Function and Biology Details
Reaction catalysed:
Reduced putidaredoxin + NAD(+) = oxidized putidaredoxin + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Adrenodoxin-like
- 2Fe-2S ferredoxin-type iron-sulfur binding domain
- FAD/NAD(P)-binding domain superfamily
- FAD/NAD-linked reductase, dimerisation domain superfamily
- Adrenodoxin, iron-sulphur binding site
- 2Fe-2S ferredoxin-like superfamily
- Beta-grasp domain superfamily
- Reductase, C-terminal
1 more domain
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Putidaredoxin and Putidaredoxin reductase CamA (preferred)
PDBe Complex ID:
PDB-CPX-132341 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Putidaredoxin reductase CamA
Molecule details ›
Chains: A, B
Length: 436 amino acids
Theoretical weight: 47.27 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 436 amino acids
Theoretical weight: 47.27 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
- Canonical:
P16640 (Residues: 2-422; Coverage: 100%)
Sequence domains:
Structure domains:
Putidaredoxin
Molecule details ›
Chains: C, D
Length: 106 amino acids
Theoretical weight: 11.4 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
Sequence domains: 2Fe-2S iron-sulfur cluster binding domain
Structure domains: Ubiquitin-like (UB roll)
Length: 106 amino acids
Theoretical weight: 11.4 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
- Canonical: P00259 (Residues: 2-107; Coverage: 99%)
Sequence domains: 2Fe-2S iron-sulfur cluster binding domain
Structure domains: Ubiquitin-like (UB roll)
