ID   OXDD_BOVIN              Reviewed;         341 AA.
AC   P31228; O02846; Q9TRA3;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=D-aspartate oxidase;
DE            Short=DASOX;
DE            Short=DDO;
DE            EC=1.4.3.1;
GN   Name=DDO;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney cortex;
RX   PubMed=9148742; DOI=10.1042/bj3220729;
RA   Simonic T., Duga S., Negri A., Tedeschi G., Malcovati M., Tenchini M.L.,
RA   Ronchi S.;
RT   "cDNA cloning and expression of the flavoprotein D-aspartate oxidase from
RT   bovine kidney cortex.";
RL   Biochem. J. 322:729-735(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-338.
RC   TISSUE=Kidney;
RX   PubMed=1601857; DOI=10.1016/s0021-9258(19)49778-0;
RA   Negri A., Ceciliani F., Tedeschi G., Simonic T., Ronchi S.;
RT   "The primary structure of the flavoprotein D-aspartate oxidase from beef
RT   kidney.";
RL   J. Biol. Chem. 267:11865-11871(1992).
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;
CC       Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR   EMBL; X95310; CAA64622.1; -; mRNA.
DR   PIR; A44132; A44132.
DR   RefSeq; NP_776333.1; NM_173908.2.
DR   AlphaFoldDB; P31228; -.
DR   SMR; P31228; -.
DR   STRING; 9913.ENSBTAP00000013892; -.
DR   BindingDB; P31228; -.
DR   ChEMBL; CHEMBL1795183; -.
DR   PaxDb; P31228; -.
DR   GeneID; 280763; -.
DR   KEGG; bta:280763; -.
DR   CTD; 8528; -.
DR   eggNOG; KOG3923; Eukaryota.
DR   InParanoid; P31228; -.
DR   OrthoDB; 1363414at2759; -.
DR   PRO; PR:P31228; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008445; F:D-aspartate 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   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Peroxisome;
KW   Reference proteome.
FT   CHAIN           1..341
FT                   /note="D-aspartate oxidase"
FT                   /id="PRO_0000162769"
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"
FT   MOD_RES         1
FT                   /note="Blocked amino end (Met)"
FT   VARIANT         228
FT                   /note="V -> I (in some molecules)"
FT   CONFLICT        274
FT                   /note="K -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        283
FT                   /note="S -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   341 AA;  37660 MW;  355EF4EE42C53B49 CRC64;
     MDTVRIAVVG AGVMGLSTAV CISKMVPGCS ITVISDKFTP ETTSDVAAGM LIPPTYPDTP
     IQKQKQWFKE TFDHLFAIVN SAEAEDAGVI LVSGWQIFQS IPTEEVPYWA DVVLGFRKMT
     KDELKKFPQH VFGHAFTTLK CEGPAYLPWL QKRVKGNGGL ILTRRIEDLW ELHPSFDIVV
     NCSGLGSRQL AGDSKIFPVR GQVLKVQAPW VKHFIRDSSG LTYIYPGVSN VTLGGTRQKG
     DWNLSPDAEI SKEILSRCCA LEPSLRGAYD LREKVGLRPT RPSVRLEKEL LAQDSRRLPV
     VHHYGHGSGG IAMHWGTALE ATRLVNECVQ VLRTPAPKSK L