ID   OXDD2_CAEEL             Reviewed;         334 AA.
AC   O45307;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 2.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=D-aspartate oxidase 2;
DE            Short=DASOX 2;
DE            EC=1.4.3.1;
DE   AltName: Full=DDO 2;
GN   ORFNames=C47A10.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=Bristol N2;
RX   PubMed=17140416; DOI=10.1111/j.1742-4658.2006.05571.x;
RA   Katane M., Seida Y., Sekine M., Furuchi T., Homma H.;
RT   "Caenorhabditis elegans has two genes encoding functional D-aspartate
RT   oxidases.";
RL   FEBS J. 274:137-149(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Selectively catalyzes the oxidative deamination of D-
CC       aspartate and its N-methylated derivative, N-methyl D-aspartate.
CC   -!- CATALYTIC ACTIVITY: D-aspartate + H(2)O + O(2) = oxaloacetate +
CC       NH(3) + H(2)O(2).
CC   -!- COFACTOR: FAD.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.02 mM for D-Asp;
CC         KM=0.23 mM for D-Glu;
CC         KM=0.84 mM for NMDA;
CC         Vmax=6.16 umol/min/mg enzyme with D-Asp as substrate;
CC         Vmax=7.62 umol/min/mg enzyme with D-Glu as substrate;
CC         Vmax=8.80 umol/min/mg enzyme with NMDA as substrate;
CC   -!- SUBCELLULAR LOCATION: Peroxisome (Probable).
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC   -!- CAUTION: The conserved active site Tyr residue in position 221 is
CC       replaced by a Phe.
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DR   EMBL; AB275891; BAF34314.1; -; mRNA.
DR   EMBL; Z81484; CAB03970.2; -; Genomic_DNA.
DR   PIR; T19979; T19979.
DR   RefSeq; NP_507491.2; -.
DR   UniGene; Cel.4486; -.
DR   HSSP; P00371; 1AN9.
DR   Ensembl; C47A10.5; Caenorhabditis elegans.
DR   GeneID; 183530; -.
DR   KEGG; cel:C47A10.5; -.
DR   NMPDR; fig|6239.3.peg.21577; -.
DR   WormBase; WBGene00008127; C47A10.5.
DR   WormPep; C47A10.5; CE36691.
DR   OMA; O45307; HYGHGGN.
DR   BRENDA; 1.4.3.1; 672.
DR   NextBio; 921480; -.
DR   ArrayExpress; O45307; -.
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:InterPro.
DR   GO; GO:0008445; F:D-aspartate 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   1: Evidence at protein level;
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase; Peroxisome.
FT   CHAIN         1    334       D-aspartate oxidase 2.
FT                                /FTId=PRO_0000317123.
FT   NP_BIND       5     19       FAD (By similarity).
FT   NP_BIND      35     36       FAD (By similarity).
FT   NP_BIND      42     43       FAD (By similarity).
FT   NP_BIND      47     49       FAD (By similarity).
FT   NP_BIND     307    311       FAD (By similarity).
FT   MOTIF       332    334       Microbody targeting signal (Potential).
FT   BINDING     163    163       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     276    276       Substrate (By similarity).
FT   BINDING     308    308       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     312    312       FAD (By similarity).
SQ   SEQUENCE   334 AA;  37637 MW;  7C30DFEA2EE5F22C CRC64;
     MTPKIAIIGE GVIGCSTALQ VAQAVPDARV TVLSDRPFEQ TCSFGPAGLF RIDDIANREF
     GKSTFDWFAH LHRTEKGDKT GVKLLSGHIQ SDSKERLEQQ QKAYGDIVYN FRFLEKREIL
     DLFPNPSEHC IHYTAFASEG NKYVPYLKFQ CQARGVEFLH RKVRDLEELA NEGYDVIVNC
     AGLSGGTLAG DDDSVYPIRG VVLDVEAHWH KHFNYKDFIT FTIPKENSVV IGSVKQENRW
     DLEITDVDRK DILERYVALH PAMREPKILG EWSGLRPARK TIRIEKVEKK SEKSGKKYTV
     VHHYGHGGNG FTLGWGTAVE ATKLVKSALN SSKL
//