Function and Biology Details
Reaction catalysed:
2 reduced [2Fe-2S] ferredoxin + NAD(+) + H(+) = 2 oxidized [2Fe-2S] ferredoxin + NADH
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Flavoprotein pyridine nucleotide cytochrome reductase
- 2Fe-2S ferredoxin-type iron-sulfur binding domain
- Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
- Beta-grasp domain superfamily
- 2Fe-2S ferredoxin, iron-sulphur binding site
- Riboflavin synthase-like beta-barrel
- Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
- Oxidoreductase FAD/NAD(P)-binding
2 more domains
Structure analysis Details
Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Toluene-4-monooxygenase system, ferredoxin--NAD(+) reductase component
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 35.89 KDa
Source organism: Pseudomonas mendocina
Expression system: Escherichia coli BL21
UniProt:
Sequence domains:
Length: 326 amino acids
Theoretical weight: 35.89 KDa
Source organism: Pseudomonas mendocina
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q03304 (Residues: 2-326; Coverage: 100%)
Sequence domains:
- Oxidoreductase NAD-binding domain
- Oxidoreductase FAD-binding domain
- 2Fe-2S iron-sulfur cluster binding domain
