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Protein

D-amino-acid oxidase

Gene

DAO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.1 Publication

Cofactori

Kineticsi

  1. KM=3.6 mM for D-serine2 Publications
  2. KM=1.7 mM for D-proline2 Publications
  3. KM=1.1 mM for D-tyrosine2 Publications
  4. KM=1.5 mM for D-DOPA2 Publications
  5. KM=1.2 mM for D-phenylalanine2 Publications
  6. KM=0.9 mM for D-alanine2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531Substrate
    Binding sitei164 – 1641FAD; via amide nitrogen and carbonyl oxygen2 Publications
    Binding sitei182 – 1821FAD2 Publications
    Binding sitei217 – 2171Substrate
    Binding sitei228 – 2281Substrate
    Binding sitei283 – 2831Substrate
    Binding sitei313 – 3131Substrate; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi3 – 1715FAD2 PublicationsAdd
    BLAST
    Nucleotide bindingi37 – 382FAD2 Publications
    Nucleotide bindingi44 – 452FAD2 Publications
    Nucleotide bindingi49 – 513FAD2 Publications
    Nucleotide bindingi312 – 3176FAD2 Publications

    GO - Molecular functioni

    • cofactor binding Source: UniProtKB
    • D-amino-acid oxidase activity Source: UniProtKB
    • FAD binding Source: UniProtKB
    • protein dimerization activity Source: UniProtKB
    • receptor binding Source: UniProtKB

    GO - Biological processi

    • cellular nitrogen compound metabolic process Source: Reactome
    • D-alanine catabolic process Source: UniProtKB
    • dopamine biosynthetic process Source: UniProtKB
    • D-serine catabolic process Source: UniProtKB
    • D-serine metabolic process Source: UniProtKB
    • glyoxylate metabolic process Source: Reactome
    • leucine metabolic process Source: Ensembl
    • proline catabolic process Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03351-MONOMER.
    BRENDAi1.4.3.3. 2681.
    ReactomeiREACT_16925. Glyoxylate metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-amino-acid oxidase (EC:1.4.3.3)
    Short name:
    DAAO
    Short name:
    DAMOX
    Short name:
    DAO
    Gene namesi
    Name:DAO
    Synonyms:DAMOX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:2671. DAO.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • peroxisomal matrix Source: Reactome
    • peroxisomal membrane Source: UniProtKB
    • peroxisome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti803. Amyotrophic lateral sclerosis.
    PharmGKBiPA27139.

    Chemistry

    DrugBankiDB03147. Flavin adenine dinucleotide.

    Polymorphism and mutation databases

    BioMutaiDAO.
    DMDMi25453448.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 347347D-amino-acid oxidasePRO_0000162761Add
    BLAST

    Proteomic databases

    PaxDbiP14920.
    PRIDEiP14920.

    Expressioni

    Gene expression databases

    BgeeiP14920.
    CleanExiHS_DAO.
    ExpressionAtlasiP14920. baseline and differential.
    GenevisibleiP14920. HS.

    Organism-specific databases

    HPAiHPA038653.
    HPA038654.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRKAB2O437414EBI-3908043,EBI-1053424

    Protein-protein interaction databases

    BioGridi107980. 5 interactions.
    IntActiP14920. 2 interactions.
    STRINGi9606.ENSP00000228476.

    Structurei

    Secondary structure

    1
    347
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Helixi10 – 2314Combined sources
    Beta strandi25 – 284Combined sources
    Beta strandi31 – 377Combined sources
    Helixi40 – 423Combined sources
    Helixi44 – 474Combined sources
    Helixi63 – 7715Combined sources
    Turni78 – 803Combined sources
    Helixi84 – 874Combined sources
    Beta strandi89 – 10012Combined sources
    Turni106 – 1105Combined sources
    Beta strandi111 – 1166Combined sources
    Helixi119 – 1224Combined sources
    Beta strandi129 – 13911Combined sources
    Helixi141 – 15414Combined sources
    Beta strandi158 – 1614Combined sources
    Helixi167 – 1726Combined sources
    Beta strandi176 – 1805Combined sources
    Helixi183 – 1886Combined sources
    Beta strandi196 – 20611Combined sources
    Beta strandi212 – 2165Combined sources
    Turni219 – 2213Combined sources
    Beta strandi228 – 2314Combined sources
    Beta strandi233 – 2397Combined sources
    Helixi253 – 26614Combined sources
    Helixi268 – 2725Combined sources
    Beta strandi274 – 28512Combined sources
    Beta strandi290 – 2967Combined sources
    Beta strandi298 – 3014Combined sources
    Beta strandi303 – 3097Combined sources
    Helixi312 – 3143Combined sources
    Helixi315 – 33622Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    4QFCX-ray2.40A/B1-347[»]
    4QFDX-ray2.85A/B1-347[»]
    ProteinModelPortaliP14920.
    SMRiP14920. Positions 1-340.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14920.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi345 – 3473Microbody targeting signal

    Sequence similaritiesi

    Belongs to the DAMOX/DASOX family.Curated

    Phylogenomic databases

    eggNOGiCOG0665.
    GeneTreeiENSGT00390000018635.
    HOGENOMiHOG000046303.
    HOVERGENiHBG003493.
    InParanoidiP14920.
    KOiK00273.
    OMAiIHEHYHS.
    OrthoDBiEOG7B31NB.
    PhylomeDBiP14920.
    TreeFamiTF313887.

