Function and Biology Details
Reactions catalysed:
Xanthine + H(2)O + O(2) = urate + H(2)O(2)
Xanthine + NAD(+) + H(2)O = urate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- FAD-binding, type PCMH-like superfamily
- CO dehydrogenase flavoprotein, C-terminal domain superfamily
- Aldehyde oxidase/xanthine dehydrogenase
- Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain superfamily
- 2Fe-2S ferredoxin-like superfamily
- [2Fe-2S]-binding domain superfamily
- Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead superfamily
- Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead
6 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xanthine dehydrogenase/oxidase
Molecule details ›
Chains: A, B
Length: 1332 amino acids
Theoretical weight: 146.99 KDa
Source organism: Bos taurus
UniProt:
Sequence domains:
Length: 1332 amino acids
Theoretical weight: 146.99 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P80457 (Residues: 1-1332; Coverage: 100%)
Sequence domains:
- [2Fe-2S] binding domain
- Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain
- FAD binding domain in molybdopterin dehydrogenase
- Molybdopterin cofactor-binding domain
- Molybdopterin cofactor-binding domain
- CO dehydrogenase flavoprotein C-terminal domain
- 2Fe-2S iron-sulfur cluster binding domain
- Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
- Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain
- Ubiquitin-like (UB roll)
- Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2
- Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead
- CO dehydrogenase flavoprotein, C-terminal domain
- [2Fe-2S]-binding domain
