|
Name |
Accession |
Description |
Interval |
E-value |
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
3-329 |
1.79e-171 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 479.64 E-value: 1.79e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 3 KTTESKGNEITKEQARWMYEKMLEIRKFEDKVHELFAQGVLpGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCIA 82
Cdd:COG1071 8 DGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 83 KGCDLNGMMAELFGKVTGLCKGKGGSMHIADLNKGMLGANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTF 162
Cdd:COG1071 87 RGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 163 HEGVNLAAIWKLPVIFIAENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERARNGGGPTII 242
Cdd:COG1071 167 HEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 243 ECMTYRNYGHFEGEAQT-YKTSEEKEEHLnEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEFSENSPYPEDE 321
Cdd:COG1071 247 EAKTYRLGGHSTSDDPTrYRTKEEVEEWR-ERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPE 325
|
....*...
gi 1029200861 322 ELLKDVYV 329
Cdd:COG1071 326 ELFDDVYA 333
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
20-311 |
1.82e-150 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 424.60 E-value: 1.82e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 20 MYEKMLEIRKFEDKVHELFAQGVLPGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCIAKGCDLNGMMAELFGKVT 99
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 100 GLCKGKGGSMHIADLNKGMLGANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTFHEGVNLAAIWKLPVIFI 179
Cdd:cd02000 81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 180 AENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERARNGGGPTIIECMTYRNYGHF-EGEAQ 258
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHStSDDPS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1029200861 259 TYKTSEEkEEHLNEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEF 311
Cdd:cd02000 241 RYRTKEE-VEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEF 292
|
|
| PDH_E1_alph_y |
TIGR03182 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
14-329 |
6.28e-135 |
|
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 274473 [Multi-domain] Cd Length: 315 Bit Score: 385.77 E-value: 6.28e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 14 KEQARWMYEKMLEIRKFEDKVHELFAQGVLPGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCIAKGCDLNGMMAE 93
Cdd:TIGR03182 1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 94 LFGKVTGLCKGKGGSMHIADLNKGMLGANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTFHEGVNLAAIWK 173
Cdd:TIGR03182 81 LTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 174 LPVIFIAENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERARNGGGPTIIECMTYRNYGHF 253
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1029200861 254 EGEAQTYKTSEEKEEhLNEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEFSENSPYPEDEELLKDVYV 329
Cdd:TIGR03182 241 MSDPAKYRSKEEVEE-WRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
22-321 |
7.66e-113 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 329.29 E-value: 7.66e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 22 EKMLEIRKFEDKVHELFAQGVLPGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCIAKGCDLNGMMAELFGKVtgl 101
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 102 CKGKGGSMHIADLNKG--MLGANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTFHEGVNLAAIWKLPVIFI 179
Cdd:pfam00676 78 AKGKGGSMHGYYGAKGnrFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 180 AENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERARNGGGPTIIECMTYRNYGHFEG-EAQ 258
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSdDPS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1029200861 259 TYKTSEEKEEHLNEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEFSENSPYPEDE 321
Cdd:pfam00676 238 TYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
2-332 |
2.93e-98 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 296.85 E-value: 2.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 2 LKTTESKGNE----ITKEQARWMYEKMLEIRKFEDKVHELFAQGVLPGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGH 77
Cdd:PLN02374 69 VKEKNSKASAsdllVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 78 GHCIAKGCDLNGMMAELFGKVTGLCKGKGGSMHIADLNKGMLGANGIVGGGFPLACGSALTAKYK-------GTKDVSVC 150
Cdd:PLN02374 149 VHALSKGVPARAVMSELFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSKYRrevlkeeSCDDVTLA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 151 FFGDGANNEGTFHEGVNLAAIWKLPVIFIAENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAV 230
Cdd:PLN02374 229 FFGDGTCNNGQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 231 ERARNGGGPTIIECMTYRNYGHFEGEAQTYKTSEEKeEHLNEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIE 310
Cdd:PLN02374 309 ERARRGEGPTLVECETYRFRGHSLADPDELRDPAEK-AHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVE 387
|
330 340
....*....|....*....|..
gi 1029200861 311 FSENSPYPEDEELLKDVYVSYK 332
Cdd:PLN02374 388 FADASPLPPRSQLLENVFADPK 409
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
3-329 |
1.79e-171 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 479.64 E-value: 1.79e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 3 KTTESKGNEITKEQARWMYEKMLEIRKFEDKVHELFAQGVLpGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCIA 82
Cdd:COG1071 8 DGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 83 KGCDLNGMMAELFGKVTGLCKGKGGSMHIADLNKGMLGANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTF 162
Cdd:COG1071 87 RGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 163 HEGVNLAAIWKLPVIFIAENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERARNGGGPTII 242
Cdd:COG1071 167 HEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 243 ECMTYRNYGHFEGEAQT-YKTSEEKEEHLnEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEFSENSPYPEDE 321
Cdd:COG1071 247 EAKTYRLGGHSTSDDPTrYRTKEEVEEWR-ERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPE 325
|
....*...
