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InterPro: IPR006093 Oxygen oxidoreductase covalent FAD-binding site

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UniProtKB

Matches:

489 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR006093 Oxy_OxRdtase_FAD_BS

Secondary

IPR001575

Type

Binding_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00862	OX2_COVAL_FAD	489
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006094 FAD linked oxidase, N-terminal
IPR010031 Sugar 1,4-lactone oxidase
IPR010032 FAD-linked oxidoreductase
IPR016166 FAD-binding, type 2

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

This signature contains a conserved histidine to which an FAD group is attached covalently via an 8-alpha-(N3-histidyl)-riboflavin linkage. Various enzymes use FAD as a co-factor, most of these enzymes are oxygen-dependent oxidoreductases. One of the enzymes Vanillyl-alcohol oxidase (VAO, EC:1.1.3.38) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110 [1]. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging from aromatic amines to 4-alkylphenols.

Other members include:

D-lactate dehydrogenase, this enzyme catalyses the conversion of D-lactate to pyruvate using FAD as a co-factor
mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance
MurB, an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan [2].

Structural links Help

PDB - click here

SCOP: d.145.1.1

Database links Help

PDBe-motif: PS00862

Enzyme: EC:1

PROSITE doc: PDOC00674

Blocks: IPB006093

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006093

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O22213 Cytokinin dehydrogenase 1

P08159 6-hydroxy-D-nicotine oxidase

P10867 L-gulonolactone oxidase

P54783 D-arabinono-1,4-lactone oxidase

P58710 L-gulonolactone oxidase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR007173	D-arabinono-1,4-lactone oxidase
IPR015345	Cytokinin dehydrogenase 1, FAD/cytokinin binding domain
IPR006093	Oxygen oxidoreductase covalent FAD-binding site
IPR016168	FAD-linked oxidase, FAD-binding, subdomain 2
IPR016166	FAD-binding, type 2
IPR006094	FAD linked oxidase, N-terminal
IPR016164	FAD-linked oxidase-like, C-terminal
IPR012951	Berberine/berberine-like
IPR010031	Sugar 1,4-lactone oxidase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A. Structural analysis of flavinylation in vanillyl-alcohol oxidase. J. Biol. Chem. 275 38654-8 2000 [PubMed: 10984479] http://dx.doi.org/10.1074/jbc.M004753200
2.	Benson TE, Walsh CT, Hogle JM. The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls. Structure 4 47-54 1996 [PubMed: 8805513] http://dx.doi.org/10.1016/S0969-2126(96)00008-1

Additional Reading Open in usermanual
	Dittrich H, Kutchan TM. 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 1991 9969-73 [PubMed: 1946465] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=1946465&action=stream&blobtype=pdf
	August PR, Flickinger MC, Sherman DH. Cloning and analysis of a locus (mcr) involved in mitomycin C resistance in Streptomyces lavendulae. J. Bacteriol. 176 1994 4448-54 [PubMed: 7517396] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=7517396&action=stream&blobtype=pdf
	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 1988 1619-21 [PubMed: 3338984] http://intl.jbc.org/cgi/reprint/263/4/1619.pdf
	Brandsch R, Hinkkanen AE, 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 1987 315-20 [PubMed: 3622516] http://dx.doi.org/10.1111/j.1432-1033.1987.tb13338.x
	Malito E, Coda A, Bilyeu KD, Fraaije MW, Mattevi A. Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis. J. Mol. Biol. 341 2004 1237-49 [PubMed: 15321719] http://dx.doi.org/10.1016/j.jmb.2004.06.083
	Huh WK, Lee BH, Kim ST, Kim YR, Rhie GE, Baek YW, Hwang CS, Lee JS, Kang SO. D-Erythroascorbic acid is an important antioxidant molecule in Saccharomyces cerevisiae. Mol. Microbiol. 30 1998 895-903 [PubMed: 10094636] http://dx.doi.org/10.1046/j.1365-2958.1998.01133.x

InterPro 24.0