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
- Peripheral subunit-binding domain
- E3-binding domain superfamily
- 2-oxo acid dehydrogenase, lipoyl-binding site
- Single hybrid motif
- 2-oxoacid dehydrogenase acyltransferase, catalytic domain
- Chloramphenicol acetyltransferase-like domain superfamily
- Dihydrolipoamide acetyltransferase/Pyruvate dehydrogenase protein X component
1 more domain
Structure analysis Details
Assembly composition:
homo 60-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-240748 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Molecule details ›
Chains: 01, 02, 03, 04, 05, 0z, 1a, 1b, 1c, 1d, 1e, 1f, 1g, 1h, 1i, 1j, 1k, 1l, 1m, 1n, 1o, 1p, 1q, 1r, 1s, 1t, 1u, 1v, 1w, 1x, 1z, 2a, 2b, 2c, 2d, 2e, 2f, 2g, 2h, 2i, 2j, 2k, 2l, 2m, 2n, 2o, 2p, 2q, 2r, 2s, 2t, 2u, 2v, 2w, 2x, 2y, 2z, 3a, 3b, 3c
Length: 647 amino acids
Theoretical weight: 69.14 KDa
Source organism: Bos taurus
UniProt:
Length: 647 amino acids
Theoretical weight: 69.14 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P11180 (Residues: 1-647; Coverage: 100%)
