Function and Biology Details
Reaction catalysed:
An aldehyde + H(2)O + O(2) = a carboxylate + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead
- CO dehydrogenase flavoprotein, C-terminal
- 2Fe-2S ferredoxin-type iron-sulfur binding domain
- Aldehyde oxidase/xanthine dehydrogenase-like
- Aldehyde oxidase/xanthine dehydrogenase, second molybdopterin binding domain
- Oxidoreductase, molybdopterin binding site
- Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain
- Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain superfamily
13 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Aldehyde oxidase (preferred)
PDBe Complex ID:
PDB-CPX-170321 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldehyde oxidase
Molecule details ›
Chain: A
Length: 1338 amino acids
Theoretical weight: 148.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 1338 amino acids
Theoretical weight: 148.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q06278 (Residues: 1-1338; Coverage: 100%)
Sequence domains:
- 2Fe-2S iron-sulfur cluster binding domain
- [2Fe-2S] binding domain
- FAD binding domain in molybdopterin dehydrogenase
- CO dehydrogenase flavoprotein C-terminal domain
- Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain
- Molybdopterin cofactor-binding domain
- Molybdopterin cofactor-binding domain
