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| 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 |
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| 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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