[1]	PROTEIN SEQUENCE. TISSUE=Kidney; PubMed=6124543 [NCBI, ExPASy, EBI, Israel, Japan] Ronchi S., Minchiotti L., Galliano M., Curti B., Swenson R.P., Williams C.H. Jr., Massey V.; "The primary structure of D-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence."; J. Biol. Chem. 257:8824-8834(1982).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Kidney; DOI=10.1021/bi00386a054; PubMed=2888479 [NCBI, ExPASy, EBI, Israel, Japan] Fukui K., Watanabe F., Shibata T., Miyake Y.; "Molecular cloning and sequence analysis of cDNAs encoding porcine kidney D-amino acid oxidase."; Biochemistry 26:3612-3618(1987).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. DOI=10.1016/0378-1119(87)90266-6; PubMed=2893757 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Porcine D-amino acid oxidase: determination of the mRNA nucleotide sequence by the characterization of genomic and cDNA clones."; Gene 59:55-61(1987).
[4]	PROTEIN SEQUENCE. TISSUE=Kidney; PubMed=2905598 [NCBI, ExPASy, EBI, Israel, Japan] Nicholson B.H., Batra S.P.; "Structural interpretation of the binding of 9-azidoacridine to D-amino acid oxidase."; Biochem. J. 255:907-912(1988).
[5]	NUCLEOTIDE SEQUENCE OF 1-14. DOI=10.1016/0006-291X(89)92762-9; PubMed=2575382 [NCBI, ExPASy, EBI, Israel, Japan] Watanabe F., Fukui K., Momoi K., Miyake Y.; "Expression of normal and abnormal porcine kidney D-amino acid oxidase in Escherichia coli: purification and characterization of the enzymes."; Biochem. Biophys. Res. Commun. 165:1422-1427(1989).
[6]	PRELIMINARY STUDIES ON ACTIVE SITE. PubMed=6120171 [NCBI, ExPASy, EBI, Israel, Japan] Swenson R.P., Williams C.H. Jr., Massey V.; "Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene."; J. Biol. Chem. 257:1937-1944(1982).
[7]	PRELIMINARY STUDIES ON ACTIVE SITE. PubMed=6129252 [NCBI, ExPASy, EBI, Israel, Japan] Swenson R.P., Williams C.H. Jr., Massey V.; "Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride."; J. Biol. Chem. 258:497-502(1983).
[8]	MUTAGENESIS OF TYR-55; MET-110 AND HIS-217. DOI=10.1016/0014-5793(88)80494-0; PubMed=2901989 [NCBI, ExPASy, EBI, Israel, Japan] Watanabe F., Fukui K., Momoi K., Miyake Y.; "Effect of site-specific mutagenesis of tyrosine-55, methionine-110 and histidine-217 in porcine kidney D-amino acid oxidase on its catalytic function."; FEBS Lett. 238:269-272(1988).
[9]	ACTIVE SITES TYR-228 AND HIS-307. PubMed=1673125 [NCBI, ExPASy, EBI, Israel, Japan] 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. 109:171-177(1991).
[10]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). PubMed=8864836 [NCBI, ExPASy, EBI, Israel, Japan] Mizutani H., Miyahara I., Hirotsu K., Nishima Y., Shiga K., Setoyama C., Miura R.; "Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0-A resolution."; J. Biochem. 120:14-17(1996).
[11]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). DOI=10.1073/pnas.93.15.7496; PubMed=8755502 [NCBI, ExPASy, EBI, Israel, Japan] Mattevi A., Vanoni M.A., Todone F., Rizzi M., Teplyakov A., Coda A., Bolognesi M., Curti B.; "Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2."; Proc. Natl. Acad. Sci. U.S.A. 93:7496-7501(1996).
[12]	X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). DOI=10.1021/bi9630570; PubMed=9153426 [NCBI, ExPASy, EBI, Israel, Japan] Todone F., Vanoni M.A., Mozzarelli A., Bolognesi M., Coda A., Curti B., Mattevi A.; "Active site plasticity in D-amino acid oxidase: a crystallographic analysis."; Biochemistry 36:5853-5860(1997).

