OXDA_CAVPO
ID OXDA_CAVPO Reviewed; 347 AA.
AC Q9Z1M5;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Cerebellum;
RX PubMed=10376208; DOI=10.3109/10425179909008422;
RA Konno R., Kurabayashi A., Tsuchiya M., Niwa A.;
RT "Guinea pig D-amino acid oxidase cDNA and phylogenetic position.";
RL DNA Seq. 10:85-91(1999).
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; AJ007710; CAA07616.1; -; mRNA.
DR RefSeq; NP_001166518.1; NM_001173047.1.
DR AlphaFoldDB; Q9Z1M5; -.
DR SMR; Q9Z1M5; -.
DR STRING; 10141.ENSCPOP00000007341; -.
DR Ensembl; ENSCPOT00000034560; ENSCPOP00000027474; ENSCPOG00000008164.
DR GeneID; 100192327; -.
DR KEGG; cpoc:100192327; -.
DR CTD; 1610; -.
DR eggNOG; KOG3923; Eukaryota.
DR GeneTree; ENSGT00390000018635; -.
DR HOGENOM; CLU_034311_0_1_1; -.
DR InParanoid; Q9Z1M5; -.
DR OMA; LWWPYRI; -.
DR OrthoDB; 1363414at2759; -.
DR TreeFam; TF313887; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000008164; Expressed in adult mammalian kidney and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0055130; P:D-alanine catabolic process; IEA:Ensembl.
DR GO; GO:0036088; P:D-serine catabolic process; IEA:Ensembl.
DR GO; GO:0042416; P:dopamine biosynthetic process; IEA:Ensembl.
DR GO; GO:0006562; P:proline catabolic process; IEA:Ensembl.
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_0000162759"
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; 39284 MW; 3B86E534272057C4 CRC64;
MRVVVIGAGV IGLSTALCIC ERYHSVLQQL DLRVYADRFT PLTNTDVAAG LWQPYLSGPD
NPQEVEWNQQ TFDYLLSHIH SPNAEQMGLA LVSGYNLFRE AVPDPFWKNM VLGFRKLTPR
ELDVFPDYGY GWFHTSLIIE GKSYLAWLTE RLTERGVKFF QRKVESLEEV ARGGADVIIN
CTGVWAGALQ PDPLLQPGRG QIIKVNAPWI KHFILTHDPE RGIYKSPYII PGIQEVTLGG
IFQLGNWNEI NSTQDHNTIW KGCCSLEPTL RNARIVGEYT GFRPVRPQLR LEREQLRVGS
ANTEVIHNYG HGGYGLTIHW GCALEAAKLF GKILEEKELY RMPPSHL
