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P14920

- OXDA_HUMAN

UniProt

P14920 - OXDA_HUMAN

Protein

D-amino-acid oxidase

Gene

DAO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (25 Nov 2002)
      Previous versions | rss
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    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

    FAD.

    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

    1. cofactor binding Source: UniProtKB
    2. D-amino-acid oxidase activity Source: UniProtKB
    3. FAD binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein dimerization activity Source: UniProtKB
    6. receptor binding Source: UniProtKB

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. D-alanine catabolic process Source: UniProtKB
    3. dopamine biosynthetic process Source: UniProtKB
    4. D-serine catabolic process Source: UniProtKB
    5. D-serine metabolic process Source: UniProtKB
    6. glyoxylate metabolic process Source: Reactome
    7. leucine metabolic process Source: Ensembl
    8. proline catabolic process Source: UniProtKB
    9. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03351-MONOMER.
    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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:2671. DAO.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. peroxisomal matrix Source: Reactome
    3. peroxisomal membrane Source: UniProtKB
    4. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti803. Amyotrophic lateral sclerosis.
    PharmGKBiPA27139.

    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

    ArrayExpressiP14920.
    BgeeiP14920.
    CleanExiHS_DAO.
    GenevestigatoriP14920.

    Organism-specific databases

    HPAiHPA038653.
    HPA038654.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi107980. 3 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 – 65
    Helixi10 – 2314
    Beta strandi25 – 284
    Beta strandi31 – 377
    Helixi40 – 423
    Helixi44 – 474
    Helixi63 – 7715
    Turni78 – 803
    Helixi84 – 874
    Beta strandi89 – 10012
    Turni106 – 1105
    Beta strandi111 – 1166
    Helixi119 – 1224
    Beta strandi129 – 13911
    Helixi141 – 15414
    Beta strandi158 – 1614
    Helixi167 – 1726
    Beta strandi176 – 1805
    Helixi183 – 1886
    Beta strandi196 – 20611
    Beta strandi212 – 2165
    Turni219 – 2213
    Beta strandi228 – 2314
    Beta strandi233 – 2397
    Helixi253 – 26614
    Helixi268 – 2725
    Beta strandi274 – 28512
    Beta strandi290 – 2967
    Beta strandi298 – 3014
    Beta strandi303 – 3097
    Helixi312 – 3143
    Helixi315 – 33622

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    HOGENOMiHOG000046303.
    HOVERGENiHBG003493.
    InParanoidiP14920.
    KOiK00273.
    OMAiPNAEKMG.
    OrthoDBiEOG7B31NB.
    PhylomeDBiP14920.
    TreeFamiTF313887.

    Family and domain databases

    InterProiIPR023209. D-aa_oxidase.
    IPR006181. D-amino_acid_oxidase_CS.
    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

    MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG    50
    LWQPYLSDPN NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE 100
    AIPDPSWKDT VLGFRKLTPR ELDMFPDYGY GWFHTSLILE GKNYLQWLTE 150
    RLTERGVKFF QRKVESFEEV AREGADVIVN CTGVWAGALQ RDPLLQPGRG 200
    QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG IFQLGNWSEL 250
    NNIQDHNTIW EGCCRLEPTL KNARIIGERT GFRPVRPQIR LEREQLRTGP 300
    SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL 347
    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:
    EMBL
    GenBank
    DDBJ
    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.
    XP_006719331.1. XM_006719268.1.
    UniGeneiHs.113227.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi25453448.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS9122.1.
    PIRi S01340.
    RefSeqi NP_001908.3. NM_001917.4.
    XP_006719331.1. XM_006719268.1.
    UniGenei Hs.113227.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DU8 X-ray 2.50 A/B/G/J 1-347 [» ]
    2E48 X-ray 2.90 A/B/C/D 1-347 [» ]
    2E49 X-ray 3.20 A/B/C/D 1-347 [» ]
    2E4A X-ray 2.60 A/B/C/D 1-347 [» ]
    2E82 X-ray 2.70 A/B/C/D 1-347 [» ]
    2GNZ model - A 1-339 [» ]
    3CUK X-ray 2.49 A/B/C/D 1-347 [» ]
    3G3E X-ray 2.20 A/B/C/D 1-347 [» ]
    3W4I X-ray 2.50 A/B/C/D 1-347 [» ]
    3W4J X-ray 2.74 A/B/C/D 1-347 [» ]
    3W4K X-ray 2.86 A/B/C/D 1-347 [» ]
    3ZNN X-ray 1.90 A/B 1-347 [» ]
    3ZNO X-ray 2.30 A/B 1-347 [» ]
    3ZNP X-ray 2.40 A/B 1-347 [» ]
    3ZNQ X-ray 2.75 A/B 1-347 [» ]
    ProteinModelPortali P14920.
    SMRi P14920. Positions 1-340.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107980. 3 interactions.
    IntActi P14920. 2 interactions.
    STRINGi 9606.ENSP00000228476.

    Chemistry

    BindingDBi P14920.
    ChEMBLi CHEMBL5485.

    Polymorphism databases

    DMDMi 25453448.

    Proteomic databases

    PaxDbi P14920.
    PRIDEi P14920.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228476 ; ENSP00000228476 ; ENSG00000110887 .
    GeneIDi 1610.
    KEGGi hsa:1610.
    UCSCi uc001tnq.4. human.

    Organism-specific databases

    CTDi 1610.
    GeneCardsi GC12P109273.
    HGNCi HGNC:2671. DAO.
    HPAi HPA038653.
    HPA038654.
    MIMi 124050. gene.
    neXtProti NX_P14920.
    Orphaneti 803. Amyotrophic lateral sclerosis.
    PharmGKBi PA27139.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0665.
    HOGENOMi HOG000046303.
    HOVERGENi HBG003493.
    InParanoidi P14920.
    KOi K00273.
    OMAi PNAEKMG.
    OrthoDBi EOG7B31NB.
    PhylomeDBi P14920.
    TreeFami TF313887.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03351-MONOMER.
    Reactomei REACT_16925. Glyoxylate metabolism.

    Miscellaneous databases

    EvolutionaryTracei P14920.
    GenomeRNAii 1610.
    NextBioi 6618.
    PROi P14920.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14920.
    Bgeei P14920.
    CleanExi HS_DAO.
    Genevestigatori P14920.

    Family and domain databases

    InterProi IPR023209. D-aa_oxidase.
    IPR006181. D-amino_acid_oxidase_CS.
    IPR006076. FAD-dep_OxRdtase.
    [Graphical view ]
    PANTHERi PTHR11530. PTHR11530. 1 hit.
    Pfami PF01266. DAO. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000189. D-aa_oxidase. 1 hit.
    PROSITEi PS00677. DAO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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. 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: October 1, 2014
    This is version 147 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