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Reviewed, UniProtKB/Swiss-Prot P22942 (OXDA_RABIT)

Last modified September 1, 2009. Version 61. 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

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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
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Protein attributes

Sequence length347 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.

Subunit structure

Homodimer By similarity.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the DAMOX/DASOX family.

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Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
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 – 347347D-amino-acid oxidase
PRO_0000162764

Regions

Nucleotide binding3 – 1715FAD By similarity
Nucleotide binding37 – 382FAD By similarity
Nucleotide binding44 – 452FAD By similarity
Nucleotide binding49 – 513FAD By similarity
Nucleotide binding312 – 3165FAD By similarity
Motif345 – 3473Microbody targeting signal

Sites

Binding site531Substrate By similarity
Binding site1641FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1821FAD By similarity
Binding site2171Substrate By similarity
Binding site2281Substrate By similarity
Binding site2831Substrate By similarity
Binding site3131Substrate; via carbonyl oxygen By similarity
Binding site3171FAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
P22942-1 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: E22CFC0D944AFA61

FASTA34738,590
        10         20         30         40         50         60 
MRVVVIGAGV IGLSTALCIH ELYHSALQPL DMTIYADRFT PLTNTDVAAG LWQPYLSDPS 

        70         80         90        100        110        120 
NPQEADWSRQ TFNHLLSHIH SPSAEKMGLA LISGYNLFRK AVPDPSWKDT VLGFRKLTLR 

       130        140        150        160        170        180 
ELDMFPGYSY GWFNTSLILD GRSYLQWLTK RLTERGVKLF QRKVESFDEV AGGGVDVIVN 

       190        200        210        220        230        240 
CTGVWASALQ PDPLLQPGRG QIIKVDAPWV KHFIITHDPE SGIYKSPYII PGVHAVTLGG 

       250        260        270        280        290        300 
IFQMGNWSEG NSTDDHNTIW KGCCSLEPTL KDARIVGEWT GFRPVRPQIR LGREQLSAGP 

       310        320        330        340 
SKTEVIHNYG HGGYGLTIHW GCALEAAKLF GKILEEKKSS RMPPSHL

« Hide

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References

[1]"Gene expression of D-amino acid oxidase in rabbit kidney."
Momoi K., Fukui K., Tada M., Miyake Y.
J. Biochem. 108:406-413(1990) [PubMed: 1980495] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.

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Cross-references

Sequence databases

D12494 mRNA. Translation: BAA02058.1.
PIRJX0132.
RefSeqNP_001075658.1.
UniGeneOcu.3052

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2I3Kmodel-@1-337[»]
SMRP22942. Positions 1-340.
ModBaseSearch...

Genome annotation databases

EnsemblENSOCUT00000001322; ENSOCUP00000001140; ENSOCUG00000001322; Oryctolagus cuniculus. [Genome view]
GeneID100008977.

Organism-specific databases

CTD100008977.

Phylogenomic databases

HOVERGENP22942.

Enzyme and pathway databases

BRENDA1.4.3.3. 255.

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_RABIT
AccessionPrimary (citable) accession number: P22942
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: September 1, 2009
This is version 61 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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