Comments

FUNCTION: 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: Homodimer.
SUBCELLULAR LOCATION: Peroxisome.
SIMILARITY: Belongs to the DAMOX/DASOX family.
WEB RESOURCE: Name=Worthington enzyme manual; URL="http://www.worthington-biochem.com/DAOFF/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M16972; AAA30985.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18447; AAA31025.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18444; AAA31025.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18445; AAA31025.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18446; AAA31025.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18448; AAA31026.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A29598; OXPGDA.
A33798; A33798.

RefSeq

NP_999231.1; -.

UniGene

Ssc.232

3D structure databases

PDB

1AN9; X-ray; 2.50 A; A/B=1-340.	[ExPASy / RCSB / EBI]
1DAO; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-347.	[ExPASy / RCSB / EBI]
1DDO; X-ray; 3.10 A; A/B/C/D/E/F/G/H=1-347.	[ExPASy / RCSB / EBI]
1EVI; X-ray; 2.50 A; A/B=1-340.	[ExPASy / RCSB / EBI]
1KIF; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-347.	[ExPASy / RCSB / EBI]
1VE9; X-ray; 2.50 A; A/B=1-347.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AN9; -.
1DAO; -.
1DDO; -.
1EVI; -.
1KIF; -.
1VE9; -.

ModBase

P00371.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006181; D-amino_acid_oxidase_CS.
IPR006076; FAD-dep_OxRdtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

PS00677; DAO; 1.

Genome annotation databases

GeneID

397134; -.

KEGG

ssc:397134; -.

Phylogenomic databases

HOVERGEN

P00371; -.

Other

LinkHub

P00371; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Peroxisome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 347`	`347`	`D-amino-acid oxidase.`	`PRO_0000162763`
`NP_BIND`	`3 17`	`15`	`FAD (Potential).`
`MOTIF`	`345 347`	`3`	`Microbody targeting signal.`
`ACT_SITE`	`228 228`
`ACT_SITE`	`307 307`
`MUTAGEN`	`55 55`		`Y->F: No effect.`
`MUTAGEN`	`110 110`		`M->L: No effect.`
`MUTAGEN`	`217 217`		`H->L: No effect.`
`MUTAGEN`	`228 228`		`Y->F: Reduces activity.`
`MUTAGEN`	`307 307`		`H->L: Reduces activity.`
`STRAND`	`2 6`	`5`
`HELIX`	`10 23`	`14`
`TURN`	`24 26`	`3`
`STRAND`	`27 29`	`3`
`STRAND`	`31 38`	`8`
`HELIX`	`40 42`	`3`
`HELIX`	`44 47`	`4`
`HELIX`	`63 76`	`14`
`TURN`	`77 80`	`4`
`TURN`	`82 88`	`7`
`STRAND`	`89 100`	`12`
`TURN`	`106 110`	`5`
`STRAND`	`111 116`	`6`
`HELIX`	`119 122`	`4`
`STRAND`	`129 139`	`11`
`HELIX`	`141 153`	`13`
`TURN`	`154 156`	`3`
`STRAND`	`158 161`	`4`
`HELIX`	`167 172`	`6`
`STRAND`	`176 180`	`5`
`HELIX`	`183 185`	`3`
`HELIX`	`186 189`	`4`
`STRAND`	`196 206`	`11`
`STRAND`	`212 217`	`6`
`HELIX`	`219 221`	`3`
`STRAND`	`228 231`	`4`
`STRAND`	`233 239`	`7`
`HELIX`	`253 266`	`14`
`HELIX`	`268 272`	`5`
`STRAND`	`274 285`	`12`
`STRAND`	`290 296`	`7`
`TURN`	`298 301`	`4`
`STRAND`	`303 309`	`7`
`HELIX`	`315 336`	`22`

Sequence information

Length: 347 AA [This is the length of the unprocessed precursor]

Molecular weight: 39336 Da [This is the MW of the unprocessed precursor]

CRC64: 0EC6577BDB2BF46C [This is a checksum on the sequence]

        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

P00371 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools