Function and Biology Details
Reaction catalysed:
Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH
Biochemical function:
Biological process:
- not assigned
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-101698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyl dehydrogenase
Molecule details ›
Chains: A, B, C, D
Length: 481 amino acids
Theoretical weight: 50.51 KDa
Source organism: Pseudomonas aeruginosa UCBPP-PA14
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 481 amino acids
Theoretical weight: 50.51 KDa
Source organism: Pseudomonas aeruginosa UCBPP-PA14
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A0A0H2Z9F5 (Residues: 1-478; Coverage: 100%)
Sequence domains:
- Pyridine nucleotide-disulphide oxidoreductase
- Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
