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Reviewed, UniProtKB/Swiss-Prot Q9Z302 (OXDA_CRIGR)

Last modified June 16, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

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Names and origin

Protein namesRecommended name:
    D-amino-acid oxidase
      Short name=DAMOX
      Short name=DAAO
      Short name=DAO
    EC=1.4.3.3
Gene names
Name: DAO
OrganismCricetulus griseus (Chinese hamster)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

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Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. 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 By similarity.

Catalytic activity

A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactor

FAD By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the DAMOX/DASOX family.

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Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionD-amino-acid oxidase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346D-amino-acid oxidase
PRO_0000162760

Regions

Nucleotide binding3 – 1715FAD By similarity
Nucleotide binding36 – 372FAD By similarity
Nucleotide binding43 – 442FAD By similarity
Nucleotide binding48 – 503FAD By similarity
Nucleotide binding311 – 3155FAD By similarity
Motif344 – 3463Microbody targeting signal By similarity

Sites

Binding site521Substrate By similarity
Binding site1631FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1811FAD By similarity
Binding site2161Substrate By similarity
Binding site2271Substrate By similarity
Binding site2821Substrate By similarity
Binding site3121Substrate; via carbonyl oxygen By similarity
Binding site3161FAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9Z302-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 320FD17769437F3C

FASTA34639,146
        10         20         30         40         50         60 
MRVVVIGAGV IGLSTALCIH ERFSPVQPLH MKIYADRFTP FTTSDVAAGF WQPYLSDPRN 

        70         80         90        100        110        120 
PQEVEWNQQT FDYLLSHIHS PNAEKMGLSL ISGYNLFKEE VPDPFWRNTV LGFRKLTPRE 

       130        140        150        160        170        180 
MDIFPDYGYG WFNTSLTLEG KSYLPWLTER LTERGVKLFH RKVESFEEVA RGGADVIINC 

       190        200        210        220        230        240 
TGVWAGALQA DTSLQPGRGQ IIQVEAPWMK HFILTHDPRL GIYNSPYIIP GSKTVTLGGV 

       250        260        270        280        290        300 
FQLGNWNELN SVHDHNTIWK SCCKLEPTLK NAKIVGELTG FRPVRHQVRL KKKQLHFGSS 

       310        320        330        340 
SVEVIHNYGH GGYGLTIHWG CAMEAANLFG KILEEKKLSR MPASHL

« Hide

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References

[1]"Hamster D-amino-acid oxidase."
Konno R.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.

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Cross-references

Sequence databases

AB016530 mRNA. Translation: BAA74715.1.

3D structure databases

HSSPHSSP built from PDB template 1VE9 based on UniProtKB P00371.
SMRQ9Z302. Positions 1-339.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ9Z302.

Enzyme and pathway databases

BRENDA1.4.3.3. 18.

Family and domain databases

InterProIPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[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...

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Entry information

Entry nameOXDA_CRIGR
AccessionPrimary (citable) accession number: Q9Z302
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

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