PROSITE documentation PDOC00674

Oxygen oxidoreductases covalent FAD-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-α-(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-γ-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.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

OX2_COVAL_FAD, PS00862; Oxygen oxidoreductases covalent FAD-binding site  (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
• Retrieve an alignment of Swiss-Prot true positive hits:
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• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00862
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00862
• Scan Swiss-Prot/TrEMBL entries against PS00862
• view ligand binding statistics
Matching PDB structures: 1W1O 1W1Q 1W1R 1W1S ... [ALL]

References

1 Authors Brandsch R., Hinkkanen A.E., Mauch L., Nagursky H., Decker K.
Title 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase.
Source Eur. J. Biochem. 167:315-320(1987).
PubMed ID 3622516
2 Authors Dittrich H., Kutchan T.M.
Title 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.
Source Proc. Natl. Acad. Sci. U.S.A. 88:9969-9973(1991).
PubMed ID 1946465
3 Authors Koshizaka T., Nishikimi M., Ozawa T., Yagi K.
Title Isolation and sequence analysis of a complementary DNA encoding rat liver L-gulono-gamma-lactone oxidase, a key enzyme for L-ascorbic acid biosynthesis.
Source J. Biol. Chem. 263:1619-1621(1988).
PubMed ID 3338984
4 Authors 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.
Title D-erythroascorbic acid is an important antioxidant molecule in Saccharomyces cerevisiae.
Source Mol. Microbiol. 30:895-903(1998).
PubMed ID 10094636
5 Authors August P.R., Flickinger M.C., Sherman D.H.
Title Cloning and analysis of a locus (mcr) involved in mitomycin C resistance in Streptomyces lavendulae.
Source J. Bacteriol. 176:4448-4454(1994).
PubMed ID 7517396

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