OXDA_RAT
ID OXDA_RAT Reviewed; 346 AA.
AC O35078;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
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; Synonyms=Dao1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=9473656; DOI=10.1016/s0167-4781(97)00185-1;
RA Konno R.;
RT "Rat D-amino-acid oxidase cDNA: rat D-amino-acid oxidase as an intermediate
RT form between mouse and other mammalian D-amino-acid oxidases.";
RL Biochim. Biophys. Acta 1395:165-170(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.
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; AB003400; BAA22840.1; -; mRNA.
DR EMBL; BC088395; AAH88395.1; -; mRNA.
DR RefSeq; NP_446078.1; NM_053626.1.
DR AlphaFoldDB; O35078; -.
DR SMR; O35078; -.
DR BioGRID; 250263; 173.
DR IntAct; O35078; 1.
DR MINT; O35078; -.
DR STRING; 10116.ENSRNOP00000000881; -.
DR BindingDB; O35078; -.
DR ChEMBL; CHEMBL5756; -.
DR iPTMnet; O35078; -.
DR PhosphoSitePlus; O35078; -.
DR PaxDb; O35078; -.
DR PRIDE; O35078; -.
DR Ensembl; ENSRNOT00000094356; ENSRNOP00000079300; ENSRNOG00000054962.
DR GeneID; 114027; -.
DR KEGG; rno:114027; -.
DR UCSC; RGD:621138; rat.
DR CTD; 1610; -.
DR RGD; 621138; Dao.
DR eggNOG; KOG3923; Eukaryota.
DR GeneTree; ENSGT00390000018635; -.
DR InParanoid; O35078; -.
DR OrthoDB; 1363414at2759; -.
DR PhylomeDB; O35078; -.
DR TreeFam; TF313887; -.
DR BRENDA; 1.4.3.3; 5301.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR SABIO-RK; O35078; -.
DR PRO; PR:O35078; -.
DR Proteomes; UP000002494; Chromosome 12.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; ISO:RGD.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; ISO:RGD.
DR GO; GO:0071949; F:FAD binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0055130; P:D-alanine catabolic process; ISO:RGD.
DR GO; GO:0019478; P:D-amino acid catabolic process; IBA:GO_Central.
DR GO; GO:0036088; P:D-serine catabolic process; ISO:RGD.
DR GO; GO:0070178; P:D-serine metabolic process; ISO:RGD.
DR GO; GO:0042416; P:dopamine biosynthetic process; ISO:RGD.
DR GO; GO:0006551; P:leucine metabolic process; ISO:RGD.
DR GO; GO:0006562; P:proline catabolic process; ISO:RGD.
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..346
FT /note="D-amino-acid oxidase"
FT /id="PRO_0000162765"
FT MOTIF 344..346
FT /note="Microbody targeting signal"
FT BINDING 3..17
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 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 311..315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 38820 MW; 2C4697960137A4FE CRC64;
MRVAVIGAGV IGLSTALCIH ERYHPAQPLH MKIYADRFTP FTTSDVAAGL WQPYLSDPSN
PQEAEWNQQT FDHLQSCLHS PNAEKMGLAL ISGYNLFRDE VPDPFWKSTV LGFRKLTPSE
LDMFPDYSYG WFNTSLLLEG KSYLSWLTER LTERGVKFIH RKVASFEEVV RGGVDVIINC
TGVWAGALQA DASLQPGRGQ IIQVEAPWIK HFILTHDPSL GIYNSPYIIP GSKTVTLGGV
FQLGNWSELN SVHDHNTIWK SCCQLEPTLK NARIMGELTG FRPVRPQVRL ERERLRFGSS
SAEVIHNYGH GGYGLTIHWG CAMEAANLFG KILEEKNLSR MPPSHL
