Function and Biology Details
Reaction catalysed:
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
- Glutathione reductase/thioredoxin reductase-like
- Thioredoxin/glutathione reductase selenoprotein
- Pyridine nucleotide-disulphide oxidoreductase, class I
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Thioredoxin reductase 1, mitochondrial (preferred)
PDBe Complex ID:
PDB-CPX-161051 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin reductase 1, mitochondrial
Molecule details ›
Chain: X
Length: 488 amino acids
Theoretical weight: 52.99 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 488 amino acids
Theoretical weight: 52.99 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
- Canonical:
P91938 (Residues: 106-593; Coverage: 82%)
Sequence domains:
- FAD binding domain
- Pyridine nucleotide-disulphide oxidoreductase
- Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
