Reviewed, UniProtKB/Swiss-Prot P00371 (OXDA_PIG)

Names and origin

Protein names

Recommended name:
    D-amino-acid oxidase
      Short name=DAMOX
      Short name=DAAO
      Short name=DAO
    EC=1.4.3.3

Gene names

Name:

DAO

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.
Catalytic activity	A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD.
Subunit structure	Homodimer. Ref.12
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the DAMOX/DASOX family.

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	D-amino-acid oxidase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 347

347

D-amino-acid oxidase

PRO_0000162763

Regions

Nucleotide binding

3 – 17

15

FAD

Nucleotide binding

37 – 38

2

FAD

Nucleotide binding

44 – 45

2

FAD

Nucleotide binding

49 – 51

3

FAD

Nucleotide binding

312 – 316

5

FAD

Motif

345 – 347

3

Microbody targeting signal

Sites

Binding site

53

1

Substrate

Binding site

164

1

FAD; via amide nitrogen and carbonyl oxygen

Binding site

182

1

FAD

Binding site

217

1

Substrate

Binding site

228

1

Substrate

Binding site

283

1

Substrate

Binding site

313

1

Substrate; via carbonyl oxygen

Binding site

317

1

FAD

Experimental info

Mutagenesis

55

1

Y → F: No effect. Ref.8

Mutagenesis

110

1

M → L: No effect. Ref.8

Mutagenesis

217

1

H → L: No effect. Ref.8

Mutagenesis

228

1

Y → F: Reduces activity.

Mutagenesis

307

1

H → L: Reduces activity.

Secondary structure

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347

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

10 – 23

14

Turn

24 – 26

3

Beta strand

27 – 29

3

Beta strand

31 – 38

8

Helix

40 – 42

3

Helix

44 – 47

4

Helix

63 – 76

14

Turn

77 – 80

4

Turn

82 – 88

7

Beta strand

89 – 100

12

Turn

106 – 110

5

Beta strand

111 – 116

6

Helix

119 – 122

4

Beta strand

129 – 139

11

Helix

141 – 153

13

Turn

154 – 156

3

Beta strand

158 – 161

4

Helix

167 – 172

6

Beta strand

176 – 180

5

Helix

183 – 185

3

Helix

186 – 189

4

Beta strand

196 – 206

11

Beta strand

212 – 217

6

Helix

219 – 221

3

Beta strand

228 – 231

4

Beta strand

233 – 239

7

Helix

253 – 266

14

Helix

268 – 272

5

Beta strand

274 – 285

12

Beta strand

290 – 296

7

Turn

298 – 301

4

Beta strand

303 – 309

7

Helix

315 – 336

22

Sequences

	Sequence		Length	Mass (Da)
	P00371-1 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: 0EC6577BDB2BF46C	FASTA	347	39,336
	10 20 30 40 50 60 MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DVKVYADRFT PFTTTDVAAG LWQPYTSEPS 70 80 90 100 110 120 NPQEANWNQQ TFNYLLSHIG SPNAANMGLT PVSGYNLFRE AVPDPYWKDM VLGFRKLTPR 130 140 150 160 170 180 ELDMFPDYRY GWFNTSLILE GRKYLQWLTE RLTERGVKFF LRKVESFEEV ARGGADVIIN 190 200 210 220 230 240 CTGVWAGVLQ PDPLLQPGRG QIIKVDAPWL KNFIITHDLE RGIYNSPYII PGLQAVTLGG 250 260 270 280 290 300 TFQVGNWNEI NNIQDHNTIW EGCCRLEPTL KDAKIVGEYT GFRPVRPQVR LEREQLRFGS 310 320 330 340 SNTEVIHNYG HGGYGLTIHW GCALEVAKLF GKVLEERNLL TMPPSHL

