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InterPro: IPR006076 FAD dependent oxidoreductase

Protein matches Help

UniProtKB

Matches:

15891 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
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

IPR006076 FAD-dep_OxRdtase

Secondary

IPR000927

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01266	DAO	15891
Signatures in BioMart

InterPro Relationships Help

Children

IPR000447 FAD-dependent glycerol-3-phosphate dehydrogenase
IPR017610 tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal

Found in

IPR004379 UDP-galactopyranose mutase
IPR006277 Sarcosine oxidase, alpha subunit, heterotetrameric
IPR006278 Sarcosine oxidase, beta subunit, heterotetrameric
IPR006281 Sarcosine oxidase, monomeric
IPR010971 Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6
IPR011295 2-polyprenyl-6-methoxyphenol 4-hydroxylase
IPR011803 Adenylylsulphate reductase, alpha subunit
IPR012727 Glycine oxidase ThiO
IPR012814 Pyranose oxidase
IPR014101 Carotene isomerase
IPR014104 Myxoxanthophyll biosynthesis, C-3',4' desaturase CrtD
IPR015657 Aminobutyraldehyde dehydrogenase
IPR017631 Salicylate 1-monooxygenase
IPR017715 Putative aminophosphonate oxidoreductase
IPR017741 FAD-dependent oxidoreductase, HpnW

Contains

IPR006181 D-amino acid oxidase, conserved site

GO Term annotation Help

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase (EC:1.1.99.5), Sarcosine oxidase beta subunit (EC:1.5.3.1), D-alanine oxidase (EC:1.4.99.1), D-aspartate oxidase (EC:1.4.3.1).

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.3.1.2 , c.3.1.4 , c.3.1.5 , c.4.1.2 , c.4.1.3 , d.16.1.3 , d.16.1.5

CATH: 3.30.9.10 , 3.40.50.720 , 3.50.50.60

Database links Help

Enzyme: EC:1

PANDIT: PF01266

Pfam Clan: CL0063.21

AC	CL0063.21
ID	NADP_Rossmann
DE	FAD/NAD(P)-binding Rossmann fold Superfamily
PF00044	IPR020828	Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
PF00056	IPR001236	Lactate/malate dehydrogenase
PF00070	IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PF00106	IPR002198	Short-chain dehydrogenase/reductase SDR
PF00107	IPR013149	Alcohol dehydrogenase, zinc-binding
PF00208	IPR006096	Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal
PF00479	IPR001282	Glucose-6-phosphate dehydrogenase
PF00670	IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding
PF00732	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
PF00743	IPR000960	Flavin-containing monooxygenase FMO
PF00890	IPR003953	Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00899	IPR000594	UBA/THIF-type NAD/FAD binding fold
PF00996	IPR018203	GDP dissociation inhibitor
PF01073	IPR002225	3-beta hydroxysteroid dehydrogenase/isomerase
PF01113	IPR000846	Dihydrodipicolinate reductase
PF01118	IPR000534	Semialdehyde dehydrogenase, NAD-binding
PF01134	IPR002218	Glucose-inhibited division protein A-related
PF01210	IPR011128	NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
PF01225	IPR000713	Mur ligase, N-terminal
PF01232	IPR013131	Mannitol dehydrogenase, N-terminal
PF01262	IPR007698	Alanine dehydrogenase/PNT, C-terminal
PF01266	IPR006076	FAD dependent oxidoreductase
PF01370	IPR001509	NAD-dependent epimerase/dehydratase
PF01408	IPR000683	Oxidoreductase, N-terminal
PF01488	IPR006151	Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
PF01494	IPR002938	Monooxygenase, FAD-binding
PF01593	IPR002937	Amine oxidase
PF01946	IPR002922	Thiamine biosynthesis Thi4 protein
PF02153	IPR003099	Prephenate dehydrogenase
PF02254	IPR003148	Regulator of K+ conductance, N-terminal
PF02423	IPR003462	Ornithine cyclodeaminase/mu-crystallin
PF02558	IPR013332	Ketopantoate reductase ApbA/PanE, N-terminal
PF02629	IPR003781	CoA-binding
PF02670	IPR013512	1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
PF02719	IPR003869	Polysaccharide biosynthesis protein CapD-like
PF02737	IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding
PF02826	IPR006140	D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02882	IPR020631	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
PF03435	IPR005097	Saccharopine dehydrogenase
PF03446	IPR006115	6-phosphogluconate dehydrogenase, NAD-binding
PF03447	IPR005106	Aspartate/homoserine dehydrogenase, NAD-binding
PF03486	IPR004792	HI0933-like protein
PF03721	IPR001732	UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03807	IPR004455	NADP oxidoreductase, coenzyme F420-dependent
PF03949	IPR012302	Malic enzyme, NAD-binding
PF04321	IPR005913	dTDP-4-dehydrorhamnose reductase
PF04723	IPR006812	Glycine reductase complex selenoprotein A
PF04820	IPR006905	Tryptophan halogenase
PF05368	IPR008030	NmrA-like
PF05834	IPR008671	Lycopene beta/epsilon cyclase
PF06039	IPR006231	Malate:quinone-oxidoreductase
PF07157	IPR009826	DNA circulation, N-terminal
PF07991	IPR013116	Acetohydroxy acid isomeroreductase, catalytic
PF07992	IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PF07993	IPR013120	Male sterility, NAD-binding
PF07994	IPR002587	Myo-inositol-1-phosphate synthase
PF08491	IPR013698	Squalene epoxidase
PF08659	IPR013968	Polyketide synthase, KR
PF10727	IPR019665	Putative oxidoreductase/dehydrogenase, Rossmann-like domain

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006076

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O01739 Putative D-amino-acid oxidase 1

O65402 Squalene monooxygenase 1,2

P14920 D-amino-acid oxidase

P18894 D-amino-acid oxidase

P32191 Glycerol-3-phosphate dehydrogenase, mitochondrial

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
IPR013698	Squalene epoxidase
IPR003042	Aromatic-ring hydroxylase-like
IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
	SWISS-MODEL
	PDB Chain
	ModBase
	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
	Schiffer A, Fritz G, Kroneck PM, Ermler U. Reaction mechanism of the iron-sulfur flavoenzyme adenosine-5'-phosphosulfate reductase based on the structural characterization of different enzymatic states. Biochemistry 45 2006 2960-7 [PubMed: 16503650] http://dx.doi.org/10.1021/bi0521689
	Hassan-Abdallah A, Zhao G, Chen ZW, Mathews FS, Schuman Jorns M. Arginine 49 is a bifunctional residue important in catalysis and biosynthesis of monomeric sarcosine oxidase: a context-sensitive model for the electrostatic impact of arginine to lysine mutations. Biochemistry 47 2008 2913-22 [PubMed: 18251505] http://dx.doi.org/10.1021/bi702351v
	Ilari A, Bonamore A, Franceschini S, Fiorillo A, Boffi A, Colotti G. The X-ray structure of N-methyltryptophan oxidase reveals the structural determinants of substrate specificity. Proteins 71 2008 2065-75 [PubMed: 18186483] http://dx.doi.org/10.1002/prot.21898
	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
	Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A. Active site plasticity in D-amino acid oxidase: a crystallographic analysis. Biochemistry 36 1997 5853-60 [PubMed: 9153426] http://dx.doi.org/10.1021/bi9630570

InterPro 23.1