|
Name |
Accession |
Description |
Interval |
E-value |
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
5-322 |
6.65e-162 |
|
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: 454.98 E-value: 6.65e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 5 SKEQHLDMFLKMERIREFDSRINKLVRRGFVqGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMMA 84
Cdd:COG1071 18 SKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVDPKELMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 85 ELAGKATGVSKGRGGSMHLADFEKGNYGTNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATW 164
Cdd:COG1071 97 ELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 165 KLPVIFFIINNRYGISMSINNATNTPHLYTRAEAYGVPGFYCeDGNDVMAVYETMGKAVEHVRGGNGPAIVEVESYRWFG 244
Cdd:COG1071 177 KLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRV-DGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGG 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499224698 245 HSTADAG-KYRTKEEVDEWKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELSVAFEDVWVD 322
Cdd:COG1071 256 HSTSDDPtRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAE 334
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
12-304 |
1.06e-146 |
|
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: 414.59 E-value: 1.06e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 12 MFLKMERIREFDSRINKLVRRGFVQGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMMAELAGKAT 91
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 92 GVSKGRGGSMHLADFEKGNYGTNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATWKLPVIFF 171
Cdd:cd02000 81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 172 IINNRYGISMSINNATNTPHLYTRAEAYGVPGFYCeDGNDVMAVYETMGKAVEHVRGGNGPAIVEVESYRWFGHSTA-DA 250
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRV-DGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499224698 251 GKYRTKEEVDEWKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFA 304
Cdd:cd02000 240 SRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PDH_E1_alph_y |
TIGR03182 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
6-321 |
2.49e-132 |
|
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: 378.84 E-value: 2.49e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 6 KEQHLDMFLKMERIREFDSRINKLVRRGFVQGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMMAE 85
Cdd:TIGR03182 1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 86 LAGKATGVSKGRGGSMHLADFEKGNYGTNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATWK 165
Cdd:TIGR03182 81 LTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 166 LPVIFFIINNRYGISMSINNATNTPHLYTRAEAYGVPGFYCeDGNDVMAVYETMGKAVEHVRGGNGPAIVEVESYRWFGH 245
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERV-DGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGH 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499224698 246 STADAGKYRTKEEVDEWKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELSVAFEDVWV 321
Cdd:TIGR03182 240 SMSDPAKYRSKEEVEEWRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
15-313 |
5.52e-97 |
|
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: 288.45 E-value: 5.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 15 KMERIREFDSRINKLVRRGFVQGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMMAELAGKatgVS 94
Cdd:pfam00676 2 RMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGR---VA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 95 KGRGGSMHLADFEKGN--YGTNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATWKLPVIFFI 172
Cdd:pfam00676 79 KGKGGSMHGYYGAKGNrfYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 173 INNRYGISMSINNATNTPHLYTRAEAYGVPGFYCeDGNDVMAVYETMGKAVEHVRGGNGPAIVEVESYRWFGHSTADAG- 251
Cdd:pfam00676 159 ENNQYGISTPAERASASTTYADRARGYGIPGLHV-DGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPs 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499224698 252 KYRTKEEVDE-WKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELS 313
Cdd:pfam00676 238 TYRTRDEYEEvRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
1-321 |
1.27e-81 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 251.56 E-value: 1.27e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 1 MVTVSKEQHLDMFLKMERIREFDSRINKLVRRGFVQGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLN 80
Cdd:PLN02269 24 TVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 81 KMMAELAGKATGVSKGRGGSMHLADFEKGNYGTNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNM 160
Cdd:PLN02269 104 EVFAELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 161 AATWKLPVIFFIINNRYGISMSINNATNTPHLYTRAEAygVPGFYCeDGNDVMAVYETMGKAVEHVrGGNGPAIVEVESY 240
Cdd:PLN02269 184 AALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDY--VPGLKV-DGMDVLAVKQACKFAKEHA-LSNGPIVLEMDTY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 241 RWFGHSTADAGK-YRTKEEVDEWK-EKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELSVAFED 318
Cdd:PLN02269 260 RYHGHSMSDPGStYRTRDEISGVRqERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTN 339
|
...
