{PDOC00674} {PS00862; OX2_COVAL_FAD} {BEGIN} **************************************************** * Oxygen oxidoreductases covalent FAD-binding site * **************************************************** 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 are: - (R)-6-hydroxynicotine oxidase (EC 1.5.3.6) (6-HDNO) [1], 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) [2] (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) [3], 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 [4]. - Mitomycin radical oxidase [5], 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. The region around the histidine that binds the FAD group is conserved in these enzymes and can be used as a signature pattern. -Consensus pattern: P-x(7)-{L}-x(2)-[DE]-[LIVM]-x(3)-[LIVM]-x(9,12)-[LIVM]- x(3)-[GSA]-[GSTCHRQ]-G-H [H is the FAD binding site] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: 1. -Last update: April 2006 / Pattern revised. [ 1] Brandsch R., Hinkkanen A.E., Mauch L., Nagursky H., Decker K. "6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase." Eur. J. Biochem. 167:315-320(1987). PubMed=3622516 [ 2] Dittrich H., Kutchan T.M. "Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack." Proc. Natl. Acad. Sci. U.S.A. 88:9969-9973(1991). PubMed=1946465 [ 3] Koshizaka T., Nishikimi M., Ozawa T., Yagi K. "Isolation and sequence analysis of a complementary DNA encoding rat liver L-gulono-gamma-lactone oxidase, a key enzyme for L-ascorbic acid biosynthesis." J. Biol. Chem. 263:1619-1621(1988). PubMed=3338984 [ 4] Huh W.-K., Lee B.-H., Kim S.-T., Kim Y.-R., Rhie G.-E., Baek Y.-W., Hwang C.-S., Lee J.-S., Kang S.-O. "D-erythroascorbic acid is an important antioxidant molecule in Saccharomyces cerevisiae." Mol. Microbiol. 30:895-903(1998). PubMed=10094636 [ 5] August P.R., Flickinger M.C., Sherman D.H. "Cloning and analysis of a locus (mcr) involved in mitomycin C resistance in Streptomyces lavendulae." J. Bacteriol. 176:4448-4454(1994). PubMed=7517396 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}