Function and Biology Details
Reaction catalysed:
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Biotin/lipoyl attachment
- 2-oxo acid dehydrogenase, lipoyl-binding site
- Single hybrid motif
- Peripheral subunit-binding domain
- E3-binding domain superfamily
- 2-oxoacid dehydrogenase acyltransferase, catalytic domain
- Chloramphenicol acetyltransferase-like domain superfamily
- Dihydrolipoamide acetyltransferase pyruvate dehydrogenase complex
Structure analysis Details
Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139312 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 630 amino acids
Theoretical weight: 66.36 KDa
Source organism: Escherichia coli K-12
UniProt:
Sequence domains:
Length: 630 amino acids
Theoretical weight: 66.36 KDa
Source organism: Escherichia coli K-12
UniProt:
- Canonical:
P06959 (Residues: 1-630; Coverage: 100%)
Sequence domains:
