ID   OXDA_CRIGR              Reviewed;         346 AA.
AC   Q9Z302;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=D-amino-acid oxidase;
DE            Short=DAAO;
DE            Short=DAMOX;
DE            Short=DAO;
DE            EC=1.4.3.3;
GN   Name=DAO;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Konno R.;
RT   "Hamster D-amino-acid oxidase.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates the level of the neuromodulator D-serine in the
CC       brain. Has high activity towards D-DOPA and contributes to dopamine
CC       synthesis. Could act as a detoxifying agent which removes D-amino acids
CC       accumulated during aging. Acts on a variety of D-amino acids with a
CC       preference for those having small hydrophobic side chains followed by
CC       those bearing polar, aromatic, and basic groups. Does not act on acidic
CC       amino acids (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:59871; EC=1.4.3.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR   EMBL; AB016530; BAA74715.1; -; mRNA.
DR   RefSeq; NP_001231338.1; NM_001244409.1.
DR   AlphaFoldDB; Q9Z302; -.
DR   SMR; Q9Z302; -.
DR   STRING; 10029.XP_007607195.1; -.
DR   GeneID; 100689280; -.
DR   KEGG; cge:100689280; -.
DR   CTD; 1610; -.
DR   eggNOG; KOG3923; Eukaryota.
DR   OrthoDB; 1363414at2759; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProt.
DR   InterPro; IPR006181; D-amino_acid_oxidase_CS.
DR   InterPro; IPR023209; DAO.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   PANTHER; PTHR11530; PTHR11530; 1.
DR   Pfam; PF01266; DAO; 1.
DR   PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR   PROSITE; PS00677; DAO; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Oxidoreductase; Peroxisome.
FT   CHAIN           1..346
FT                   /note="D-amino-acid oxidase"
FT                   /id="PRO_0000162760"
FT   MOTIF           344..346
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000250"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         36..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         43..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         48..50
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         311..315
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  39146 MW;  320FD17769437F3C CRC64;
     MRVVVIGAGV IGLSTALCIH ERFSPVQPLH MKIYADRFTP FTTSDVAAGF WQPYLSDPRN
     PQEVEWNQQT FDYLLSHIHS PNAEKMGLSL ISGYNLFKEE VPDPFWRNTV LGFRKLTPRE
     MDIFPDYGYG WFNTSLTLEG KSYLPWLTER LTERGVKLFH RKVESFEEVA RGGADVIINC
     TGVWAGALQA DTSLQPGRGQ IIQVEAPWMK HFILTHDPRL GIYNSPYIIP GSKTVTLGGV
     FQLGNWNELN SVHDHNTIWK SCCKLEPTLK NAKIVGELTG FRPVRHQVRL KKKQLHFGSS
     SVEVIHNYGH GGYGLTIHWG CAMEAANLFG KILEEKKLSR MPASHL