| Description | This entry represents the conserved region around the histidine that binds the FAD group, which is conserved in these enzymes.Some oxygen-dependent oxidoreductases are flavoproteins that contain 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 1.5.3.6) (6-HDNO) [ ], a bacterial enzyme that catalyzes the oxygen-dependent degradation of 6-hydroxynicotine into 6-hydroxypyrid-N-methylosmine.Plant reticuline oxidase (EC 1.21.3.3) [ ] (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 1.1.3.8) (l-gulono-gamma-lactone oxidase) [ ], 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 1.1.3.24) (L-galactonolactone oxidase), a yeast enzyme involved in the biosynthesis of D-erythroascorbic acid [ ].Mitomycin radical oxidase [ ], a bacterial protein involved in mitomycin resistance and that probably oxidizes the reduced form of mitomycins.Cytokinin oxidase (EC 1.4.3.18), a plant enzyme.Rhodococcus fascians fasciation locus protein fas5. | Name | Oxygen oxidoreductase covalent FAD-binding site |
| Short Name | Oxy_OxRdtase_FAD_BS | Type | Binding_site |
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