gi 499224698 319 VWV 321
Cdd:PLN02269 340 VYV 342
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
5-322 |
6.65e-162 |
|
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: 454.98 E-value: 6.65e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 5 SKEQHLDMFLKMERIREFDSRINKLVRRGFVqGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMMA 84
Cdd:COG1071 18 SKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVDPKELMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 85 ELAGKATGVSKGRGGSMHLADFEKGNYGTNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATW 164
Cdd:COG1071 97 ELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 165 KLPVIFFIINNRYGISMSINNATNTPHLYTRAEAYGVPGFYCeDGNDVMAVYETMGKAVEHVRGGNGPAIVEVESYRWFG 244
Cdd:COG1071 177 KLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRV-DGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGG 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499224698 245 HSTADAG-KYRTKEEVDEWKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELSVAFEDVWVD 322
Cdd:COG1071 256 HSTSDDPtRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAE 334
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
12-304 |
1.06e-146 |
|
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: 414.59 E-value: 1.06e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 12 MFLKMERIREFDSRINKLVRRGFVQGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMMAELAGKAT 91
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 92 GVSKGRGGSMHLADFEKGNYGTNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATWKLPVIFF 171
Cdd:cd02000 81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 172 IINNRYGISMSINNATNTPHLYTRAEAYGVPGFYCeDGNDVMAVYETMGKAVEHVRGGNGPAIVEVESYRWFGHSTA-DA 250
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRV-DGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499224698 251 GKYRTKEEVDEWKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFA 304
Cdd:cd02000 240 SRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PDH_E1_alph_y |
TIGR03182 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
6-321 |
2.49e-132 |
|
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: 378.84 E-value: 2.49e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 6 KEQHLDMFLKMERIREFDSRINKLVRRGFVQGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMMAE 85
Cdd:TIGR03182 1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 86 LAGKATGVSKGRGGSMHLADFEKGNYGTNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATWK 165
Cdd:TIGR03182 81 LTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 166 LPVIFFIINNRYGISMSINNATNTPHLYTRAEAYGVPGFYCeDGNDVMAVYETMGKAVEHVRGGNGPAIVEVESYRWFGH 245
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERV-DGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGH 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499224698 246 STADAGKYRTKEEVDEWKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELSVAFEDVWV 321
Cdd:TIGR03182 240 SMSDPAKYRSKEEVEEWRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
15-313 |
5.52e-97 |
|
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: 288.45 E-value: 5.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 15 KMERIREFDSRINKLVRRGFVQGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMMAELAGKatgVS 94
Cdd:pfam00676 2 RMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGR---VA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 95 KGRGGSMHLADFEKGN--YGTNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATWKLPVIFFI 172
Cdd:pfam00676 79 KGKGGSMHGYYGAKGNrfYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 173 INNRYGISMSINNATNTPHLYTRAEAYGVPGFYCeDGNDVMAVYETMGKAVEHVRGGNGPAIVEVESYRWFGHSTADAG- 251
Cdd:pfam00676 159 ENNQYGISTPAERASASTTYADRARGYGIPGLHV-DGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPs 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499224698 252 KYRTKEEVDE-WKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELS 313
Cdd:pfam00676 238 TYRTRDEYEEvRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
4-319 |
1.33e-86 |
|
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: 263.62 E-value: 1.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 4 VSKEQHLDMFLKMERIREFDSRINKLVRRGFVqGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMM 83
Cdd:TIGR03181 21 LSDEELVELYRDMVLTRRFDTKALALQRQGRL-GTYAPNLGQEAAQVGSALALRKDDWVFPSYRDHAAMLARGVPLVEIL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 84 AelagkatgVSKGRggsmhladfEKGNYGTNG--------IVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFH 155
