Binding Site

Oxygen oxidoreductase covalent FAD-binding site (IPR006093)

Short name: Oxy_OxRdtase_FAD_BS


Some oxygen-dependent oxidoreductases are flavoproteins that contains a covalently bound FAD group which is attached to a histidine via an 8-alpha- (N3-histidyl)-riboflavin linkage. These proteins include:

  • (R)-6-hydroxynicotine oxidase (EC (6-HDNO) [PMID: 3622516], a bacterial enzyme that catalyzes the oxygen-dependent degradation of 6-hydroxynicotine into 6-hydroxypyrid-N-methylosmine.
  • Plant reticuline oxidase (EC [PMID: 1946465] (berberine-bridge-forming enzyme), an enzyme that catalyzes the oxidation of (S)-reticuline into (S)- scoulerine in the pathway leading to benzophenanthridine alkaloids.
  • L-gulonolactone oxidase (EC (l-gulono-gamma-lactone oxidase) [PMID: 3338984], a mammalian enzyme which catalyzes the oxidation of L-gulono-1,4-lactone to L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
  • D-arabinono-1,4-lactone oxidase (EC (L-galactonolactone oxidase), a yeast enzyme involved in the biosynthesis of D-erythroascorbic acid [PMID: 10094636].
  • Mitomycin radical oxidase [PMID: 7517396], a bacterial protein involved in mitomycin resistance and that probably oxidizes the reduced form of mitomycins.
  • Cytokinin oxidase (EC, a plant enzyme.
  • Rhodococcus fascians fasciation locus protein fas5.

This entry represents the conserved region around the histidine that binds the FAD group is conserved in these enzymes.

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0016491 oxidoreductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns