Function and Biology Details
Reaction catalysed:
Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH
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
- Thioredoxin/glutathione reductase selenoprotein
- Glutathione reductase/thioredoxin reductase-like
- Glutaredoxin active site
4 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
thioredoxin-disulfide reductase (preferred)
PDBe Complex ID:
PDB-CPX-104927 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
thioredoxin-disulfide reductase
Molecule details ›
Chain: A
Length: 598 amino acids
Theoretical weight: 65.11 KDa
Source organism: Schistosoma mansoni
Expression system: Escherichia coli
UniProt:
Length: 598 amino acids
Theoretical weight: 65.11 KDa
Source organism: Schistosoma mansoni
Expression system: Escherichia coli
UniProt:
- Canonical:
A0A3Q0KFL1 (Residues: 35-630; Coverage: 95%)
