRPI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 271 FQK--ENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIA 348
Cdd:PRK06205 240 MGKqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDID 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4557237 349 MWEVNEAFSLVVLANIKMLEIDPQ---KVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGG 417
Cdd:PRK06205 320 LIELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQrrQARYGLETMCIGGG 393
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
39-427 |
8.48e-89 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 274.72 E-value: 8.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIG-SFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVL-QGGEGQAPTRQAVLGAGLPIS 116
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANpEGATGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 117 TPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGstpyggvKLEDLIVKDGLTDVYnkIHMGSC 196
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRH-------MLREGWLVEHKPEIY--WSMLQT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 197 AENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQ---------PDVVVKEDEEYkRVDFSK--VP 265
Cdd:PRK07108 152 AENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVAdkatgrlftKEVTVSADEGI-RPDTTLegVS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 266 KLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKE 345
Cdd:PRK07108 231 KIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 346 DIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGhltHALKQGE-----YGLASICNGGGGAS 420
Cdd:PRK07108 309 DIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTG---HALIEGKrrgakYVVVTMCIGGGQGA 385
|
....*..
gi 4557237 421 AMLIQKL 427
Cdd:PRK07108 386 AGLFEVL 392
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
39-426 |
1.35e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 271.98 E-value: 1.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIGSFLGS------LSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQA-PTRQAVLGA 111
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPIFLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 112 GLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNki 191
Cdd:PRK06445 81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNPKLLTDPKYIEYDLTTGYV-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 192 hMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVF 271
Cdd:PRK06445 159 -MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLPPAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 272 qKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWE 351
Cdd:PRK06445 238 -KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557237 352 VNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQK 426
Cdd:PRK06445 317 INEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLqiKGKDYGVATLCVGGGQGGAVVLER 393
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
39-427 |
1.72e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 263.49 E-value: 1.72e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGeGQAP--TRQAVLGAGLPIS 116
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQAGniARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 117 TPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP--YVMNRG-----STPYGGVKledlivkdGLTDVYN 189
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPisSAMTAGeqlgfTSPFAESK--------GWLHRYG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 190 K--IHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkgqpDVVVkeDEEYKRVDFSKVPKL 267
Cdd:PRK07801 152 DqeVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG-------GVTV--DEGPRETSLEKMAGL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 268 KTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDI 347
Cdd:PRK07801 223 KPLV--EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 348 AMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 425
Cdd:PRK07801 301 DVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERtgGRYGLQTMCEGGGTANVTIIE 380
|
..
gi 4557237 426 KL 427
Cdd:PRK07801 381 RL 382
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
41-427 |
3.78e-83 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 260.71 E-value: 3.78e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 41 EVVIVSATRTPIG-SFLGSLSLLPATKLGSIAIQGAIEKA-GIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPiST 117
Cdd:PRK07851 3 EAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYD-FL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 118 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNvpYVM-NRGSTP-------------------YGGVKLED 177
Cdd:PRK07851 82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSR--FAKgNSDSLPdtknplfaeaqartaaraeGGAEAWHD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 178 LIVKDGLTDVYnkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvkgqPD--VVVKEDEE 255
Cdd:PRK07851 160 PREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL-----PDgtVVSTDDGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 256 YKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASM 335
Cdd:PRK07851 233 RAGTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 336 VLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASIC 413
Cdd:PRK07851 312 ALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQthDKTFGLETMC 391
|
410
....*....|....
gi 4557237 414 NGGGGASAMLIQKL 427
Cdd:PRK07851 392 VGGGQGMAMVLERL 405
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
39-427 |
2.95e-82 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 258.01 E-value: 2.95e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIG-SFLGSLSLLPATKLGSIAIQGAIEKA-GIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPI 115
Cdd:PRK09052 5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEqGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 116 STPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGS-TPYGGVKLEDLIVKDGltdvynkihMG 194
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSmSPAIFARDENVGIAYG---------MG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 195 SCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKgQPD-----VVVKEDE----EYKRVDFS--K 263
Cdd:PRK09052 156 LTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITER-FPDlatgeVDVKTRTvdldEGPRADTSleG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 264 VPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLK 343
Cdd:PRK09052 235 LAKLKPVFANK-GSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 344 KEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASA 421
Cdd:PRK09052 314 QDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMVTMCVGTGMGAA 393
|
....*.