References

[1]	"The primary structure of D-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence." Ronchi S., Minchiotti L., Galliano M., Curti B., Swenson R.P., Williams C.H. Jr., Massey V. J. Biol. Chem. 257:8824-8834(1982) [PubMed: 6124543] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Kidney.
[2]	"Molecular cloning and sequence analysis of cDNAs encoding porcine kidney D-amino acid oxidase." Fukui K., Watanabe F., Shibata T., Miyake Y. Biochemistry 26:3612-3618(1987) [PubMed: 2888479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	"Porcine D-amino acid oxidase: determination of the mRNA nucleotide sequence by the characterization of genomic and cDNA clones." Jacobs P., Brockly F., Massaer M., Loriau R., Guillaume J.P., Ciccarelli E., Heinderyckx M., Cravador A., Biemans R., van Elsen A., Herzog A., Bollen A. Gene 59:55-61(1987) [PubMed: 2893757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]	"Structural interpretation of the binding of 9-azidoacridine to D-amino acid oxidase." Nicholson B.H., Batra S.P. Biochem. J. 255:907-912(1988) [PubMed: 2905598] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Kidney.
[5]	"Expression of normal and abnormal porcine kidney D-amino acid oxidase in Escherichia coli: purification and characterization of the enzymes." Watanabe F., Fukui K., Momoi K., Miyake Y. Biochem. Biophys. Res. Commun. 165:1422-1427(1989) [PubMed: 2575382] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-14.
[6]	"Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene." Swenson R.P., Williams C.H. Jr., Massey V. J. Biol. Chem. 257:1937-1944(1982) [PubMed: 6120171] [Abstract] Cited for: PRELIMINARY STUDIES ON ACTIVE SITE.
[7]	"Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride." Swenson R.P., Williams C.H. Jr., Massey V. J. Biol. Chem. 258:497-502(1983) [PubMed: 6129252] [Abstract] Cited for: PRELIMINARY STUDIES ON ACTIVE SITE.
[8]	"Effect of site-specific mutagenesis of tyrosine-55, methionine-110 and histidine-217 in porcine kidney D-amino acid oxidase on its catalytic function." Watanabe F., Fukui K., Momoi K., Miyake Y. FEBS Lett. 238:269-272(1988) [PubMed: 2901989] [Abstract] Cited for: MUTAGENESIS OF TYR-55; MET-110 AND HIS-217.
[9]	"Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization." Miyano M., Fukui K., Watanabe F., Takahashi S., Tada M., Kanashiro M., Miyake Y. J. Biochem. 109:171-177(1991) [PubMed: 1673125] [Abstract] Cited for: ACTIVE SITES TYR-228 AND HIS-307.
[10]	"Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0-A resolution." Mizutani H., Miyahara I., Hirotsu K., Nishima Y., Shiga K., Setoyama C., Miura R. J. Biochem. 120:14-17(1996) [PubMed: 8864836] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[11]	"Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2." Mattevi A., Vanoni M.A., Todone F., Rizzi M., Teplyakov A., Coda A., Bolognesi M., Curti B. Proc. Natl. Acad. Sci. U.S.A. 93:7496-7501(1996) [PubMed: 8755502] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD AND BENZOATE.
[12]	"Active site plasticity in D-amino acid oxidase: a crystallographic analysis." Todone F., Vanoni M.A., Mozzarelli A., Bolognesi M., Coda A., Curti B., Mattevi A. Biochemistry 36:5853-5860(1997) [PubMed: 9153426] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEXES WITH FAD; D-ARGININE; IMINO-TRYPTOPHAN AND 3-METHYL-2-OXOBUTYRIC ACID, SUBUNIT, ENZYME MECHANISM.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBLGenBankDDBJ

M16972 mRNA. Translation: AAA30985.1.
M18447 , M18444, M18445, M18446 Genomic DNA. Translation: AAA31025.1.
M18448 mRNA. Translation: AAA31026.1.

PIR

OXPGDA. A29598.
A33798.

RefSeq

NP_999231.1.

UniGene

Ssc.232

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AN9	X-ray	2.50	A/B	1-340	[»]
1DAO	X-ray	3.20	A/B/C/D/E/F/G/H	1-347	[»]
1DDO	X-ray	3.10	A/B/C/D/E/F/G/H	1-347	[»]
1EVI	X-ray	2.50	A/B	1-340	[»]
1KIF	X-ray	2.60	A/B/C/D/E/F/G/H	1-347	[»]
1VE9	X-ray	2.50	A/B	1-347	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSSSCT00000010894; ENSSSCP00000010609; ENSSSCG00000009942; Sus scrofa. [Genome view]

GeneID

397134.

KEGG

ssc:397134.

Organism-specific databases

CTD

397134.

Phylogenomic databases

HOVERGEN

P00371.

Enzyme and pathway databases

BRENDA

1.4.3.3. 249.

Family and domain databases

InterPro

IPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF01266. DAO. 1 hit.
[Graphical view]

PROSITE

PS00677. DAO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P00371.

PMAP-CutDB

P00371.

Entry information

Entry name

OXDA_PIG

Accession

Primary (citable) accession number: P00371

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 1, 1989
Last modified:	November 24, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)