Q54C70 · ODPA_DICDI
- ProteinPyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- GenepdhA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids377 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic activity
- N6-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate + H+ = N6-[(R)-S8-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Cofactor
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Activity regulation
E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 83 | pyruvate (UniProtKB | ChEBI) | |||
Binding site | 109 | pyruvate (UniProtKB | ChEBI) | |||
Binding site | 109 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | |||
Binding site | 110 | pyruvate (UniProtKB | ChEBI) | |||
Binding site | 110 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | |||
Binding site | 156 | pyruvate (UniProtKB | ChEBI) | |||
Binding site | 156 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | |||
Binding site | 158 | pyruvate (UniProtKB | ChEBI) | |||
Binding site | 158 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | |||
Binding site | 187 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 187 | pyruvate (UniProtKB | ChEBI) | |||
Binding site | 187 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | |||
Binding site | 188 | pyruvate (UniProtKB | ChEBI) | |||
Binding site | 188 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | |||
Binding site | 189 | pyruvate (UniProtKB | ChEBI) | |||
Binding site | 189 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | |||
Binding site | 216 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 216 | pyruvate (UniProtKB | ChEBI) | |||
Binding site | 216 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | |||
Binding site | 218 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 218 | pyruvate (UniProtKB | ChEBI) | |||
Binding site | 283 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | phagocytic vesicle | |
Cellular Component | pyruvate dehydrogenase complex | |
Molecular Function | metal ion binding | |
Molecular Function | pyruvate dehydrogenase (acetyl-transferring) activity | |
Biological Process | acetyl-CoA biosynthetic process from pyruvate |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- EC number
- Short namesPDHE1-A
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Amoebozoa > Evosea > Eumycetozoa > Dictyostelia > Dictyosteliales > Dictyosteliaceae > Dictyostelium
Accessions
- Primary accessionQ54C70
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-26 | Mitochondrion | |||
Chain | PRO_0000327983 | 27-377 | Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial | ||
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length377
- Mass (Da)41,988
- Last updated2005-05-24 v1
- MD5 Checksum102DBCCC72FBF95F35764F159AE0F2C8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAFI02000199 EMBL· GenBank· DDBJ | EAL60849.1 EMBL· GenBank· DDBJ | Genomic DNA |