gi 4557237 422 MLIQKL 427
Cdd:PRK09052 394 GIFERL 399
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
39-421 |
6.93e-81 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 254.29 E-value: 6.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 39 LKEVVIVSATRTPIG-SFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPIS 116
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEqGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 117 TPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVmnrgstpyGGVKLEDLIVKDGLTDVYnkIHMGSC 196
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--------GHVVRPNPRLVEAAPEYY--MGMGHT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 197 AENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV-------KGQPDVVVKEDEEYKRVDFSK--VPKL 267
Cdd:PRK07661 151 AEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLrtvgennKLQEETITFSQDEGVRADTTLeiLGKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 268 KTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDI 347
Cdd:PRK07661 231 RPAFNV-KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDI 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557237 348 AMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK-QGE-YGLASICNGGGGASA 421
Cdd:PRK07661 310 GLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKrRNEqFGIVTMCIGGGMGAA 385
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
44-426 |
8.71e-81 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 254.32 E-value: 8.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 44 IVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPISTPCTTI 122
Cdd:PRK08131 6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 123 NKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGgvklEDLIVKDG----------LTDVYNKIH 192
Cdd:PRK08131 86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFS----RDAKVFDTtigarfpnpkIVAQYGNDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 193 MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV-TVKGQPDVVVKEDEEYK-RVDFSKVPKLKTV 270
Cdd:PRK08131 162 MPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVpQGRKLPPKLVAEDEHPRpSSTVEALTKLKPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 271 FqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMW 350
Cdd:PRK08131 242 F--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDII 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 351 EVNEAFSLVVLANIKMLEI--DPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLIQK 426
Cdd:PRK08131 320 EINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQrrGKRYAVVSLCIGVGQGLAMVIER 399
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
41-427 |
9.67e-81 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 253.88 E-value: 9.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 41 EVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPISTPC 119
Cdd:PRK07850 3 NPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 120 TTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyGGVKLEDLIVkdgltDVYNKIhmgSCAEN 199
Cdd:PRK07850 83 TTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGR-GLPRPDSWDI-----DMPNQF---EAAER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 200 TAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV---KGQP---DVVVKEDEEYKRVDFSKVPKLKTVFqk 273
Cdd:PRK07850 154 IAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVldeEGQPtgeTRLVTRDQGLRDTTMEGLAGLKPVL-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 274 ENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVN 353
Cdd:PRK07850 232 EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEIN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557237 354 EAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 427
Cdd:PRK07850 312 EAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERtdKSTALITMCAGGALSTGTIIERI 387
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
41-427 |
5.21e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 251.96 E-value: 5.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 41 EVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEgQAPT--RQAVLGAGLPISTP 118
Cdd:PRK06504 3 EAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGE-QATNvaRNAVLASKLPESVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 119 CTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMNRGSTpyggvkledLIVKDGLTDV--------YNK 190
Cdd:PRK06504 82 GTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP--MGSPST---------LPAKNGLGHYkspgmeerYPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 191 IH----MGscAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYkRVDFS--KV 264
Cdd:PRK06504 151 IQfsqfTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGI-RFDATleGI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 265 PKLKTVfqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKK 344
Cdd:PRK06504 228 AGVKLI--AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 345 EDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAM 422
Cdd:PRK06504 306 DDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQrgKRYGLQTMCEGGGMANVT 385
|
....*
gi 4557237 423 LIQKL 427
Cdd:PRK06504 386 IVERL 390
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
42-425 |
8.95e-78 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 247.59 E-value: 8.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 42 VVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTT 121
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 122 INKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP-----------YVMNRGST------PYGGVKLEDLI-VKDG 183
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaralVDLNKARTlgqrlkLFSRLRLRDLLpVPPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 184 LTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQP---DVVVKEDEeykrvD 260
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPleeDNNIRGDS-----T 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 261 FSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPI-DFPIAPVYAASMVLKD 339