gi 1029200861 322 ELLKDVYV 329
Cdd:COG1071 326 ELFDDVYA 333
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
20-311 |
1.82e-150 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 424.60 E-value: 1.82e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 20 MYEKMLEIRKFEDKVHELFAQGVLPGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCIAKGCDLNGMMAELFGKVT 99
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 100 GLCKGKGGSMHIADLNKGMLGANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTFHEGVNLAAIWKLPVIFI 179
Cdd:cd02000 81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 180 AENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERARNGGGPTIIECMTYRNYGHF-EGEAQ 258
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHStSDDPS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1029200861 259 TYKTSEEkEEHLNEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEF 311
Cdd:cd02000 241 RYRTKEE-VEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEF 292
|
|
| PDH_E1_alph_y |
TIGR03182 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
14-329 |
6.28e-135 |
|
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 274473 [Multi-domain] Cd Length: 315 Bit Score: 385.77 E-value: 6.28e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 14 KEQARWMYEKMLEIRKFEDKVHELFAQGVLPGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCIAKGCDLNGMMAE 93
Cdd:TIGR03182 1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 94 LFGKVTGLCKGKGGSMHIADLNKGMLGANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTFHEGVNLAAIWK 173
Cdd:TIGR03182 81 LTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 174 LPVIFIAENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERARNGGGPTIIECMTYRNYGHF 253
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1029200861 254 EGEAQTYKTSEEKEEhLNEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEFSENSPYPEDEELLKDVYV 329
Cdd:TIGR03182 241 MSDPAKYRSKEEVEE-WRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
22-321 |
7.66e-113 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 329.29 E-value: 7.66e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 22 EKMLEIRKFEDKVHELFAQGVLPGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCIAKGCDLNGMMAELFGKVtgl 101
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 102 CKGKGGSMHIADLNKG--MLGANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTFHEGVNLAAIWKLPVIFI 179
Cdd:pfam00676 78 AKGKGGSMHGYYGAKGnrFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 180 AENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERARNGGGPTIIECMTYRNYGHFEG-EAQ 258
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSdDPS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1029200861 259 TYKTSEEKEEHLNEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEFSENSPYPEDE 321
Cdd:pfam00676 238 TYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
2-332 |
2.93e-98 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 296.85 E-value: 2.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 2 LKTTESKGNE----ITKEQARWMYEKMLEIRKFEDKVHELFAQGVLPGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGH 77
Cdd:PLN02374 69 VKEKNSKASAsdllVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 78 GHCIAKGCDLNGMMAELFGKVTGLCKGKGGSMHIADLNKGMLGANGIVGGGFPLACGSALTAKYK-------GTKDVSVC 150
Cdd:PLN02374 149 VHALSKGVPARAVMSELFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSKYRrevlkeeSCDDVTLA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 151 FFGDGANNEGTFHEGVNLAAIWKLPVIFIAENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAV 230
Cdd:PLN02374 229 FFGDGTCNNGQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 231 ERARNGGGPTIIECMTYRNYGHFEGEAQTYKTSEEKeEHLNEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIE 310
Cdd:PLN02374 309 ERARRGEGPTLVECETYRFRGHSLADPDELRDPAEK-AHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVE 387
|
330 340
....*....|....*....|..
gi 1029200861 311 FSENSPYPEDEELLKDVYVSYK 332
Cdd:PLN02374 388 FADASPLPPRSQLLENVFADPK 409
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
2-330 |
6.43e-93 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 280.21 E-value: 6.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 2 LKTTESKGNEITKEQARWMYEKMLEIRKFEDKVHELFAQGVLPGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCI 81
Cdd:CHL00149 7 LPLTNSNENNINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 82 AKGCDLNGMMAELFGKVTGLCKGKGGSMHIADLNKGMLGANGIVGGGFPLACGSALTAKYK-------GTKDVSVCFFGD 154
Cdd:CHL00149 87 SKGVPPKNVMAELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSIYRqqvlkevQPLRVTACFFGD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 155 GANNEGTFHEGVNLAAIWKLPVIFIAENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERAR 234
Cdd:CHL00149 167 GTTNNGQFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERAR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 235 NGGGPTIIECMTYRNYGHFEGEAQTYKTSEEKEEHLnEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEFSEN 314
Cdd:CHL00149 247 QGDGPTLIEALTYRFRGHSLADPDELRSKQEKEAWV-ARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAIS 325
|
330
....*....|....*.
gi 1029200861 315 SPYPEDEELLKDVYVS 330
Cdd:CHL00149 326 SPEPNISDLKKYLFAD 341
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
11-330 |
3.87e-81 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 250.79 E-value: 3.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 11 EITKEQARWMYEKMLEIRKFEDKVHELFAQGVLPGFVHLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCIAKGCDLNGM 90
Cdd:PLN02269 26 ETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLEV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 91 MAELFGKVTGLCKGKGGSMHIADLNKGMLGANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTFHEGVNLAA 170
Cdd:PLN02269 106 FAELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 171 IWKLPVIFIAENNGYGEATTFEYASSCDSIADRAKAynIPGVQVDGKDLLAVYKAAEEAVERARNgGGPTIIECMTYRNY 250
Cdd:PLN02269 186 LWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDY--VPGLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMDTYRYH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 251 GH-FEGEAQTYKTSEEKEEHLNEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEFSENSPYPEDEELLKDVYV 329
Cdd:PLN02269 263 GHsMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVYV 342
|
.
gi 1029200861 330 S 330
Cdd:PLN02269 343 K 343
|
|
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
12-328 |
4.36e-75 |
|
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 213783 [Multi-domain] Cd Length: 341 Bit Score: 234.35 E-value: 4.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 12 ITKEQARWMYEKMLEIRKFEDKVHELFAQGVLPGFVhLYAGEEAVAVGVCAHLTDCDSITSTHRGHGHCIAKGCDlngmM 91
Cdd:TIGR03181 21 LSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYA-PNLGQEAAQVGSALALRKDDWVFPSYRDHAAMLARGVP----L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 92 AELFGKVTGLCKGkggsMHIADlNKGMLGANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTFHEGVNLAAI 171
Cdd:TIGR03181 96 VEILLYWRGDERG----SWDPE-GVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGDFYEALNFAGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 172 WKLPVIFIAENNGYGEATTFEYASSCDSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERARNGGGPTIIECMTYRnYG 251
Cdd:TIGR03181 171 FKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGPTLIEAVTYR-LG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 252 hfegeAQT-------YKTSEEKEEHLnEKDAIVNFRKHLIHEALLTESELVDIEKAVDEAVQRSIEFSENSPYPEDEELL 324
Cdd:TIGR03181 250 -----PHTtaddptrYRTKEEEEEWR-KKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPVDDIF 323
|
....
gi 1029200861 325 KDVY 328
Cdd:TIGR03181 324 DHVY 327
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
121-251 |
1.85e-12 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 66.37 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 121 ANGIVGGGFPLACGSALTAKYKGTKDVSVCFFGDGANNEGTFHEGVNLAAIWKL-PVIFIAENNGYGEATTFEYASSCDS 199
Cdd:cd02012 103 TTGSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNRIQIDGPTDDILFTED 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1029200861 200 IADRAKAYNIPGVQVDGKDLLAVYKAAEEAverARNGGGPTIIECMTYRNYG 251
Cdd:cd02012 183 LAKKFEAFGWNVIEVDGHDVEEILAALEEA---KKSKGKPTLIIAKTIKGKG 231
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
120-246 |
4.54e-11 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 60.73 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 120 GANGIVGGGFPLACGSALTAKykgtKDVSVCFFGDGAnnegtFHEGVN---LAAIWKLPVIFI-AENNGYG------EAT 189
Cdd:cd00568 43 TGFGAMGYGLPAAIGAALAAP----DRPVVCIAGDGG-----FMMTGQelaTAVRYGLPVIVVvFNNGGYGtirmhqEAF 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1029200861 190 TFEYASSCD----SIADRAKAYNIPGVQVDGKDllavykAAEEAVERARNGGGPTIIECMT 246
Cdd:cd00568 114 YGGRVSGTDlsnpDFAALAEAYGAKGVRVEDPE------DLEAALAEALAAGGPALIEVKT 168
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
126-246 |
1.18e-07 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 53.21 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 126 GGGFPLACGSALTAKYKGTK----DVSV------CFFGDGANNEGTFHEGVNLAAIWKL-PVIFIAENNGY---GEATTf 191
