Function and Biology Details
Reactions catalysed:
NADPH + H(2)O(2) = NADP(+) + 2 H(2)O
Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
- not assigned
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
- Pyridine nucleotide-disulphide oxidoreductase, class I
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Thioredoxin reductase 1, cytoplasmic (preferred)
PDBe Complex ID:
PDB-CPX-172612 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin reductase 1, cytoplasmic
Molecule details ›
Chains: A, B, C, D
Length: 513 amino acids
Theoretical weight: 56.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt: Gene names: GRIM12, KDRF, TXNRD1
Sequence domains:
Length: 513 amino acids
Theoretical weight: 56.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt: Gene names: GRIM12, KDRF, TXNRD1
Q16881Sequence domains:
- Pyridine nucleotide-disulphide oxidoreductase
- Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