Cdd:PRK08963 242 LEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWqDMLLGPAYATPLALER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 340 VGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL 402
Cdd:PRK08963 322 AGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHEL 401
|
410 420
....*....|....*....|....*
gi 4557237 403 KQ--GEYGLASICNGGGGASAMLIQ 425
Cdd:PRK08963 402 RRrgGGLGLTTACAAGGLGAAMVLE 426
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
40-427 |
2.89e-77 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 244.87 E-value: 2.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 40 KEVVIVSATRTPIG-SFLGSLSLLPATKLGSIAIQGAIEK-AGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPIS 116
Cdd:PRK08947 2 EDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLEqGFNIARNAALLAGIPHS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 117 TPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMNRGSTPYggvkledlivkDGLTDVYNKIH--MG 194
Cdd:PRK08947 82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--MNHGVDFH-----------PGLSKNVAKAAgmMG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 195 SCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkGQpdvvvKEDEEYKRVDFSKV---------- 264
Cdd:PRK08947 149 LTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTE----GH-----DADGVLKLFDYDEVirpettveal 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 265 PKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKK 344
Cdd:PRK08947 220 AALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 345 EDIAMWEVNEAF---SLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGA 419
Cdd:PRK08947 300 SDIDVFELNEAFaaqSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERkdAQFGLATMCIGLGQG 379
|
....*...
gi 4557237 420 SAMLIQKL 427
Cdd:PRK08947 380 IATVFERV 387
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
41-423 |
4.42e-77 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 246.60 E-value: 4.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 41 EVVIVSATRTPI-GSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQA-PTRQAVLGAGLPISTP 118
Cdd:PLN02287 47 DVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnECRMAAFYAGFPETVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 119 CTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyggvKLEDL-IVKDGLtdvynkIHMGSCA 197
Cdd:PLN02287 127 VRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNP----RVESFsQAQDCL------LPMGITS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 198 ENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV------TVKGQPDVVVKEDEEYKRVDFSKVPKLKTVF 271
Cdd:PLN02287 197 ENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTkivdpkTGEEKPIVISVDDGIRPNTTLADLAKLKPVF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 272 qKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWE 351
Cdd:PLN02287 277 -KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFE 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557237 352 VNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ----GEYGLASICNGGG-GASAML 423
Cdd:PLN02287 356 INEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgkdCRFGVVSMCIGTGmGAAAVF 432
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
40-427 |
8.80e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 242.23 E-value: 8.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 40 KEVVIVSATRTP-------IGSFLGSlsllpatklgSIAIQgaiekAGIP--------KEEVKEAYMGNVLQGGEGQAPT 104
Cdd:PRK08170 3 RPVYIVDGARTPflkarggPGPFSAS----------DLAVA-----AGRAllnrqpfaPDDLDEVILGCAMPSPDEANIA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 105 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY---------GGVKL 175
Cdd:PRK08170 68 RVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWlagwyaaksIGQKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 176 EDL-------------IVKdGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGnEVIPVtVTV 242
Cdd:PRK08170 148 AALgklrpsylapvigLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL-FDR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 243 KGQpdvvVKEDEEYKRVDFS--KVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAV 320
Cdd:PRK08170 225 DGK----FYDHDDGVRPDSSmeKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 321 EPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EIDPQKVNINGGAVSL 383
Cdd:PRK08170 301 DPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWadeeycreqlgldgalgELDRERLNVDGGAIAL 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 4557237 384 GHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 427
Cdd:PRK08170 381 GHPVGASGARIVLHLLHALKRrgTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
41-427 |
8.49e-72 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 231.31 E-value: 8.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 41 EVVIVSATRTPIGSFL--GSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPIST 117
Cdd:PRK08242 3 EAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDqGADIARTAVLAAGLPETV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 118 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyggvkledliVKDGLTDVYNKIHMGSCA 197
Cdd:PRK08242 83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWA----------MDPSTNFPTYFVPQGISA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 198 ENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVtvtvKGQPDVVVKEDEEYKR--VDFSKVPKLKTVFQ--- 272
Cdd:PRK08242 153 DLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV----KDQNGLTILDHDEHMRpgTTMESLAKLKPSFAmmg 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 273 -----------------KENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASM 335
Cdd:PRK08242 229 emggfdavalqkypeveRINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 336 VLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASIC 413
Cdd:PRK08242 309 ALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELerRGKRTALITLC 388
|
410
....*....|....
