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Conserved domains on  [gi|4885543|ref|NP_005381|]
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pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial precursor [Homo sapiens]

Protein Classification

pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha( domain architecture ID 10799057)

pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha is part of the thiamine pyrophosphate-dependent enzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
56-368 0e+00

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: 526.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543     56 RAEGLKYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSILAE 135
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    136 LTGRRGGCAKGKGGSMHMYT--KNFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAANQGQIAEAFNMAALWK 213
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    214 LPCVFICENNLYGMGTSTERAAASPDYYKRGNF--IPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHS 291
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4885543    292 MSDPGvSYRTREEIQEVRsKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLEELGHHIYS 368
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
 
Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
56-368 0e+00

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: 526.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543     56 RAEGLKYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSILAE 135
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    136 LTGRRGGCAKGKGGSMHMYT--KNFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAANQGQIAEAFNMAALWK 213
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    214 LPCVFICENNLYGMGTSTERAAASPDYYKRGNF--IPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHS 291
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4885543    292 MSDPGvSYRTREEIQEVRsKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLEELGHHIYS 368
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
28-380 0e+00

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 509.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    28 SSNDATFEIKKC-DLYLLEEgPPVTTVLTRAEGLKYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGI 106
Cdd:PLN02269   1 STDPITIETPVPfKGHLCDP-PSRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   107 NPSDHVITSYRAHGVCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTK--NFYGGNGIVGAQGPLGAGIALACKYKGN 184
Cdd:PLN02269  80 TKEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   185 DEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDYYKRGNFIPGLKVDGMDVLCVREAT 264
Cdd:PLN02269 160 ENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQAC 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   265 KFAANYCRSgKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEI 344
Cdd:PLN02269 240 KFAKEHALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEV 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 4885543   345 DDAAQFATTDPEPHLEELGHHIYSSDSSFEVRGANP 380
Cdd:PLN02269 319 DDAVAKAKESPMPDPSELFTNVYVKGLGVESYGADR 354
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
62-351 4.36e-152

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: 430.76  E-value: 4.36e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   62 YYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSILAELTGRRG 141
Cdd:cd02000   1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  142 GCAKGKGGSMHM--YTKNFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFI 219
Cdd:cd02000  81 GPCKGRGGSMHIgdKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  220 CENNLYGMGTSTERAAASPDYYKRG--NFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGV 297
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAaaYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 4885543  298 SYRTREEIQEvRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFA 351
Cdd:cd02000 241 RYRTKEEVEE-WKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
63-360 1.91e-151

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: 429.44  E-value: 1.91e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543     63 YRMMlTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSILAELTGRRGg 142
Cdd:pfam00676   1 RRMM-TLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVA- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    143 caKGKGGSMHMYTK----NFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVF 218
Cdd:pfam00676  79 --KGKGGSMHGYYGakgnRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    219 ICENNLYGMGTSTERAAASPDYYK--RGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPG 296
Cdd:pfam00676 157 VCENNQYGISTPAERASASTTYADraRGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDP 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4885543    297 VSYRTREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLE 360
Cdd:pfam00676 237 STYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
42-368 3.80e-146

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: 418.01  E-value: 3.80e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   42 YLLEEGPPVTTV-LTRAEGLKYYRMMLTVRRMELKADQLYKQKFIrGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHG 120
Cdd:COG1071   4 VLDPDGTEAALPdLSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  121 VCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTK--NFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAAN 198
Cdd:COG1071  83 HALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKelNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  199 QGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDYYKRGN-F-IPGLKVDGMDVLCVREATKFAANYCRSGKG 276
Cdd:COG1071 163 EGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAgYgIPGVRVDGNDVLAVYAAVKEAVERARAGEG 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  277 PILMELQTYRYHGHSMSDPGVSYRTREEIQEVRsKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPE 356
Cdd:COG1071 243 PTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWR-ERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPE 321
                       330
                ....*....|..
gi 4885543  357 PHLEELGHHIYS 368
Cdd:COG1071 322 PDPEELFDDVYA 333
 
Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
56-368 0e+00

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: 526.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543     56 RAEGLKYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSILAE 135
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    136 LTGRRGGCAKGKGGSMHMYT--KNFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAANQGQIAEAFNMAALWK 213
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    214 LPCVFICENNLYGMGTSTERAAASPDYYKRGNF--IPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHS 291
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4885543    292 MSDPGvSYRTREEIQEVRsKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLEELGHHIYS 368
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
28-380 0e+00

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 509.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    28 SSNDATFEIKKC-DLYLLEEgPPVTTVLTRAEGLKYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGI 106
Cdd:PLN02269   1 STDPITIETPVPfKGHLCDP-PSRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   107 NPSDHVITSYRAHGVCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTK--NFYGGNGIVGAQGPLGAGIALACKYKGN 184
Cdd:PLN02269  80 TKEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   185 DEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDYYKRGNFIPGLKVDGMDVLCVREAT 264
Cdd:PLN02269 160 ENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQAC 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   265 KFAANYCRSgKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEI 344
Cdd:PLN02269 240 KFAKEHALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEV 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 4885543   345 DDAAQFATTDPEPHLEELGHHIYSSDSSFEVRGANP 380
Cdd:PLN02269 319 DDAVAKAKESPMPDPSELFTNVYVKGLGVESYGADR 354
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
62-351 4.36e-152

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: 430.76  E-value: 4.36e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   62 YYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSILAELTGRRG 141
Cdd:cd02000   1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  142 GCAKGKGGSMHM--YTKNFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFI 219
Cdd:cd02000  81 GPCKGRGGSMHIgdKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  220 CENNLYGMGTSTERAAASPDYYKRG--NFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGV 297
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAaaYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 4885543  298 SYRTREEIQEvRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFA 351
Cdd:cd02000 241 RYRTKEEVEE-WKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
63-360 1.91e-151

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: 429.44  E-value: 1.91e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543     63 YRMMlTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSILAELTGRRGg 142
Cdd:pfam00676   1 RRMM-TLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVA- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    143 caKGKGGSMHMYTK----NFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVF 218
Cdd:pfam00676  79 --KGKGGSMHGYYGakgnRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    219 ICENNLYGMGTSTERAAASPDYYK--RGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPG 296
Cdd:pfam00676 157 VCENNQYGISTPAERASASTTYADraRGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDP 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4885543    297 VSYRTREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLE 360
Cdd:pfam00676 237 STYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
42-368 3.80e-146

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: 418.01  E-value: 3.80e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   42 YLLEEGPPVTTV-LTRAEGLKYYRMMLTVRRMELKADQLYKQKFIrGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHG 120
Cdd:COG1071   4 VLDPDGTEAALPdLSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  121 VCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTK--NFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAAN 198
Cdd:COG1071  83 HALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKelNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  199 QGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDYYKRGN-F-IPGLKVDGMDVLCVREATKFAANYCRSGKG 276
Cdd:COG1071 163 EGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAgYgIPGVRVDGNDVLAVYAAVKEAVERARAGEG 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  277 PILMELQTYRYHGHSMSDPGVSYRTREEIQEVRsKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPE 356
Cdd:COG1071 243 PTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWR-ERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPE 321
                       330
                ....*....|..
gi 4885543  357 PHLEELGHHIYS 368
Cdd:COG1071 322 PDPEELFDDVYA 333
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
53-373 9.85e-84

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 261.80  E-value: 9.85e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    53 VLTRAEGLKYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSI 132
Cdd:PLN02374  82 LVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAV 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   133 LAELTGRRGGCAKGKGGSMHMYTK--NFYGGNGIVGAQGPLGAGIALACKYK-------GNDEICLTLYGDGAANQGQIA 203
Cdd:PLN02374 162 MSELFGKATGCCRGQGGSMHMFSKehNLLGGFAFIGEGIPVATGAAFSSKYRrevlkeeSCDDVTLAFFGDGTCNNGQFF 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   204 EAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDYYKRGNF--IPGLKVDGMDVLCVREATKFAANYCRSGKGPILME 281
Cdd:PLN02374 242 ECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAfgMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVE 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   282 LQTYRYHGHSMSDPGvsyRTREEIQEVR-SKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLE 360
Cdd:PLN02374 322 CETYRFRGHSLADPD---ELRDPAEKAHyAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPRS 398
                        330
                 ....*....|...
gi 4885543   361 ELGHHIYSSDSSF 373
Cdd:PLN02374 399 QLLENVFADPKGF 411
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
54-369 5.48e-82

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 254.41  E-value: 5.48e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543    54 LTRAEGLKYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSIL 133
Cdd:CHL00149  17 INSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   134 AELTGRRGGCAKGKGGSMHMYTK--NFYGGNGIVGAQGPLGAGIALACKYKGN-----DEICLT--LYGDGAANQGQIAE 204
Cdd:CHL00149  97 AELFGKETGCSRGRGGSMHIFSAphNFLGGFAFIGEGIPIALGAAFQSIYRQQvlkevQPLRVTacFFGDGTTNNGQFFE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   205 AFNMAALWKLPCVFICENNLYGMGTSTERAAASPDYYKRGNF--IPGLKVDGMDVLCVREATKFAANYCRSGKGPILMEL 282
Cdd:CHL00149 177 CLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAfgLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEA 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543   283 QTYRYHGHSMSDPGvSYRTREEiQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLEEL 362
Cdd:CHL00149 257 LTYRFRGHSLADPD-ELRSKQE-KEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDL 334

                 ....*..
gi 4885543   363 GHHIYSS 369
Cdd:CHL00149 335 KKYLFAD 341
TPP_E1_OGDC_like cd02016
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ...
167-294 7.61e-08

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: 52.92  E-value: 7.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  167 AQGPLGAGIALACKYKGNDE-----ICLTLYGDGA-ANQGQIAEAFNMaalWKLP------CVFICENNLYGMGTSTERA 234
Cdd:cd02016 117 AVNPVVMGKTRAKQDYRGDGerdkvLPILIHGDAAfAGQGVVYETLNL---SNLPgyttggTIHIVVNNQIGFTTDPRDS 193
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4885543  235 AASPdyY----KRGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSD 294
Cdd:cd02016 194 RSSP--YctdvAKMIGAPIFHVNGDDPEAVVRATRLALEYRQKFKKDVVIDLVCYRRHGHNELD 255
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
163-294 8.44e-08

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: 52.89  E-value: 8.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885543  163 GIVGAQGPLG------AGIALACKYKG--NDEICLTlyGDGAANQGQIAEAFNMAALWKLP--CVFICENNLyGMGTSTE 232
Cdd:cd02012  99 GVEVTTGSLGqglsvaVGMALAEKLLGfdYRVYVLL--GDGELQEGSVWEAASFAGHYKLDnlIAIVDSNRI-QIDGPTD 175
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4885543  233 RAAASPDYYKR----G-NFIpglKVDGMDVLCVREA-TKFAANY-------CRS--GKGPILMElQTYRYHGHSMSD 294
Cdd:cd02012 176 DILFTEDLAKKfeafGwNVI---EVDGHDVEEILAAlEEAKKSKgkptliiAKTikGKGVPFME-NTAKWHGKPLGE 248
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
158-223 8.78e-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: 36.80  E-value: 8.78e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4885543  158 FYGGNGIvGAQGPLGAGIALACkyKGNDEICLTlyGDGAANqgqiaeaFNMAALW-----KLPCVFICENN 223
Cdd:cd02002  45 TLRGGGL-GWGLPAAVGAALAN--PDRKVVAII--GDGSFM-------YTIQALWtaaryGLPVTVVILNN 103
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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