Cdd:PRK05899 121 GQGLANAVGMALAEKYLAALfnrpGLDIvdhytyVLCGDGDLMEGISHEACSLAGHLKLgNLIVIYDDNRIsidGPTEG- 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1029200861 192 eyaSSCDSIADRAKAYNIPGVQVDGKDLLAVYKAaeeaVERARNGGGPTIIECMT 246
Cdd:PRK05899 200 ---WFTEDVKKRFEAYGWHVIEVDGHDVEAIDAA----IEEAKASTKPTLIIAKT 247
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
126-246 |
1.61e-06 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 49.39 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 126 GGGFPLACGSALTAKykgTKDVsVCFFGDGAnnegtFheGVNLAAIW-----KLPVIF-IAENNGYG------EATTFEY 193
Cdd:COG0028 415 GYGLPAAIGAKLARP---DRPV-VAITGDGG-----F--QMNLQELAtavryGLPVKVvVLNNGGLGmvrqwqELFYGGR 483
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1029200861 194 ASSCD----SIADRAKAYNIPGVQVDGKDLLavykaaEEAVERARNGGGPTIIECMT 246
Cdd:COG0028 484 YSGTDlpnpDFAKLAEAFGAKGERVETPEEL------EAALEEALASDGPALIDVRV 534
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
120-244 |
1.90e-06 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 46.81 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 120 GANGIVGGGFPLACGsaltAKYKGTKDVSVCFFGDGanneGTFHEGVNLAAIW--KLPVIFIAENNG-YG------EATT 190
Cdd:pfam02775 25 GGLGTMGYGLPAAIG----AKLARPDRPVVAIAGDG----GFQMNLQELATAVryNLPITVVVLNNGgYGmtrgqqTPFG 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1029200861 191 FEYASSCDSIADR-------AKAYNIPGVQVDgkdllaVYKAAEEAVERARNGGGPTIIEC 244
Cdd:pfam02775 97 GGRYSGPSGKILPpvdfaklAEAYGAKGARVE------SPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_E1_OGDC_like |
cd02016 |
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ... |
130-255 |
1.59e-05 |
|
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDC). OGDC catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA and carbon dioxide, a key reaction of the tricarboxylic acid cycle.
Pssm-ID: 238974 [Multi-domain] Cd Length: 265 Bit Score: 45.60 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 130 PLACGSA-----LTAKYKGTKDVSVCFFGDGA-NNEGTFHEGVNLaaiWKLP------VIFIAENNGYGEATTFEYASSC 197
Cdd:cd02016 120 PVVMGKTrakqdYRGDGERDKVLPILIHGDAAfAGQGVVYETLNL---SNLPgyttggTIHIVVNNQIGFTTDPRDSRSS 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1029200861 198 DSIADRAKAYNIPGVQVDGKDLLAVYKAAEEAVERARNGGGPTIIECMTYRNYGHFEG 255
Cdd:cd02016 197 PYCTDVAKMIGAPIFHVNGDDPEAVVRATRLALEYRQKFKKDVVIDLVCYRRHGHNEL 254
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
120-246 |
8.03e-05 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 44.18 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 120 GANGIVGGGFPLACGSALtAKykgTKDVSVCFFGDGANNEGtfhegvnLAAIW-----KLPVIFIAENNG-YGE----AT 189
Cdd:PRK07092 404 MASGGLGYGLPAAVGVAL-AQ---PGRRVIGLIGDGSAMYS-------IQALWsaaqlKLPVTFVILNNGrYGAlrwfAP 472
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 190 TFEYAsscdsiadrakayNIPGVQVDGKDLLA-----------VYKAAE--EAVERARNGGGPTIIECMT 246
Cdd:PRK07092 473 VFGVR-------------DVPGLDLPGLDFVAlargygceavrVSDAAElaDALARALAADGPVLVEVEV 529
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
131-246 |
1.30e-04 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 42.15 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 131 LACGSALTAKYKGTKDVSVCFFGDGANNEGTFHEGVNLAAIWKLPVIF--------IAENNGYGeATTFEyasscdsiad 202
Cdd:cd02007 83 AALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVilndnemsISPNVGTP-GNLFE---------- 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1029200861 203 rAKAYNIPGVqVDGKDLLAVykaaEEAVERARNGGGPTIIECMT 246
Cdd:cd02007 152 -ELGFRYIGP-VDGHNIEAL----IKVLKEVKDLKGPVLLHVVT 189
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
126-246 |
1.00e-03 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 39.50 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029200861 126 GGGFPLACGSALTAKykgTKDVsVCFFGDGAnnegtFHEGVNlaAIW-----KLPVIFIAENNG------------YGEA 188
Cdd:cd02002 52 GWGLPAAVGAALANP---DRKV-VAIIGDGS-----FMYTIQ--ALWtaaryGLPVTVVILNNRgygalrsflkrvGPEG 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1029200861 189 TTFEYASSCDS------IADRAKAYNIPGVQVDGKDLLAvykaaeEAVERARNGGGPTIIECMT 246
Cdd:cd02002 121 PGENAPDGLDLldpgidFAAIAKAFGVEAERVETPEELD------EALREALAEGGPALIEVVV 178
|
|
| |