gi 4557237 414 NGGGGASAMLIQKL 427
Cdd:PRK08242 389 VGGGMGIATIIERV 402
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
41-427 |
4.02e-66 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 215.40 E-value: 4.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 41 EVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQgaIEKAGIPkEEVKEAYMGNVLQGGEGQAptRQAVLGAGLPISTPCT 120
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLT--FLSKGME-REIDDVILGNVVGPGGNVA--RLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 121 TINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyggvkledlivkdgltDVYNKIHMGSCAENT 200
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSP----------------ETIGDPDMGVAAEYV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 201 AKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkGQPDVVVKEDEEYKRVdfskVPKLKTVFQKeNGTVTA 280
Cdd:PRK06690 141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN----GLLDESIKKEMNYERI----IKRTKPAFLH-NGTVTA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 281 ANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVV 360
Cdd:PRK06690 212 GNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKV 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557237 361 LANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 427
Cdd:PRK06690 292 VACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKRedMKYGIATLGIGGGIGLALLFEKV 360
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
41-427 |
1.28e-58 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 197.31 E-value: 1.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 41 EVVIVSATRTP--IGSF-LGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQ-GGEGQAPTRQAVLGAGLPIS 116
Cdd:PRK06025 3 EAYIIDAVRTPrgIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQrGKQGGDLGRMAALDAGYDIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 117 TPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS----NVPYVMNRGSTPYGgvkledliVKDG---LTDVYN 189
Cdd:PRK06025 83 ASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaaMAAEDMAAGKPPLG--------MGSGnlrLRALHP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 190 KIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkgQPDVVVKED-EEYKRVDFSK--VPK 266
Cdd:PRK06025 155 QSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY-----RDDGSVALDhEEFPRPQTTAegLAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 267 LKTVFQK-------ENGTV------------------TAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVE 321
Cdd:PRK06025 230 LKPAFTAiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 322 PIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHA 401
Cdd:PRK06025 310 PTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDE 389
|
410 420
....*....|....*....|....*...
gi 4557237 402 LKQ--GEYGLASICNGGGGASAMLIQKL 427
Cdd:PRK06025 390 LERrgLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
306-426 |
2.21e-58 |
|
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: 187.08 E-value: 2.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 306 VTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGH 385
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 4557237 386 PIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 426
Cdd:pfam02803 81 PLGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
45-425 |
3.60e-53 |
|
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: 182.31 E-value: 3.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 45 VSATRTPIGSFLGSLSLL---PATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTT 121
Cdd:cd00826 1 AGAAMTAFGKFGGENGADandLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 122 INKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvmnrgstpyggvklEDLIVKDGLTDVYNKIHMgscaenta 201
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSA---------------ENNAKEKHIDVLINKYGM-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 202 kklniaRNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvKGQPDVVVKEDEEYKR----VDFSKVPKLKTVFQKEnGT 277
Cdd:cd00826 138 ------RACPDAFALAGQAGAEAAEKDGRFKDEFAKFGV--KGRKGDIHSDADEYIQfgdeASLDEIAKLRPAFDKE-DF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 278 VTAANASTLNDGAAALVLMTADAA-------KRLNVTPLARIVAFADAAVEPIDFPIA----PVYAASMVLKDVGLKKED 346
Cdd:cd00826 209 LTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVggdgPIEAARKALEKAGLGIGD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 347 IAMWEVNEAFSLVVLANIKMLEIDPQK------------------VNINGGAVSLGHPIGMSGARIVGHLTHALKQGEY- 407
Cdd:cd00826 289 LDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGk 368
|
410 420
....*....|....*....|....
