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Reviewed, UniProtKB/Swiss-Prot O45307 (OXDD2_CAEEL)

Last modified November 25, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.

Catalytic activity

D-aspartate + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2).

Cofactor

FAD.

Subcellular location

PeroxisomeProbable.

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

KM=0.23 mM for D-Glu

KM=0.84 mM for NMDA

Vmax=6.16 µmol/min/mg enzyme with D-Asp as substrate

Vmax=7.62 µmol/min/mg enzyme with D-Glu as substrate

Vmax=8.80 µmol/min/mg enzyme with NMDA as substrate

Ontologies

Keywords

   Cellular componentPeroxisome
   LigandATP-binding
FAD
Flavoprotein
Nucleotide-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

D-amino-acid oxidase activity

Inferred from electronic annotation. Source: InterPro

D-aspartate oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334D-aspartate oxidase 2
PRO_0000317123

Regions

Nucleotide binding5 – 1915FAD By similarity
Nucleotide binding56 – 638ATP Potential
Motif332 – 3343Microbody targeting signal Potential

Sites

Active site3021 By similarity

Sequences

Sequence LengthMass (Da)Tools
O45307-1 [UniParc].

Last modified September 13, 2004. Version 2.
Checksum: 7C30DFEA2EE5F22C

FASTA33437,637
        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 

« Hide

References

« Hide '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

AB275891 mRNA. Translation: BAF34314.1.
Z81484 Genomic DNA. Translation: CAB03970.2.
PIRT19979.
RefSeqNP_507491.2.
UniGeneCel.4486

3D structure databases

HSSPHSSP built from PDB template 1AN9 based on UniProtKB P00371.
ModBaseSearch...

Genome annotation databases

EnsemblC47A10.5. Caenorhabditis elegans. [Contig view]
GeneID183530.
KEGGcel:C47A10.5.
NMPDRfig|6239.3.peg.21577.

Organism-specific databases

WormBaseWBGene00008127. C47A10.5.
WormPepC47A10.5. CE36691. [WorfDB]

Gene expression databases

ArrayExpressO45307.

Family and domain databases

InterProIPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01266. DAO. 1 hit.
[Graphical view]
PROSITEPS00677. DAO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio921480.

Entry information

Entry nameOXDD2_CAEEL
AccessionPrimary (citable) accession number: O45307
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 13, 2004
Last modified: November 25, 2008
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents