ID   OXDA_RABIT              Reviewed;         347 AA.
AC   P22942;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 113.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=1980495; DOI=10.1093/oxfordjournals.jbchem.a123214;
RA   Momoi K., Fukui K., Tada M., Miyake Y.;
RT   "Gene expression of D-amino acid oxidase in rabbit kidney.";
RL   J. Biochem. 108:406-413(1990).
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;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR   EMBL; D12494; BAA02058.1; -; mRNA.
DR   PIR; JX0132; JX0132.
DR   RefSeq; NP_001075658.1; NM_001082189.1.
DR   AlphaFoldDB; P22942; -.
DR   SMR; P22942; -.
DR   STRING; 9986.ENSOCUP00000015665; -.
DR   GeneID; 100008977; -.
DR   KEGG; ocu:100008977; -.
DR   CTD; 1610; -.
DR   eggNOG; KOG3923; Eukaryota.
DR   InParanoid; P22942; -.
DR   OrthoDB; 1363414at2759; -.
DR   Proteomes; UP000001811; 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_0000162764"
FT   MOTIF           345..347
FT                   /note="Microbody targeting signal"
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;  38590 MW;  E22CFC0D944AFA61 CRC64;
     MRVVVIGAGV IGLSTALCIH ELYHSALQPL DMTIYADRFT PLTNTDVAAG LWQPYLSDPS
     NPQEADWSRQ TFNHLLSHIH SPSAEKMGLA LISGYNLFRK AVPDPSWKDT VLGFRKLTLR
     ELDMFPGYSY GWFNTSLILD GRSYLQWLTK RLTERGVKLF QRKVESFDEV AGGGVDVIVN
     CTGVWASALQ PDPLLQPGRG QIIKVDAPWV KHFIITHDPE SGIYKSPYII PGVHAVTLGG
     IFQMGNWSEG NSTDDHNTIW KGCCSLEPTL KDARIVGEWT GFRPVRPQIR LGREQLSAGP
     SKTEVIHNYG HGGYGLTIHW GCALEAAKLF GKILEEKKSS RMPPSHL