ID   OXDD_PIG                Reviewed;         341 AA.
AC   A3KCL7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=D-aspartate oxidase;
DE            Short=DASOX;
DE            Short=DDO;
DE            EC=1.4.3.1;
GN   Name=DDO;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Yamamoto A., Tanaka H., Ishida T., Horiike K.;
RT   "Purification, cDNA cloning and characterization of D-aspartate oxidase
RT   from porcine kidney.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Selectively catalyzes the oxidative deamination of D-
CC       aspartate and its N-methylated derivative, N-methyl D-aspartate.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate;
CC         Xref=Rhea:RHEA:12512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29990; EC=1.4.3.1;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR   EMBL; AB271762; BAF47961.1; -; mRNA.
DR   RefSeq; NP_001090895.1; NM_001097426.1.
DR   AlphaFoldDB; A3KCL7; -.
DR   SMR; A3KCL7; -.
DR   STRING; 9823.ENSSSCP00000004749; -.
DR   PaxDb; A3KCL7; -.
DR   PeptideAtlas; A3KCL7; -.
DR   GeneID; 100037287; -.
DR   KEGG; ssc:100037287; -.
DR   CTD; 8528; -.
DR   eggNOG; KOG3923; Eukaryota.
DR   InParanoid; A3KCL7; -.
DR   OrthoDB; 1363414at2759; -.
DR   BioCyc; MetaCyc:MON-14481; -.
DR   BRENDA; 1.4.3.1; 6170.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003884; F:D-amino-acid oxidase activity; IBA:GO_Central.
DR   GO; GO:0008445; F:D-aspartate oxidase activity; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006533; P:aspartate catabolic process; IBA:GO_Central.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IBA:GO_Central.
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..341
FT                   /note="D-aspartate oxidase"
FT                   /id="PRO_0000330729"
FT   MOTIF           339..341
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   BINDING         6..20
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         166
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         307..311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  37316 MW;  97AFE48AD15A0D23 CRC64;
     MDTVRIAVVG AGVMGLSTAV CIFKLVPGCS ITVISDKFTP ETTSDVAAGM LIPPVYPDTP
     IHKQKQWFKD TFDHLFAIAN SAEAKDAGVL LVSGWQIFQS APTEEVPFWA DVVLGFRKMT
     KNELKKFPQH VCGQAFTTLK YEGPTYLPWL EKRVKGSGGL VLTRRVEDLW ELHPSFDIVV
     NCSGLGSKQL VGDMDIFPVR GQVLKVQAPW VKHFIRDGSG LTYIYPGLAN VTLGGTRQKG
     DWNLSPNAEI SKQILSRCCA LEPSLRGACD IREKVGLRPS RPGVRLEKEL LVQGSQRLPV
     VHNYGHGSGG IAMHWGTALE AARLVSECVQ ALRTPAPKSK L