Function and Biology Details
Reactions catalysed:
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2)
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II
- Transketolase-like, pyrimidine-binding domain
- Thiamin diphosphate-binding fold
- Peripheral subunit-binding domain
- E3-binding domain superfamily
- Biotin/lipoyl attachment
- Transketolase, C-terminal domain
- Dehydrogenase, E1 component
5 more domains
Structure analysis Details
Assembly composition:
hetero pentamer (preferred)
PDBe Complex ID:
PDB-CPX-146012 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Pyruvate dehydrogenase E1 component subunit alpha
Molecule details ›
Chains: A, C, E, G
Length: 369 amino acids
Theoretical weight: 41.52 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
Sequence domains: Dehydrogenase E1 component
Structure domains: Rossmann fold
Length: 369 amino acids
Theoretical weight: 41.52 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
- Canonical:
P21873 (Residues: 1-369; Coverage: 100%)
Sequence domains: Dehydrogenase E1 component
Structure domains: Rossmann fold
Pyruvate dehydrogenase E1 component subunit beta
Molecule details ›
Chains: B, D, F, H
Length: 325 amino acids
Theoretical weight: 35.5 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 325 amino acids
Theoretical weight: 35.5 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
- Canonical: P21874 (Residues: 1-325; Coverage: 100%)
Sequence domains:
Structure domains:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Molecule details ›
Chains: I, J
Length: 428 amino acids
Theoretical weight: 46.39 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 428 amino acids
Theoretical weight: 46.39 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
- Canonical: P11961 (Residues: 1-428; Coverage: 100%)
Sequence domains:
- Biotin-requiring enzyme
- e3 binding domain
- 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