    Family and domain databases

    InterProiIPR006181. D-amino_acid_oxidase_CS.
    IPR023209. DAO.
    IPR006076. FAD-dep_OxRdtase.
    [Graphical view]
    PANTHERiPTHR11530. PTHR11530. 1 hit.
    PfamiPF01266. DAO. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000189. D-aa_oxidase. 1 hit.
    PROSITEiPS00677. DAO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14920-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG
    60 70 80 90 100
    LWQPYLSDPN NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE
    110 120 130 140 150
    AIPDPSWKDT VLGFRKLTPR ELDMFPDYGY GWFHTSLILE GKNYLQWLTE
    160 170 180 190 200
    RLTERGVKFF QRKVESFEEV AREGADVIVN CTGVWAGALQ RDPLLQPGRG
    210 220 230 240 250
    QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG IFQLGNWSEL
    260 270 280 290 300
    NNIQDHNTIW EGCCRLEPTL KNARIIGERT GFRPVRPQIR LEREQLRTGP
    310 320 330 340
    SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL
    Length:347
    Mass (Da):39,474
    Last modified:November 25, 2002 - v3
    Checksum:iA508E603872F3072
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311D → H in CAA31614 (PubMed:2901986).Curated
    Sequence conflicti279 – 2791R → A in CAA31614 (PubMed:2901986).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS9122.1.
    PIRiS01340.
    RefSeqiNP_001908.3. NM_001917.4.
    UniGeneiHs.113227.

    Genome annotation databases

    EnsembliENST00000228476; ENSP00000228476; ENSG00000110887.
    GeneIDi1610.
    KEGGihsa:1610.
    UCSCiuc001tnq.4. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS9122.1.
    PIRiS01340.
    RefSeqiNP_001908.3. NM_001917.4.
    UniGeneiHs.113227.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    4QFCX-ray2.40A/B1-347[»]
    4QFDX-ray2.85A/B1-347[»]
    ProteinModelPortaliP14920.
    SMRiP14920. Positions 1-340.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107980. 5 interactions.
    IntActiP14920. 2 interactions.
    STRINGi9606.ENSP00000228476.

    Chemistry

    BindingDBiP14920.
    ChEMBLiCHEMBL5485.
    DrugBankiDB03147. Flavin adenine dinucleotide.

    Polymorphism and mutation databases

    BioMutaiDAO.
    DMDMi25453448.

    Proteomic databases

    PaxDbiP14920.
    PRIDEiP14920.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000228476; ENSP00000228476; ENSG00000110887.
    GeneIDi1610.
    KEGGihsa:1610.
    UCSCiuc001tnq.4. human.

    Organism-specific databases

    CTDi1610.
    GeneCardsiGC12P109273.
    HGNCiHGNC:2671. DAO.
    HPAiHPA038653.
    HPA038654.
    MIMi124050. gene.
    neXtProtiNX_P14920.
    Orphaneti803. Amyotrophic lateral sclerosis.
    PharmGKBiPA27139.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0665.
    GeneTreeiENSGT00390000018635.
    HOGENOMiHOG000046303.
    HOVERGENiHBG003493.
    InParanoidiP14920.
    KOiK00273.
    OMAiIHEHYHS.
    OrthoDBiEOG7B31NB.
    PhylomeDBiP14920.
    TreeFamiTF313887.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03351-MONOMER.
    BRENDAi1.4.3.3. 2681.
    ReactomeiREACT_16925. Glyoxylate metabolism.

    Miscellaneous databases

    ChiTaRSiDAO. human.
    EvolutionaryTraceiP14920.
    GenomeRNAii1610.
    NextBioi6618.
    PROiP14920.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP14920.
    CleanExiHS_DAO.
    ExpressionAtlasiP14920. baseline and differential.
    GenevisibleiP14920. HS.

    Family and domain databases

    InterProiIPR006181. D-amino_acid_oxidase_CS.
    IPR023209. DAO.
    IPR006076. FAD-dep_OxRdtase.
    [Graphical view]
    PANTHERiPTHR11530. PTHR11530. 1 hit.
    PfamiPF01266. DAO. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000189. D-aa_oxidase. 1 hit.
    PROSITEiPS00677. DAO. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
      , 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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "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.
    9. "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.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH FAD AND SYNTHETIC INHIBITOR.

    Entry informationi

    Entry nameiOXDA_HUMAN
    AccessioniPrimary (citable) accession number: P14920
    Secondary accession number(s): B2R7I5, Q16758, Q8N6R2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 25, 2002
    Last modified: June 24, 2015
    This is version 154 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.