Protein Domain : Oxygen oxidoreductase covalent FAD-binding site IPR006093

Type  Binding_site
Description  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 1.5.3.6) (6-HDNO) [ ], a bacterial enzymethat catalyzes the oxygen-dependent degradation of 6-hydroxynicotine into 6-hydroxypyrid-N-methylosmine.Plant reticuline oxidase (EC 1.21.3.3) [ ] (berberine-bridge-formingenzyme), 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 mitomycinresistance 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.This entry represents the conserved region around the histidine that binds the FAD group is conserved in these enzymes.
Short Name  Oxy_OxRdtase_FAD_BS

0 Child Features

0 Gene Families

768 Genes

1 Ontology Annotations

0 Parent Features

13 Publications

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