gi 4557237 408 ------GLASICNGGGGASAMLIQ 425
Cdd:cd00826 369 rqgagaGLALLCIGGGGGAAMCIE 392
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
37-426 |
1.94e-49 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 173.16 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 37 PTLKEVVIVSATRTPIG------SFLGSLSLLPAtklgsiAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLG 110
Cdd:PRK09268 4 PTVRRVAILGGNRIPFArsngayADASNQDMLTA------ALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 111 AGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYV-----------MNRGSTPYGGVKL---- 175
Cdd:PRK09268 78 SALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAvneglrkilleLNRAKTTGDRLKAlgkl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 176 --EDLIV--------KDGLTdvynkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQ 245
Cdd:PRK09268 158 rpKHLAPeiprngepRTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTRDN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 246 ---PDVVVKedeeykrvdfsKVPKLKTVFQK-ENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVE 321
Cdd:PRK09268 231 nlrPDSSLE-----------KLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 322 PIDFP----IAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLE-----------------IDPQKVNINGGA 380
Cdd:PRK09268 300 FVHGKegllMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEdeeycrerlgldaplgsIDRSKLNVNGSS 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 4557237 381 VSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQK 426
Cdd:PRK09268 380 LAAGHPFAATGGRIVATLAKLLaeKGSGRGLISICAAGGQGVTAILER 427
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
71-421 |
2.16e-17 |
|
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: 83.08 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 71 AIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPIsTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVA 150
Cdd:cd00829 23 AARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIASGLADVVLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 151 GGMESMSNVPYVMNRGSTPyGGVKLEDLIVKDGLT--DVYNKI---HM---GSCAENTAKklnIARNEQDAYAINSYtrs 222
Cdd:cd00829 102 VGAEKMSDVPTGDEAGGRA-SDLEWEGPEPPGGLTppALYALAarrYMhryGTTREDLAK---VAVKNHRNAARNPY--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 223 kaAWEAGkfgneviPVTV-TVKGQPDVVvkedEEYKRVDFSKVpklktvfqkengtvtaanastlNDGAAALVLMTADAA 301
Cdd:cd00829 175 --AQFRK-------PITVeDVLNSRMIA----DPLRLLDCCPV----------------------SDGAAAVVLASEERA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 302 KRLNVTPlARIVAFADA-------AVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML------- 367
Cdd:cd00829 220 RELTDRP-VWILGVGAAsdtpslsERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLgfcekge 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557237 368 --------EIDPQ---KVNINGGAVSLGHPIGMSGARIVGHLTHALKqGEYG--------LASICNGGGGASA 421
Cdd:cd00829 299 ggklvregDTAIGgdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLR-GEAGarqvpgarVGLAHNIGGTGSA 370
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
64-424 |
1.91e-14 |
|
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: 72.86 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 64 ATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPiSTPCTTINKVCASGMKAIMMASQSLMCG 143
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 144 HQDVMVAGGMESmsnvpyvmnrgstpyggvkledlivkdgltdvynkihmgscaentakklniarneqdayainsytrsk 223