Cdd:TIGR03181 100 L--------YWRGD---------ERGSWDPEGvnilppniPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGDFY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 156 ESVNMAATWKLPVIFFIINNRYGISMSINNATNTPHLYTRAEAYGVPGFYCeDGNDVMAVYETMGKAVEHVRGGNGPAIV 235
Cdd:TIGR03181 163 EALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQV-DGNDVLAVYAVTKEAVERARSGGGPTLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 236 EVESYRWFGHSTAD-AGKYRTKEEVDEWKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELSV 314
Cdd:TIGR03181 242 EAVTYRLGPHTTADdPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPVDD 321
|
....*
gi 499224698 315 AFEDV 319
Cdd:TIGR03181 322 IFDHV 326
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
1-321 |
1.27e-81 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 251.56 E-value: 1.27e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 1 MVTVSKEQHLDMFLKMERIREFDSRINKLVRRGFVQGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLN 80
Cdd:PLN02269 24 TVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 81 KMMAELAGKATGVSKGRGGSMHLADFEKGNYGTNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNM 160
Cdd:PLN02269 104 EVFAELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 161 AATWKLPVIFFIINNRYGISMSINNATNTPHLYTRAEAygVPGFYCeDGNDVMAVYETMGKAVEHVrGGNGPAIVEVESY 240
Cdd:PLN02269 184 AALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDY--VPGLKV-DGMDVLAVKQACKFAKEHA-LSNGPIVLEMDTY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 241 RWFGHSTADAGK-YRTKEEVDEWK-EKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELSVAFED 318
Cdd:PLN02269 260 RYHGHSMSDPGStYRTRDEISGVRqERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTN 339
|
...
gi 499224698 319 VWV 321
Cdd:PLN02269 340 VYV 342
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
4-322 |
2.80e-79 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 247.93 E-value: 2.80e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 4 VSKEQHLDMFLKMERIREFDSRINKLVRRGFVQGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMM 83
Cdd:PLN02374 83 VTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVM 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 84 AELAGKATGVSKGRGGSMHLADFEKGNYGTNGIVGGGYALAVGAALTQQYK-------GTNNIAVAFSGDGATNEGSFHE 156
Cdd:PLN02374 163 SELFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSKYRrevlkeeSCDDVTLAFFGDGTCNNGQFFE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 157 SVNMAATWKLPVIFFIINNRYGISMSINNATNTPHLYTRAEAYGVPGFYCeDGNDVMAVYETMGKAVEHVRGGNGPAIVE 236
Cdd:PLN02374 243 CLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHV-DGMDVLKVREVAKEAIERARRGEGPTLVE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 237 VESYRWFGHSTADAGKYRTKEEVDEWKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELSVAF 316
Cdd:PLN02374 322 CETYRFRGHSLADPDELRDPAEKAHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPRSQLL 401
|
....*.
gi 499224698 317 EDVWVD 322
Cdd:PLN02374 402 ENVFAD 407
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
4-313 |
1.74e-76 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 237.84 E-value: 1.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 4 VSKEQHLDMFLKMERIREFDSRINKLVRRGFVQGMTHFSVGEEAANVGAVAHLSYDDIIFSNHRGHGQSIAKDMDLNKMM 83
Cdd:CHL00149 17 INSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 84 AELAGKATGVSKGRGGSMHLADFEKGNYGTNGIVGGGYALAVGAALTQQYK-------GTNNIAVAFSGDGATNEGSFHE 156
Cdd:CHL00149 97 AELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSIYRqqvlkevQPLRVTACFFGDGTTNNGQFFE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 157 SVNMAATWKLPVIFFIINNRYGISMSINNATNTPHLYTRAEAYGVPGfyCE-DGNDVMAVYETMGKAVEHVRGGNGPAIV 235
Cdd:CHL00149 177 CLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPG--IEvDGMDVLAVREVAKEAVERARQGDGPTLI 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499224698 236 EVESYRWFGHSTADAGKYRTKEEVDEWKEKDPMIKYRTYLTSEGIATDDELDAIQAQVKKEVDDAYEFAQNSPDPELS 313
Cdd:CHL00149 255 EALTYRFRGHSLADPDELRSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNIS 332
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
113-222 |
1.63e-11 |
|
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: 63.29 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 113 TNGIVGGGYALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATWKL-PVIFFIINNRYGISMSINNATNTPH 191
Cdd:cd02012 103 TTGSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNRIQIDGPTDDILFTED 182
|
90 100 110
....*....|....*....|....*....|...
