Reviewed, UniProtKB/Swiss-Prot O45307 (OXDD2_CAEEL)

Names and origin

Protein names

Recommended name:
    D-aspartate oxidase 2
      Short name=DASOX 2
    EC=1.4.3.1
Alternative name(s):
    DDO 2

Gene names

ORF Names:

C47A10.5

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. Ref.1
Catalytic activity	D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2.
Cofactor	FAD. UniProtKB P31228
Subcellular location	Peroxisome Probable. Ref.1
Sequence similarities	Belongs to the DAMOX/DASOX family.
Caution	The conserved active site Tyr residue in position 221 is replaced by a Phe.
biophysicochemical properties	Kinetic parameters: KM=2.02 mM for D-Asp Ref.1 KM=0.23 mM for D-Glu Ref.1 KM=0.84 mM for NMDA Ref.1 Vmax=6.16 µmol/min/mg enzyme with D-Asp as substrate Ref.1 Vmax=7.62 µmol/min/mg enzyme with D-Glu as substrate Ref.1 Vmax=8.80 µmol/min/mg enzyme with NMDA as substrate Ref.1

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
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: InterPro D-aspartate 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 – 334	334	D-aspartate oxidase 2		PRO_0000317123
Regions
	Nucleotide binding	5 – 19	15	FAD By similarity UniProtKB P31228
	Nucleotide binding	35 – 36	2	FAD By similarity
	Nucleotide binding	42 – 43	2	FAD By similarity
	Nucleotide binding	47 – 49	3	FAD By similarity
	Nucleotide binding	307 – 311	5	FAD By similarity
	Motif	332 – 334	3	Microbody targeting signal Potential
Sites
	Binding site	163	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	276	1	Substrate By similarity
	Binding site	308	1	Substrate; via carbonyl oxygen By similarity
	Binding site	312	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	O45307-1 [UniParc]. Last modified September 13, 2004. Version 2. Checksum: 7C30DFEA2EE5F22C	FASTA	334	37,637
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Caenorhabditis elegans has two genes encoding functional D-aspartate oxidases." Katane M., Seida Y., Sekine M., Furuchi T., Homma H. FEBS J. 274:137-149(2007) [PubMed: 17140416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB275891 mRNA. Translation: BAF34314.1. Z81484 Genomic DNA. Translation: CAB03970.2.
PIR	T19979.
RefSeq	NP_507491.2.
UniGene	Cel.4486
3D structure databases
HSSP	HSSP built from PDB template 1AN9 based on UniProtKB P00371.
ModBase	Search...
Genome annotation databases
Ensembl	C47A10.5. Caenorhabditis elegans. [Contig view]
GeneID	183530.
KEGG	cel:C47A10.5.
NMPDR	fig|6239.3.peg.21577.
Organism-specific databases
WormBase	WBGene00008127. C47A10.5.
WormPep	C47A10.5. CE36691. [WorfDB]
Phylogenomic databases
OMA	O45307. HYGHGGN.
Enzyme and pathway databases
BRENDA	1.4.3.1. 672.
Gene expression databases
ArrayExpress	O45307.
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
NextBio	921480.

Entry information

Entry name

OXDD2_CAEEL

Accession

Primary (citable) accession number: O45307

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 13, 2004
Last modified:	June 16, 2009
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project