Function and Biology Details
Reaction catalysed:
Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- FAD/NAD(P)-binding domain superfamily
- FAD/NAD-linked reductase, dimerisation domain superfamily
- Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
- Pyridine nucleotide-disulphide oxidoreductase, class I, active site
- FAD/NAD(P)-binding domain
- Dihydrolipoamide dehydrogenase
- Pyridine nucleotide-disulphide oxidoreductase, class I
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Dihydrolipoyl dehydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-161554 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyl dehydrogenase
Molecule details ›
Chains: A, B, C, D
Length: 466 amino acids
Theoretical weight: 49.44 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 466 amino acids
Theoretical weight: 49.44 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P9WHH9 (Residues: 1-464; Coverage: 100%)
Sequence domains:
- FAD dependent oxidoreductase
- Pyridine nucleotide-disulphide oxidoreductase
- Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
