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Reviewed, UniProtKB/Swiss-Prot P14920 (OXDA_HUMAN)

Last modified July 7, 2009. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms: DAMOX
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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. Ref.6

Catalytic activity

A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. Ref.5

Cofactor

FAD.

Subunit structure

Homodimer. Ref.5

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the DAMOX/DASOX family.

Biophysicochemical properties

Kinetic parameters:

KM=3.6 mM for D-serine

KM=1.7 mM for D-proline

KM=1.1 mM for D-tyrosine

KM=1.5 mM for D-DOPA

KM=1.2 mM for D-phenylalanine

KM=0.9 mM for D-alanine

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Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome Ref.1

Non-traceable author statement. Source: ProtInc

   Molecular functionD-amino-acid oxidase activity Ref.4

Traceable author statement. Source: ProtInc

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_0000162761

Regions

Nucleotide binding3 – 1715FAD
Nucleotide binding37 – 382FAD
Nucleotide binding44 – 452FAD
Nucleotide binding49 – 513FAD
Nucleotide binding312 – 3176FAD
Motif345 – 3473Microbody targeting signal

Sites

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

Experimental info

Sequence conflict311D → H in CAA31614. Ref.1
Sequence conflict2791R → A in CAA31614. Ref.1

Secondary structure

1 .......................................................... 347
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P14920-1 [UniParc].

Last modified November 25, 2002. Version 3.
Checksum: A508E603872F3072

FASTA34739,474
        10         20         30         40         50         60 
MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG LWQPYLSDPN 

        70         80         90        100        110        120 
NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE AIPDPSWKDT VLGFRKLTPR 

       130        140        150        160        170        180 
ELDMFPDYGY GWFHTSLILE GKNYLQWLTE RLTERGVKFF QRKVESFEEV AREGADVIVN 

       190        200        210        220        230        240 
CTGVWAGALQ RDPLLQPGRG QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG 

       250        260        270        280        290        300 
IFQLGNWSEL NNIQDHNTIW EGCCRLEPTL KNARIIGERT GFRPVRPQIR LEREQLRTGP 

       310        320        330        340 
SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase."
Momoi K., Fukui K., Watanabe F., Miyake Y.
FEBS Lett. 238:180-184(1988) [PubMed: 2901986] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]Momoi K.
Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Colon and Kidney.
[4]"Molecular cloning and chromosomal localization of a human gene encoding D-amino-acid oxidase."
Fukui K., Miyake Y.
J. Biol. Chem. 267:18631-18638(1992) [PubMed: 1356107] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
[5]"Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring."
Kawazoe T., Tsuge H., Pilone M.S., Fukui K.
Protein Sci. 15:2708-2717(2006) [PubMed: 17088322] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FAD AND THE INHIBITOR BENZOATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[6]"Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis."
Kawazoe T., Tsuge H., Imagawa T., Aki K., Kuramitsu S., Fukui K.
Biochem. Biophys. Res. Commun. 355:385-391(2007) [PubMed: 17303072] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEXES WITH FAD AND IMINO-SERINE; IMINO-DOPA AND O-AMINOBENZOATE, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION.
[7]"The discovery of fused pyrrole carboxylic acids as novel, potent D-amino acid oxidase (DAO) inhibitors."
Sparey T., Abeywickrema P., Almond S., Brandon N., Byrne N., Campbell A., Hutson P.H., Jacobson M., Jones B., Munshi S., Pascarella D., Pike A., Prasad G.S., Sachs N., Sakatis M., Sardana V., Venkatraman S., Young M.B.
Bioorg. Med. Chem. Lett. 18:3386-3391(2008) [PubMed: 18455394] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH FAD AND SYNTHETIC INHIBITOR.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X13227 mRNA. Translation: CAA31614.1.
BC029057 mRNA. Translation: AAH29057.1.
BC074770 mRNA. Translation: AAH74770.1.
D11370 Genomic DNA. Translation: BAA20974.1.
IPIIPI00295438.
PIRS01340.
RefSeqNP_001908.3.
UniGeneHs.113227

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2DU8X-ray2.50A/B/G/J1-347[»]
2E48X-ray2.90A/B/C/D1-347[»]
2E49X-ray3.20A/B/C/D1-347[»]
2E4AX-ray2.60A/B/C/D1-347[»]
2E82X-ray2.70A/B/C/D1-347[»]
2GNZmodel-A1-339[»]
3CUKX-ray2.49A/B/C/D1-347[»]
ModBaseSearch...

Proteomic databases

PRIDEP14920.

Genome annotation databases

EnsemblENSG00000110887. Homo sapiens. [Contig view]
GeneID1610.
KEGGhsa:1610.
NMPDRfig|9606.3.peg.8199.
UCSCuc001tnr.2. human.

Organism-specific databases

GeneCardsGC12P107776.
H-InvDBHIX0017669.
HGNCHGNC:2671. DAO.
MIM124050. gene.
PharmGKBPA27139.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP14920.
HOVERGENP14920.
OMAP14920. LRKVESF.

Enzyme and pathway databases

BRENDA1.4.3.3. 247.
ReactomeREACT_16925. Glyoxylate metabolism.

Gene expression databases

ArrayExpressP14920.
BgeeP14920.
CleanExHS_DAO.
GermOnlineENSG00000110887. Homo sapiens.

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...

Other Resources

NextBio6618.
SOURCESearch...

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Entry information

Entry nameOXDA_HUMAN
AccessionPrimary (citable) accession number: P14920
Secondary accession number(s): Q16758, Q8N6R2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2002
Last modified: July 7, 2009
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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