Pathways & interactions
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 22.214.171.124) (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 126.96.36.199) [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 188.8.131.52) (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 184.108.40.206) (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 220.127.116.11), 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.
- PS00862 (OX2_COVAL_FAD)