[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. STRAIN=Bristol N2; DOI=10.1111/j.1742-4658.2006.05571.x; PubMed=17140416 [NCBI, ExPASy, EBI, Israel, Japan] Katane M., Seida Y., Sekine M., Furuchi T., Homma H.; "Caenorhabditis elegans has two genes encoding functional D-aspartate oxidases."; FEBS J. 274:137-149(2007).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).

Comments

FUNCTION: Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.
CATALYTIC ACTIVITY: D-aspartate + H₂O + O₂ = oxaloacetate + NH₃ + H₂O₂.
COFACTOR: FAD.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=2.02 mM for D-Asp;
	K_M=0.23 mM for D-Glu;
	K_M=0.84 mM for NMDA;
	V_max=6.16 µmol/min/mg enzyme with D-Asp as substrate;
	V_max=7.62 µmol/min/mg enzyme with D-Glu as substrate;
	V_max=8.80 µmol/min/mg enzyme with NMDA as substrate;

SUBCELLULAR LOCATION: Peroxisome (Probable).
SIMILARITY: Belongs to the DAMOX/DASOX family.
CAUTION: The conserved active site Tyr residue in position 221 is replaced by a Phe.

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

AB275891; BAF34314.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z81484; CAB03970.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T19979; T19979.

NP_507491.2; -.

3D structure databases

HSSP

P00371; 1AN9. [HSSP ENTRY / PDB]

ModBase

O45307.

Organism-specific databases

WormBase

WBGene00008127; C47A10.5.

WormPep

C47A10.5; CE36691. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

O45307; -.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003884;	Molecular function: D-amino-acid oxidase activity (inferred from electronic annotation from InterPro).
GO:0008445;	Molecular function: D-aspartate oxidase activity (inferred from electronic annotation from EC).
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.

PROSITE

PS00677; DAO; 1.

Genome annotation databases

Ensembl

C47A10.5; Caenorhabditis elegans. [Contig view]

GeneID

183530; -.

KEGG

cel:C47A10.5; -.

NMPDR

fig|6239.3.peg.21577; -.

Other

921480; -.

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

Keywords

ATP-binding; Complete proteome; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase; Peroxisome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 334`	`334`	`D-aspartate oxidase 2.`	`PRO_0000317123`
`NP_BIND`	`5 19`	`15`	`FAD (By similarity).`
`NP_BIND`	`56 63`	`8`	`ATP (Potential).`
`MOTIF`	`332 334`	`3`	`Microbody targeting signal (Potential).`
`ACT_SITE`	`302 302`		`By similarity.`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 37637 Da [This is the MW of the unprocessed precursor]

CRC64: 7C30DFEA2EE5F22C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTPKIAIIGE GVIGCSTALQ VAQAVPDARV TVLSDRPFEQ TCSFGPAGLF RIDDIANREF 

        70         80         90        100        110        120 
GKSTFDWFAH LHRTEKGDKT GVKLLSGHIQ SDSKERLEQQ QKAYGDIVYN FRFLEKREIL 

       130        140        150        160        170        180 
DLFPNPSEHC IHYTAFASEG NKYVPYLKFQ CQARGVEFLH RKVRDLEELA NEGYDVIVNC 

       190        200        210        220        230        240 
AGLSGGTLAG DDDSVYPIRG VVLDVEAHWH KHFNYKDFIT FTIPKENSVV IGSVKQENRW 

       250        260        270        280        290        300 
DLEITDVDRK DILERYVALH PAMREPKILG EWSGLRPARK TIRIEKVEKK SEKSGKKYTV 

       310        320        330 
VHHYGHGGNG FTLGWGTAVE ATKLVKSALN SSKL

O45307 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