Cdd:cd00327 86 KADIVLAGGSEE-------------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 224 aaweagkfgnevipvtvtvkgqpdvvvkedeeykrvdfskvpklktvfqkengtvtaanaSTLNDGAAALVLMTADAAKR 303
Cdd:cd00327 98 ------------------------------------------------------------FVFGDGAAAAVVESEEHALR 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 304 LNVTPLARIVAFADAAVEPIDFPI----APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKV---NI 376
Cdd:cd00327 118 RGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspAV 197
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 4557237 377 NGGAVSLGHPIGMSGARIVGHLTHALKQGEY---------GLASICNGGGGASAMLI 424
Cdd:cd00327 198 SATLIMTGHPLGAAGLAILDELLLMLEHEFIpptpreprtVLLLGFGLGGTNAAVVL 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
71-421 |
5.22e-13 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 69.93 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 71 AIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLG--AGLPiSTPCTTINKVCASGMKAIMMASQSLMCGHQDVM 148
Cdd:PRK06064 29 AGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIAALIAdyAGLA-PIPATRVEAACASGGAALRQAYLAVASGEADVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 149 VAGGMESMSNVP---------------YVMNRGSTPyggvkledlivkDGLTDVYNKIHM---GSCAENTAKklnIARNE 210
Cdd:PRK06064 108 LAAGVEKMTDVPtpdateaiaragdyeWEEFFGATF------------PGLYALIARRYMhkyGTTEEDLAL---VAVKN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 211 QDAYAINSYtrskaaweaGKFGNEvipVTVtvkgqpDVVVKEdeeykrvdfSKVPKLKTVFqkengtvtaaNASTLNDGA 290
Cdd:PRK06064 173 HYNGSKNPY---------AQFQKE---ITV------EQVLNS---------PPVADPLKLL----------DCSPITDGA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 291 AALVLMTADAAKRLNVTPLaRIVAFADAavepIDFPI-----------APVYAASMVLKDVGLKKEDIAMWEVNEAFSLV 359
Cdd:PRK06064 216 AAVILASEEKAKEYTDTPV-WIKASGQA----SDTIAlhdrkdfttldAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 360 VLANIKML-----------------EIDPQ-KVNINGGAVSLGHPIGMSGARIVGHLTHALKQG-----------EYGLA 410
Cdd:PRK06064 291 EILAYEDLgfakkgeggklaregqtYIGGDiPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEaekgrqqvigaGYGLT 370
|
410
....*....|..
gi 4557237 411 SicN-GGGGASA 421
Cdd:PRK06064 371 H--NvGGTGHTA 380
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
71-407 |
1.72e-08 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 56.23 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 71 AIQGAIEKAGIPKEEVKEAYMGNVLqggeGQAPTRQAVLGaGLPIS-------TPCTTINKVCASGMKAIMMASQSLMCG 143
Cdd:PRK06289 33 VVDGTLAAAGVDADDIEVVHVGNFF----GELFAGQGHLG-AMPATvhpalwgVPASRHEAACASGSVATLAAMADLRAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 144 HQDVMVAGGMESMSNVP---YVMNRGSTPYGGVKLEDL-----IVKDGLTDVYNK------IHMGSCAE-NTAkklNIAR 208
Cdd:PRK06289 108 RYDVALVVGVELMKTVPgdvAAEHLGAAAWTGHEGQDArfpwpSMFARVADEYDRrygldeEHLRAIAEiNFA---NARR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 209 NEqdayaiNSYTRSkaaWEAgkfgnevipvtvtvkgqPDVVVKEDEEYKRVDFSKVPKLktvfqkengtvtaaNASTLND 288
Cdd:PRK06289 185 NP------NAQTRG---WAF-----------------PDEATNDDDATNPVVEGRLRRQ--------------DCSQVTD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 289 GAAALVLMTADAAKRL-NVTPLARIVAF-------------ADAAVEPIDFPiaPVYAASM-VLKDVGLKKEDIAMWEVN 353
Cdd:PRK06289 225 GGAGVVLASDAYLRDYaDARPIPRIKGWghrtaplgleqklDRSAGDPYVLP--HVRQAVLdAYRRAGVGLDDLDGFEVH 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557237 354 EAFSLVVLANIKML---------------EIDP---QKVNINGGAVSLGHPIGMSGARIvghLTHALKQ-----GEY 407
Cdd:PRK06289 303 DCFTPSEYLAIDHIgltgpgeswkaiengEIAIggrLPINPSGGLIGGGHPVGASGVRM---LLDAAKQvtgtaGDY 376
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
71-395 |
2.80e-08 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 55.42 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 71 AIQGAIEKAGIPKEEVKEAYMGNVLQggegqaptRQAVLGAGLPIST-------PCTTINKVCASGMKAIMMASQSLMCG 143
Cdd:PRK06157 34 AFLEALADAGIEPKDIDAAWFGTHYD--------EIGSGKSGTPLSRalrlpniPVTRVENFCATGSEAFRGAVYAVASG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 144 HQDVMVAGGMESMSNVPY----VMNRGST-----PYG-----------------GVKLEDLivKDGLTDVYNKIHMgsca 197
Cdd:PRK06157 106 AYDIALALGVEKLKDTGYgglpVANPGTLadmtmPNVtapgnfaqlasayaakyGVSREDL--KRAMAHVSVKSHA---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 198 entakklNIARNEqdayainsytrsKAAWEAgkfgneviPVTV-TVKGQPDVVvkedeeykrvdfskvpklktvfqkenG 276
Cdd:PRK06157 180 -------NGARNP------------KAHLRK--------AVTEeQVLKAPMIA--------------------------G 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 277 TVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFAdAAVEP--------IDFPIAP--VYAASMVLKDVGLK--K 344
Cdd:PRK06157 207 PLGLFDCCGVSDGAAAAIVTTPEIARALGKKDPVYVKALQ-LAVSNgwelqyngWDGSYFPttRIAARKAYREAGITdpR 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557237 345 EDIAMWEVNEAFSLVVLANIKMLEIDPQ------------------KVNINGGAVSLGHPIGMSGARIV 395
Cdd:PRK06157 286 EELSMAEVHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
107-158 |
4.95e-06 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 48.30 E-value: 4.95e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 4557237 107 AVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSN 158
Cdd:cd00834 142 GQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
118-163 |
3.47e-05 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 45.86 E-value: 3.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 4557237 118 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNvPYVM 163
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT-PLGL 197
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
71-412 |
5.49e-05 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 45.27 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 71 AIQGAIEKAGIPKEE--VKEAYMGNVL------QGGEGQAPT-RQAVLGAGLP-ISTPCTTINKVCASGMKAIMMASQSL 140
Cdd:PTZ00455 55 AIQGTLENTGLDGKAalVDKVVVGNFLgelfssQGHLGPAAVgSLGQSGASNAlLYKPAMRVEGACASGGLAVQSAWEAL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 141 MCGHQDVMVAGGMEsmsnvpyVMNRGSTPYGG---VKLEDLIVKDGLTD-----VYNKiHMGSCAE-NTAKKLNIARNEQ 211
Cdd:PTZ00455 135 LAGTSDIALVVGVE-------VQTTVSARVGGdylARAADYRRQRKLDDftfpcLFAK-RMKYIQEhGHFTMEDTARVAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 212 DAYAiNSYTRSKAAWEAGKFGNEVIpvtvTVKGQPDVVVKEDEEYKrvdfskvPKLKTvfqkengtvtaANASTLNDGAA 291
Cdd:PTZ00455 207 KAYA-NGNKNPLAHMHTRKLSLEFC----TGASDKNPKFLGNETYK-------PFLRM-----------TDCSQVSDGGA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 292 ALVLMTADAAKRLNVTP----LARIVAFADAAVEPIDFP------IAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVL 361
Cdd:PTZ00455 264 GLVLASEEGLQKMGLSPndsrLVEIKSLACASGNLYEDPpdatrmFTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAEL 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557237 362 ANIKMLEI-DPQK-----------------VNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASI 412
Cdd:PTZ00455 344 LMYEALGIaEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGqcGEYQMKNI 414
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
118-155 |
7.15e-05 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 44.78 E-value: 7.15e-05
10 20 30
....*....|....*....|....*....|....*...
