Function and Biology Details
Reactions catalysed:
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O
NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- Flavoprotein pyridine nucleotide cytochrome reductase
- Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
- Oxidoreductase FAD/NAD(P)-binding
- NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily
- Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding
- Riboflavin synthase-like beta-barrel
- FAD-binding domain, ferredoxin reductase-type
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147079 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional cytochrome P450/NADPH--P450 reductase
Molecule details ›
Chains: A, B
Length: 391 amino acids
Theoretical weight: 43.8 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 391 amino acids
Theoretical weight: 43.8 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
- Canonical:
P14779 (Residues: 659-1049; Coverage: 37%)
Sequence domains:
Structure domains:
