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P14920 (OXDA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-amino-acid oxidase

Short name=DAAO
Short name=DAMOX
Short name=DAO
EC=1.4.3.3
Gene names
Name:DAO
Synonyms:DAMOX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.8

Catalytic activity

A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. Ref.7

Cofactor

FAD.

Subunit structure

Homodimer. Ref.7

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the DAMOX/DASOX family.

Biophysicochemical properties

Kinetic parameters:

KM=3.6 mM for D-serine Ref.7 Ref.8

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

Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processD-alanine catabolic process

Inferred from direct assay PubMed 16616139PubMed 20603179. Source: UniProtKB

D-serine catabolic process

Inferred from direct assay PubMed 18544534. Source: UniProtKB

D-serine metabolic process

Inferred from direct assay PubMed 21679769. Source: UniProtKB

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

dopamine biosynthetic process

Inferred from direct assay Ref.8. Source: UniProtKB

glyoxylate metabolic process

Traceable author statement. Source: Reactome

leucine metabolic process

Inferred from electronic annotation. Source: Ensembl

proline catabolic process

Inferred from direct assay PubMed 16616139. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from direct assay PubMed 21679769. Source: UniProtKB

peroxisomal matrix

Traceable author statement. Source: Reactome

peroxisomal membrane

Inferred from direct assay PubMed 21679769. Source: UniProtKB

peroxisome

Inferred from direct assay PubMed 18544534. Source: UniProtKB

   Molecular_functionD-amino-acid oxidase activity

Inferred from direct assay PubMed 12364586PubMed 16616139Ref.8PubMed 18544534PubMed 19309736PubMed 20603179. Source: UniProtKB

FAD binding

Inferred from direct assay PubMed 16616139PubMed 19309736PubMed 20521334. Source: UniProtKB

cofactor binding

Inferred from direct assay PubMed 20603179. Source: UniProtKB

protein dimerization activity

Inferred from direct assay PubMed 16616139PubMed 19309736. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

Complete GO annotation...

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P14920 [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

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] [Europe PMC] [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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Colon and Kidney.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
[7]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FAD AND THE INHIBITOR BENZOATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[8]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEXES WITH FAD AND IMINO-SERINE; IMINO-DOPA AND O-AMINOBENZOATE, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION.
[9]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH FAD AND SYNTHETIC INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13227 mRNA. Translation: CAA31614.1.
AK312995 mRNA. Translation: BAG35832.1.
CH471054 Genomic DNA. Translation: EAW97837.1.
BC029057 mRNA. Translation: AAH29057.1.
BC074770 mRNA. Translation: AAH74770.1.
D11370 Genomic DNA. Translation: BAA20974.1.
PIRS01340.
RefSeqNP_001908.3. NM_001917.4.
UniGeneHs.113227.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
3G3EX-ray2.20A/B/C/D1-347[»]
3W4IX-ray2.50A/B/C/D1-347[»]
3W4JX-ray2.74A/B/C/D1-347[»]
3W4KX-ray2.86A/B/C/D1-347[»]
3ZNNX-ray1.90A/B1-347[»]
3ZNOX-ray2.30A/B1-347[»]
3ZNPX-ray2.40A/B1-347[»]
3ZNQX-ray2.75A/B1-347[»]
ProteinModelPortalP14920.
SMRP14920. Positions 1-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107980. 3 interactions.
IntActP14920. 2 interactions.
STRING9606.ENSP00000228476.

Chemistry

BindingDBP14920.
ChEMBLCHEMBL5485.

Polymorphism databases

DMDM25453448.

Proteomic databases

PaxDbP14920.
PRIDEP14920.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228476; ENSP00000228476; ENSG00000110887.
GeneID1610.
KEGGhsa:1610.
UCSCuc001tnq.4. human.

Organism-specific databases

CTD1610.
GeneCardsGC12P109273.
HGNCHGNC:2671. DAO.
HPAHPA038653.
HPA038654.
MIM124050. gene.
neXtProtNX_P14920.
Orphanet803. Amyotrophic lateral sclerosis.
PharmGKBPA27139.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0665.
HOGENOMHOG000046303.
HOVERGENHBG003493.
InParanoidP14920.
KOK00273.
OMAIHEHYHS.
OrthoDBEOG7B31NB.
PhylomeDBP14920.
TreeFamTF313887.

Enzyme and pathway databases

BioCycMetaCyc:HS03351-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP14920.
BgeeP14920.
CleanExHS_DAO.
GenevestigatorP14920.

Family and domain databases

InterProIPR023209. D-aa_oxidase.
IPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
[Graphical view]
PANTHERPTHR11530. PTHR11530. 1 hit.
PfamPF01266. DAO. 1 hit.
[Graphical view]
PIRSFPIRSF000189. D-aa_oxidase. 1 hit.
PROSITEPS00677. DAO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14920.
GenomeRNAi1610.
NextBio6618.
PROP14920.
SOURCESearch...

Entry information

Entry nameOXDA_HUMAN
AccessionPrimary (citable) accession number: P14920
Secondary accession number(s): B2R7I5, Q16758, Q8N6R2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2002
Last modified: April 16, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 12

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