gi 4557237 118 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMES 155
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
75-171 |
1.93e-04 |
|
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: 42.62 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 75 AIEKAGIPKEEVKEAYMGnVLQG------GEGQAPTRQAVLGAGLPISTPCT-------------------TINKVCASG 129
Cdd:pfam00109 98 ALEDAGITPDSLDGSRTG-VFIGsgigdyAALLLLDEDGGPRRGSPFAVGTMpsviagrisyflglrgpsvTVDTACSSS 176
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 4557237 130 MKAIMMASQSLMCGHQDVMVAGGMESMSN----VPYVMNRGSTPYG 171
Cdd:pfam00109 177 LVAIHAAVQSIRSGEADVALAGGVNLLLTplgfAGFSAAGMLSPDG 222
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
71-408 |
2.29e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 43.30 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 71 AIQGAIEKAGIPKEEVKEAYMGNvlqggegqAPTRQAVLGAGLPISTPCTTINKV-------CASGMKAIMMASQSLMCG 143
Cdd:PRK12578 28 SIKEALNDAGVSQTDIELVVVGS--------TAYRGIELYPAPIVAEYSGLTGKVplrveamCATGLAASLTAYTAVASG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 144 HQDVMVAGGMESMSNVpyvmnrgstpyggvkledlivkdgltDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSK 223
Cdd:PRK12578 100 LVDMAIAVGVDKMTEV--------------------------DTSTSLAIGGRGGNYQWEYHFYGTTFPTYYALYATRHM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 224 AaweagKFG-NEVIPVTVTVKGQPDVVVKEDEEY-KRVDFSKVPKLKTVfqkeNGTVTAANASTLNDGAAALVLMTADAA 301
Cdd:PRK12578 154 A-----VYGtTEEQMALVSVKAHKYGAMNPKAHFqKPVTVEEVLKSRAI----SWPIKLLDSCPISDGSATAIFASEEKV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 302 KRLNV-TPL-------ARIVAFADAAVEPIDFPiAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML------ 367
Cdd:PRK12578 225 KELKIdSPVwitgigyANDYAYVARRGEWVGFK-ATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLgftekg 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 4557237 368 -------EIDPQK-----VNINGGAVSLGHPIGMSGARIVGHLTHALKqGEYG 408
Cdd:PRK12578 304 kggkfieEGQSEKggkvgVNLFGGLKAKGHPLGATGLSMIYEITKQLR-DEAG 355
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
63-156 |
2.76e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 42.96 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557237 63 PATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLqgGE---GQAptrqAVLGAGLpISTPCTTINKVCASGMKAIMMASQS 139
Cdd:PRK08256 21 DYPDMAAEAGRAALADAGIDYDAVQQAYVGYVY--GDstsGQR----ALYEVGM-TGIPIVNVNNNCSTGSTALFLARQA 93
|
90
....*....|....*..
gi 4557237 140 LMCGHQDVMVAGGMESM 156
Cdd:PRK08256 94 VRSGAADCALALGFEQM 110
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
87-157 |
2.92e-03 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 39.73 E-value: 2.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557237 87 KEAYMGNVLQGGEGQAPTRQAVLGAGLPIST-PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS 157
Cdd:cd00828 122 ARAVNPYVSPKWMLSPNTVAGWVNILLLSSHgPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
286-347 |
3.75e-03 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 39.44 E-value: 3.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557237 286 LNDGAAALVLMTADAAKRLNVTPLARIVAFA---DAA--VEPIDFPIAPVYAASMVLKDVGLKKEDI 347
Cdd:cd00834 229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGassDAYhiTAPDPDGEGAARAMRAALADAGLSPEDI 295
|
|
| |
