[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), 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], AND ALTERNATIVE SPLICING. 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 (By similarity).

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=0.38 mM for D-Asp;
	K_M=0.25 mM for D-Glu;
	K_M=1.84 mM for NMDA;
	V_max=4.40 µmol/min/mg enzyme with D-Asp as substrate;
	V_max=3.03 µmol/min/mg enzyme with D-Glu as substrate;
	V_max=4.31 µmol/min/mg enzyme with NMDA as substrate;

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	a
Isoform ID	Q19564-1
Note: No experimental confirmation available.
This is the isoform sequence displayed in this entry.

Name	b
Isoform ID	Q19564-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_014356, VSP_014357, VSP_014358, VSP_014359.

SIMILARITY: Belongs to the DAMOX/DASOX family.
CAUTION: The conserved active site Tyr residue in position 224 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

AB275892; BAF34315.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U53139; AAK18939.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U53139; AAN84824.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T29219; T29219.

NP_504908.1; -.

3D structure databases

HSSP

P00371; 1AN9. [HSSP ENTRY / PDB]

ModBase

Q19564.

Organism-specific databases

WormBase

WBGene00017565; F18E3.7.

WormPep

F18E3.7a; CE07083. [WormPep / WorfDB]
F18E3.7b; CE32864. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

Q19564; -.

Ontologies

GO:0009792;	Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
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.

BLOCKS

Q19564.

Genome annotation databases

Ensembl

F18E3.7; Caenorhabditis elegans. [Contig view]

GeneID

179130; -.

KEGG

cel:F18E3.7; -.

NMPDR

fig|6239.3.peg.18465; -.

Other

ProtoNet

Q19564.

UniRef

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

Keywords

Alternative splicing; Complete proteome; FAD; Flavoprotein; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 334`	`334`	`D-aspartate oxidase 1.`	`PRO_0000162772`
`NP_BIND`	`8 22`	`15`	`FAD (Potential).`
`ACT_SITE`	`305 305`		`By similarity.`
`VAR_SEQ`	`1 222`		`Missing (in isoform b).`	`VSP_014356`
`VAR_SEQ`	`223 228`		`TFTIPK -> MCQIFR (in isoform b).`	`VSP_014357`
`VAR_SEQ`	`268 273`		`EPKIIK -> VRISFF (in isoform b).`	`VSP_014358`
`VAR_SEQ`	`274 334`		`Missing (in isoform b).`	`VSP_014359`

Sequence information

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

Molecular weight: 37608 Da [This is the MW of the unprocessed precursor]

CRC64: 90B1731A702BB6FD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MANIIPKIAI IGEGVIGCTS ALQISKAIPN AKITVLHDKP FKKSCSAGPA GLFRIDYEEN 

        70         80         90        100        110        120 
TEYGRASFAW FSHLYRTTKG SETGVKLVSG HIQSDNLESL KQQQRAYGDI VYNFRFLDDR 

       130        140        150        160        170        180 
ERLDIFPEPS KHCIHYTAYA SEGNKYVPYL KNLLLEQKIE FKQQEVTSLD AVADAGYDVI 

       190        200        210        220        230        240 
VNCAGLYGGK LAGDDDTCYP IRGVILEVDA PWHKHFNYRD FTTFTIPKEH SVVVGSTKQD 

       250        260        270        280        290        300 
NRWDLEITDE DRNDILKRYI ALHPGMREPK IIKEWSALRP GRKHVRIEAQ KRTSVGNSKD 

       310        320        330 
YMVVHHYGHG SNGFTLGWGT AIEATKLVKT ALGL

Q19564 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