Function and Biology Details
Reaction catalysed:
Caffeine + O(2) + NAD(P)H = theobromine + NAD(P)(+) + H(2)O + formaldehyde
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Rieske [2Fe-2S] iron-sulphur domain
- Rieske [2Fe-2S] iron-sulphur domain superfamily
- 2Fe-2S ferredoxin-type iron-sulfur binding domain
- Vanillate O-demethylase oxygenase-like, C-terminal catalytic domain
- 2Fe-2S ferredoxin, iron-sulphur binding site
- 2Fe-2S ferredoxin-like superfamily
- Beta-grasp domain superfamily
Structure analysis Details
Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124961 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Methylxanthine N1-demethylase NdmA
Molecule details ›
Chains: A, B, C
Length: 369 amino acids
Theoretical weight: 42.38 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 369 amino acids
Theoretical weight: 42.38 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
H9N289 (Residues: 1-351; Coverage: 100%)
Sequence domains:
Oxidoreductase NdmD
Molecule details ›
Chain: D
Length: 87 amino acids
Theoretical weight: 9.66 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: 2Fe-2S iron-sulfur cluster binding domain
Length: 87 amino acids
Theoretical weight: 9.66 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: H9N291 (Residues: 502-588; Coverage: 15%)
Sequence domains: 2Fe-2S iron-sulfur cluster binding domain
