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InterPro: IPR006181 D-amino acid oxidase, conserved site

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UniProtKB

Matches:

216 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

IPR006181 D-amino_acid_oxidase_CS

Secondary

IPR000927

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00677	DAO	216
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006076 FAD dependent oxidoreductase
IPR016040 NAD(P)-binding domain

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0003884 D-amino-acid oxidase activity

InterPro annotation

Entry Details in BioMart

Abstract

D-amino acid oxidase (EC:1.4.3.3) (DAMOX or DAO) is an FAD flavoenzyme that catalyzes the oxidation of neutral and basic D-amino acids into their corresponding keto acids. DAOs have been characterised and sequenced in fungi and vertebrates where they are known to be located in the peroxisomes. D-aspartate oxidase (EC:1.4.3.1) (DASOX) [1] is an enzyme, structurally related to DAO, which catalyzes the same reaction but is active only toward dicarboxylic D-amino acids. In DAO, a conserved histidine has been shown [2] to be important for the enzyme's catalytic activity.

Structural links Help

PDB - click here

SCOP: c.4.1.2

CATH: 3.40.50.720

Database links Help

PDBe-motif: PS00677

Enzyme: EC:1.4.3

PROSITE doc: PDOC00573

Blocks: IPB006181

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006181

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O01739 Putative D-amino-acid oxidase 1

P00371 D-amino-acid oxidase

P14920 D-amino-acid oxidase

P18894 D-amino-acid oxidase

P80324 D-amino-acid oxidase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006076	FAD dependent oxidoreductase
IPR006181	D-amino acid oxidase, conserved site
IPR016040	NAD(P)-binding domain
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Negri A, Ceciliani F, Tedeschi G, Simonic T, Ronchi S. The primary structure of the flavoprotein D-aspartate oxidase from beef kidney. J. Biol. Chem. 267 11865-71 1992 [PubMed: 1601857] http://intl.jbc.org/cgi/reprint/267/17/11865.pdf
2.	Miyano M, Fukui K, Watanabe F, Takahashi S, Tada M, Kanashiro M, Miyake Y. Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization. J. Biochem. 109 171-7 1991 [PubMed: 1673125] http://jb.oxfordjournals.org/cgi/content/abstract/109/1/171

Additional Reading Open in usermanual
	Kawazoe T, Tsuge H, Imagawa T, Aki K, Kuramitsu S, Fukui K. Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis. Biochem. Biophys. Res. Commun. 355 2007 385-91 [PubMed: 17303072] http://dx.doi.org/10.1016/j.bbrc.2007.01.181
	Kawazoe T, Tsuge H, Pilone MS, Fukui K. Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. Protein Sci. 15 2006 2708-17 [PubMed: 17088322] http://dx.doi.org/10.1110/ps.062421606
	Pollegioni L, Diederichs K, Molla G, Umhau S, Welte W, Ghisla S, Pilone MS. Yeast D-amino acid oxidase: structural basis of its catalytic properties. J. Mol. Biol. 324 2002 535-46 [PubMed: 12445787] http://dx.doi.org/10.1016/S0022-2836(02)01062-8
	Umhau S, Pollegioni L, Molla G, Diederichs K, Welte W, Pilone MS, Ghisla S. The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation. Proc. Natl. Acad. Sci. U.S.A. 97 2000 12463-8 [PubMed: 11070076] http://dx.doi.org/10.1073/pnas.97.23.12463
	Mizutani H, Miyahara I, Hirotsu K, Nishina Y, Shiga K, Setoyama C, Miura R. Three-dimensional structure of the purple intermediate of porcine kidney D-amino acid oxidase. Optimization of the oxidative half-reaction through alignment of the product with reduced flavin. J. Biochem. 128 2000 73-81 [PubMed: 10876160] http://jb.oxfordjournals.org/cgi/content/abstract/128/1/73

InterPro 23.1