Function and Biology Details
Reaction catalysed:
NADPH + NAD(+) + H(+)(Side 1) = NADP(+) + H(+)(Side 2) + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Alanine dehydrogenase/pyridine nucleotide transhydrogenase, NAD(H)-binding domain
- Alanine dehydrogenase/pyridine nucleotide transhydrogenase, N-terminal
- Alanine dehydrogenase/pyridine nucleotide transhydrogenase, conserved site-2
- NAD(P)-binding domain superfamily
- Alanine dehydrogenase/NAD(P) transhydrogenase, conserved site-1
- NADP transhydrogenase beta-like domain
- DHS-like NAD/FAD-binding domain superfamily
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
NAD(P) transhydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-173910 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NAD(P) transhydrogenase subunit alpha part 1
Molecule details ›
Chains: A, B
Length: 381 amino acids
Theoretical weight: 40.07 KDa
Source organism: Rhodospirillum rubrum
UniProt:
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain
Length: 381 amino acids
Theoretical weight: 40.07 KDa
Source organism: Rhodospirillum rubrum
UniProt:
- Canonical:
Q2RSB2 (Residues: 1-381; Coverage: 99%)
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain
NAD(P) transhydrogenase subunit beta
Molecule details ›
Chain: C
Length: 174 amino acids
Theoretical weight: 18.75 KDa
Source organism: Rhodospirillum rubrum
UniProt:
Sequence domains: NAD(P) transhydrogenase beta subunit
Structure domains: TPP-binding domain
Length: 174 amino acids
Theoretical weight: 18.75 KDa
Source organism: Rhodospirillum rubrum
UniProt:
- Canonical: Q2RSB4 (Residues: 291-464; Coverage: 38%)
Sequence domains: NAD(P) transhydrogenase beta subunit
Structure domains: TPP-binding domain