gi 499224698 192 LYTRAEAYgvpGFYCE--DGNDVMAVYETMGKA 222
Cdd:cd02012 183 LAKKFEAF---GWNVIevDGHDVEEILAALEEA 212
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
79-237 |
5.07e-10 |
|
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: 57.65 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 79 LNKMMAELAGKATGVSKGRGGSMHLADFEKGN-YGTNGIVGG-GYAL--AVGAALTQQykgtNNIAVAFSGDGatnegSF 154
Cdd:cd00568 6 LRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRrFLTSTGFGAmGYGLpaAIGAALAAP----DRPVVCIAGDG-----GF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 155 HESVNMAATW---KLPVIFFIINNR-YG-ISMSINNATNTPHLYTR---------AEAYGVPGFYCEDGNDVMAVYEtmg 220
Cdd:cd00568 77 MMTGQELATAvryGLPVIVVVFNNGgYGtIRMHQEAFYGGRVSGTDlsnpdfaalAEAYGAKGVRVEDPEDLEAALA--- 153
|
170
....*....|....*..
gi 499224698 221 KAVEHvrggNGPAIVEV 237
Cdd:cd00568 154 EALAA----GGPALIEV 166
|
|
| 2oxo_dh_E1 |
TIGR00239 |
2-oxoglutarate dehydrogenase, E1 component; The 2-oxoglutarate dehydrogenase complex consists ... |
128-300 |
6.83e-10 |
|
2-oxoglutarate dehydrogenase, E1 component; The 2-oxoglutarate dehydrogenase complex consists of this thiamine pyrophosphate-binding subunit (E1), dihydrolipoamide succinyltransferase (E2), and lipoamide dehydrogenase (E3). The E1 ortholog from Corynebacterium glutamicum is unusual in having an N-terminal extension that resembles the dihydrolipoamide succinyltransferase (E2) component of 2-oxoglutarate dehydrogenase. [Energy metabolism, TCA cycle]
Pssm-ID: 161785 [Multi-domain] Cd Length: 929 Bit Score: 60.27 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 128 ALTQQYKGTNNIAVAFSGDGA-TNEGSFHESVNMAATWKLPV---IFFIINNRYGISMSINNATNTPHLYTRAEAYGVPG 203
Cdd:TIGR00239 334 RLNDSPESTKVLAILIHGDAAfAGQGVVQETLNMSKLRGYSVggtIHIIINNQIGFTTNPLDARSTPYCSDLAKMIQAPI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 204 FYCeDGNDVMAVYETMGKAVEHVRGGNGPAIVEVESYRWFGHSTADAGKYRTKEEVDEWKEKDPMIK-YRTYLTSEGIAT 282
Cdd:TIGR00239 414 FHV-NADDPEAVAFATRLAVEYRNTFKRDVFIDLVGYRRHGHNEADEPSATQPLMYQKIKKHPTPRKvYADKLVSEGVAT 492
|
170
....*....|....*...
