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   16-JUN-2009, entry version 59.
DE   RecName: Full=D-amino-acid oxidase;
DE            Short=DAMOX;
DE            Short=DAAO;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   MEDLINE=98146267; 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
RT   intermediate form between mouse and other mammalian D-amino-acid
RT   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Regulates the level of the neuromodulator D-serine in
CC       the brain. Has high activity towards D-DOPA and contributes to
CC       dopamine synthesis. Could act as a detoxifying agent which removes
CC       D-amino acids accumulated during aging. Acts on a variety of D-
CC       amino acids with a preference for those having small hydrophobic
CC       side chains followed by those bearing polar, aromatic, and basic
CC       groups. Does not act on acidic amino acids.
CC   -!- CATALYTIC ACTIVITY: A D-amino acid + H(2)O + O(2) = a 2-oxo acid +
CC       NH(3) + H(2)O(2).
CC   -!- COFACTOR: FAD.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
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DR   EMBL; AB003400; BAA22840.1; -; mRNA.
DR   EMBL; BC088395; AAH88395.1; -; mRNA.
DR   IPI; IPI00326225; -.
DR   RefSeq; NP_446078.1; -.
DR   UniGene; Rn.81058; -.
DR   HSSP; P00371; 1AN9.
DR   SMR; O35078; 1-339.
DR   PRIDE; O35078; -.
DR   Ensembl; ENSRNOG00000000694; Rattus norvegicus.
DR   GeneID; 114027; -.
DR   KEGG; rno:114027; -.
DR   RGD; 621138; Dao1.
DR   HOVERGEN; O35078; -.
DR   BRENDA; 1.4.3.3; 248.
DR   NextBio; 618183; -.
DR   ArrayExpress; O35078; -.
DR   GermOnline; ENSRNOG00000000694; Rattus norvegicus.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006181; D-amino_acid_oxidase_CS.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01266; DAO; 1.
DR   PROSITE; PS00677; DAO; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Oxidoreductase; Peroxisome.
FT   CHAIN         1    346       D-amino-acid oxidase.
FT                                /FTId=PRO_0000162765.
FT   NP_BIND       3     17       FAD (By similarity).
FT   NP_BIND      36     37       FAD (By similarity).
FT   NP_BIND      43     44       FAD (By similarity).
FT   NP_BIND      48     50       FAD (By similarity).
FT   NP_BIND     311    315       FAD (By similarity).
FT   MOTIF       344    346       Microbody targeting signal.
FT   BINDING      52     52       Substrate (By similarity).
FT   BINDING     163    163       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     181    181       FAD (By similarity).
FT   BINDING     216    216       Substrate (By similarity).
FT   BINDING     227    227       Substrate (By similarity).
FT   BINDING     282    282       Substrate (By similarity).
FT   BINDING     312    312       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     316    316       FAD (By similarity).
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
//