[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Kidney; PubMed=1980495 [NCBI, ExPASy, EBI, Israel, Japan] Momoi K., Fukui K., Tada M., Miyake Y.; "Gene expression of D-amino acid oxidase in rabbit kidney."; J. Biochem. 108:406-413(1990).

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 (By similarity).
SUBCELLULAR LOCATION: Peroxisome.
SIMILARITY: Belongs to the DAMOX/DASOX family.

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

D12494; BAA02058.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

JX0132; JX0132.

NP_001075658.1; -.

3D structure databases

PDB

2I3K; Model; -; @=1-337.

[ExPASy / RCSB / EBI]

2I3K; -.

P22942; 1-340.

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

Ensembl

ENSOCUG00000001322; Oryctolagus cuniculus. [Contig view]

GeneID

100008977; -.

Phylogenomic databases

HOVERGEN

P22942; -.

Other

UniRef

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

Keywords

3D-structure; 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_0000162764`
`NP_BIND`	`3 17`	`15`	`FAD (Potential).`
`MOTIF`	`345 347`	`3`	`Microbody targeting signal.`
`ACT_SITE`	`228 228`		`By similarity.`
`ACT_SITE`	`307 307`		`By similarity.`

Sequence information

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

Molecular weight: 38590 Da [This is the MW of the unprocessed precursor]

CRC64: E22CFC0D944AFA61 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRVVVIGAGV IGLSTALCIH ELYHSALQPL DMTIYADRFT PLTNTDVAAG LWQPYLSDPS 

        70         80         90        100        110        120 
NPQEADWSRQ TFNHLLSHIH SPSAEKMGLA LISGYNLFRK AVPDPSWKDT VLGFRKLTLR 

       130        140        150        160        170        180 
ELDMFPGYSY GWFNTSLILD GRSYLQWLTK RLTERGVKLF QRKVESFDEV AGGGVDVIVN 

       190        200        210        220        230        240 
CTGVWASALQ PDPLLQPGRG QIIKVDAPWV KHFIITHDPE SGIYKSPYII PGVHAVTLGG 

       250        260        270        280        290        300 
IFQMGNWSEG NSTDDHNTIW KGCCSLEPTL KDARIVGEWT GFRPVRPQIR LGREQLSAGP 

       310        320        330        340 
SKTEVIHNYG HGGYGLTIHW GCALEAAKLF GKILEEKKSS RMPPSHL

P22942 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