gi 499224698 283 DDELDAIQAQVKKEVDDA 300
Cdd:TIGR00239 493 EEDVTEMVNLYRDALEAA 510
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
110-237 |
1.17e-07 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 50.28 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 110 NYGTNGIVGGGYALAVGAALtqqyKGTNNIAVAFSGDGATNeGSFHESVNmAATWKLPVIFFIINNR-YGI-----SMSI 183
Cdd:pfam02775 23 TSGGLGTMGYGLPAAIGAKL----ARPDRPVVAIAGDGGFQ-MNLQELAT-AVRYNLPITVVVLNNGgYGMtrgqqTPFG 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499224698 184 NNATNTPHLYTR--------AEAYGVPGFYCEDGNDVMAVYEtmgKAVEHvrggNGPAIVEV 237
Cdd:pfam02775 97 GGRYSGPSGKILppvdfaklAEAYGAKGARVESPEELEEALK---EALEH----DGPALIDV 151
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
120-237 |
2.10e-07 |
|
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: 52.08 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 120 GYAL--AVGAALTQqykgTNNIAVAFSGDGatnegSFHESVN---MAATWKLPVIFFIINNR-YG-ISMSINNATNTPHL 192
Cdd:COG0028 415 GYGLpaAIGAKLAR----PDRPVVAITGDG-----GFQMNLQelaTAVRYGLPVKVVVLNNGgLGmVRQWQELFYGGRYS 485
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 499224698 193 YTR---------AEAYGVPGFYCEDGNDVMAVYEtmgKAVEHvrggNGPAIVEV 237
Cdd:COG0028 486 GTDlpnpdfaklAEAFGAKGERVETPEELEAALE---EALAS----DGPALIDV 532
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
113-237 |
4.19e-05 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 45.12 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 113 TNGIVGGGYALAVGAALTQQYKGTNNIAVAFS----------GDGATNEGSFHESVNMAATWKL-PVIFFIINNRYGISM 181
Cdd:PRK05899 116 TTGPLGQGLANAVGMALAEKYLAALFNRPGLDivdhytyvlcGDGDLMEGISHEACSLAGHLKLgNLIVIYDDNRISIDG 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499224698 182 SINNA--TNTPHlytRAEAYG-----VpgfyceDGNDVMAVYetmgKAVEHVRGGNGPAIVEV 237
Cdd:PRK05899 196 PTEGWftEDVKK---RFEAYGwhvieV------DGHDVEAID----AAIEEAKASTKPTLIIA 245
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
122-237 |
7.96e-05 |
|
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: 42.92 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 122 ALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATWKLPVIffIINNRYGISMSINNATNTPHLytraEAYGV 201
Cdd:cd02007 82 SAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMI--VILNDNEMSISPNVGTPGNLF----EELGF 155
|
90 100 110
....*....|....*....|....*....|....*.
gi 499224698 202 PGFYCEDGNDVmavyETMGKAVEHVRGGNGPAIVEV 237
Cdd:cd02007 156 RYIGPVDGHNI----EALIKVLKEVKDLKGPVLLHV 187
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
109-237 |
8.30e-05 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 42.52 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 109 GNYGTNGiVGGGYALAvgAALtqqYKGTNNIaVAFSGDGATnegSFH-ESVNMAATWKLPVIFFIINNR--YGIS--MSI 183
Cdd:cd02004 45 GTFGTLG-VGLGYAIA--AAL---ARPDKRV-VLVEGDGAF---GFSgMELETAVRYNLPIVVVVGNNGgwYQGLdgQQL 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499224698 184 NNATNTPH----LYTR----AEAYGVPGFYCEDgndvmavYETMGKAVEHVRGGNGPAIVEV 237
Cdd:cd02004 115 SYGLGLPVttllPDTRydlvAEAFGGKGELVTT-------PEELKPALKRALASGKPALINV 169
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
113-222 |
1.04e-04 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 43.53 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 113 TNGIVGGGYALAVGAALTQQYKG----------TNNIAVAFSGDGATNEGSFHESVNMAATWKL-PVIFFIINNRYGI-- 179
Cdd:pfam00456 110 TTGPLGQGIANAVGMAIAERNLAatynrpgfdiVDHYTYVFLGDGCLMEGVSSEASSLAGHLGLgNLIVFYDDNQISIdg 189
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 499224698 180 SMSINNATNTPhlyTRAEAYGVPGFYCEDGNDVMAVYETMGKA 222
Cdd:pfam00456 190 ETKISFTEDTA---ARFEAYGWHVIEVEDGHDVEAIAAAIEEA 229
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
109-237 |
1.20e-04 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 42.13 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 109 GNYGTNGIvggGYALAVGAALTQ---QykgtnniAVAFSGDGATnegsfheSVNM-----AATWKLPVIFFIINNR---- 176
Cdd:cd02014 48 GLLATMGN---GLPGAIAAKLAYpdrQ-------VIALSGDGGF-------AMLMgdlitAVKYNLPVIVVVFNNSdlgf 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499224698 177 ------------YGISMSINNatntphlYTR-AEAYGVPGFYCEDGNDVMAVYEtmgKAVEHvrggNGPAIVEV 237
Cdd:cd02014 111 ikweqevmgqpeFGVDLPNPD-------FAKiAEAMGIKGIRVEDPDELEAALD---EALAA----DGPVVIDV 170
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
118-238 |
2.30e-04 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 42.63 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 118 GG-GYAL--AVGAALTQQYKGTnniaVAFSGDGATNEGSfhESVNMAATWKLPVIFFIINN-RYGISMS---INNATNTP 190
Cdd:PRK07092 407 GGlGYGLpaAVGVALAQPGRRV----IGLIGDGSAMYSI--QALWSAAQLKLPVTFVILNNgRYGALRWfapVFGVRDVP 480
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 499224698 191 HLYTR-------AEAYGVPGFYCEDGNDVMAvyetmgkAVEHVRGGNGPAIVEVE 238
Cdd:PRK07092 481 GLDLPgldfvalARGYGCEAVRVSDAAELAD-------ALARALAADGPVLVEVE 528
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
118-237 |
8.91e-04 |
|
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: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 118 GG-GYAL--AVGAALTQQykgtNNIAVAFSGDGatnegSFHESVNMAATW---KLPVIFFIINNR-YGIS-------MSI 183
Cdd:cd02002 49 GGlGWGLpaAVGAALANP----DRKVVAIIGDG-----SFMYTIQALWTAaryGLPVTVVILNNRgYGALrsflkrvGPE 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499224698 184 NNATNTPHLYTR----------AEAYGVPGFYCEDGNDVMAVYEtmgKAVEHvrggNGPAIVEV 237
Cdd:cd02002 120 GPGENAPDGLDLldpgidfaaiAKAFGVEAERVETPEELDEALR---EALAE----GGPALIEV 176
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
122-244 |
9.73e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 40.76 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 122 ALAVGAALTQQYKGTNNIAVAFSGDGATNEGSFHESVNMAATWKLPVIFFIINNRygisMSInnATNTPHLYT------- 194
Cdd:PRK12315 120 ALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELKSNLIIIVNDNQ----MSI--AENHGGLYKnlkelrd 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499224698 195 ---RAE-----AYGVPGFYCEDGNDVMAVYETMGKA-------VEHV---RG-GNGPAIVEVESYRWFG 244
Cdd:PRK12315 194 tngQSEnnlfkAMGLDYRYVEDGNDIESLIEAFKEVkdidhpiVLHIhtlKGkGYQPAEENKEAFHWHM 262
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|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
53-185 |
7.95e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 37.77 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499224698 53 VAHLSYDDIIFSNHRGHGQSIAKdmdlnkmmaelagkatgvSKGRGGSMHLADFEKGNYGT---NGIVGGGYALAVGAAL 129
Cdd:PLN02234 134 VGHQSYPHKILTGRRGKMKTIRQ------------------TNGLSGYTKRRESEHDSFGTghsSTTLSAGLGMAVGRDL 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 499224698 130 tqqyKGTNNIAVAFSGDGATNEGSFHESVNMAATWKLPVIfFIINNRYGISMSINN 185
Cdd:PLN02234 196 ----KGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMI-VILNDNKQVSLPTAN 246
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
120-179 |
8.02e-03 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 36.74 E-value: 8.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499224698 120 GYAL--AVGAALTQQYKGTnniaVAFSGDGatnegSFHESVNMAAT---WKLPVIFFIINNR-YGI 179
Cdd:cd02005 53 GYSVpaALGAALAAPDRRV----ILLVGDG-----SFQMTVQELSTmirYGLNPIIFLINNDgYTI 109
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|
| |
