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:
Sequence domains:
- FAD/NAD(P)-binding domain superfamily
- Thioredoxin domain
- FAD/NAD-linked reductase, dimerisation domain superfamily
- Thioredoxin
- Thioredoxin-like superfamily
- Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
- Pyridine nucleotide-disulphide oxidoreductase, class I, active site
- FAD/NAD(P)-binding domain
3 more domains
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145352 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thioredoxin reductase 1, cytoplasmic
Molecule details ›
Chains: A, B
Length: 519 amino acids
Theoretical weight: 56.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt: Gene names: GRIM12, KDRF, TXNRD1
Sequence domains:
Length: 519 amino acids
Theoretical weight: 56.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt: Gene names: GRIM12, KDRF, TXNRD1
Sequence domains:
- Pyridine nucleotide-disulphide oxidoreductase
- Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
Thioredoxin
Molecule details ›
Chains: C, D
Length: 116 amino acids
Theoretical weight: 12.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin
Length: 116 amino acids
Theoretical weight: 12.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P10599 (Residues: 2-105; Coverage: 99%)
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin
