ID   OXDA_MACFA              Reviewed;         347 AA.
AC   A2V9Y8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 56.
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; ORFNames=Qlv-U252A-C12;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RA   Kobayashi M., Uno Y., Suzuki Y., Osada N., Kusuda J., Sugano S., Inoue I.,
RA   Hashimoto K.;
RT   "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT   microarray.";
RL   Submitted (AUG-2006) 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; AK240621; BAF47375.1; -; mRNA.
DR   RefSeq; NP_001270878.1; NM_001283949.1.
DR   AlphaFoldDB; A2V9Y8; -.
DR   SMR; A2V9Y8; -.
DR   STRING; 9541.XP_005572219.1; -.
DR   GeneID; 102146162; -.
DR   CTD; 1610; -.
DR   eggNOG; KOG3923; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
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; Reference proteome.
FT   CHAIN           1..347
FT                   /note="D-amino-acid oxidase"
FT                   /id="PRO_0000332729"
FT   MOTIF           345..347
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         37..38
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         44..45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         49..51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         312..316
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   347 AA;  39413 MW;  560F3A59A669AC53 CRC64;
     MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG FWQPYLSDPS
     NPKEADWSQQ TFDHLLSHIH SPNAEKLGLF LISGYNLFHE AIPNPSWKDT VLGFRKLTPR
     ELDIFPDYSY GWFHTSLILE GKNYLQWLTE RLTERGVKFF QRKVESFEEV AREGADVIVN
     CTGVWAGVLQ PDPLLQPGRG QIIKVDAPWI KHFILTHEPE SGIYNSPYII PGTQTVTLGG
     IFQLGNWNEL NNIQDHNTIW EGCCRLEPTL KNARIVDERT GFRPVRPKIR LEREQLRVGP
     SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS KMPPSHL