OXDD2_CAEBR
ID OXDD2_CAEBR Reviewed; 331 AA.
AC A8WXM1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=D-aspartate oxidase 2 {ECO:0000250|UniProtKB:Q19564};
DE Short=DASOX 2 {ECO:0000250|UniProtKB:Q19564};
DE Short=DDO-2 {ECO:0000250|UniProtKB:Q19564};
DE EC=1.4.3.1 {ECO:0000250|UniProtKB:Q19564};
GN Name=ddo-2 {ECO:0000312|WormBase:CBG04460};
GN ORFNames=CBG04460 {ECO:0000312|WormBase:CBG04460};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAP25156.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP25156.1};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAP25156.1}
RP SEQUENCE REVISION.
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP25156.1};
RG The C.briggsae Sequencing Consortium;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Selectively catalyzes the oxidative deamination of D-
CC aspartate and its N-methylated derivative, N-methyl D-aspartate.
CC Highest catalytic efficiency for D-Glu followed by D-Asp and NMDA. May
CC play a role in the egg-laying events and early development of the worm,
CC in addition to quality control of the germ cells.
CC {ECO:0000250|UniProtKB:Q19564}.
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 Evidence={ECO:0000250|UniProtKB:Q19564};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P14920};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q19564}.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000255}.
CC -!- CAUTION: The conserved active site Tyr residue in position 221 is
CC replaced by a Phe. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE601251; CAP25156.1; -; Genomic_DNA.
DR RefSeq; XP_002634445.1; XM_002634399.1.
DR AlphaFoldDB; A8WXM1; -.
DR SMR; A8WXM1; -.
DR STRING; 6238.CBG04460; -.
DR PRIDE; A8WXM1; -.
DR EnsemblMetazoa; CBG04460.1; CBG04460.1; WBGene00027125.
DR GeneID; 8576441; -.
DR KEGG; cbr:CBG_04460; -.
DR CTD; 8576441; -.
DR WormBase; CBG04460; CBP06757; WBGene00027125; Cbr-ddo-2.
DR eggNOG; KOG3923; Eukaryota.
DR HOGENOM; CLU_034311_0_2_1; -.
DR InParanoid; A8WXM1; -.
DR OMA; PGMREPK; -.
DR OrthoDB; 1363414at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IBA:GO_Central.
DR GO; GO:0008445; F:D-aspartate oxidase activity; ISS:UniProtKB.
DR GO; GO:0047821; F:D-glutamate oxidase activity; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0006533; P:aspartate catabolic process; ISS:UniProtKB.
DR GO; GO:0019478; P:D-amino acid catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..331
FT /note="D-aspartate oxidase 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000317122"
FT BINDING 5..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P14920"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P14920"
FT BINDING 42..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P14920"
FT BINDING 47..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P14920"
FT BINDING 163
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P14920"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14920"
FT BINDING 307..311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P14920"
FT BINDING 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00371"
SQ SEQUENCE 331 AA; 37518 MW; 87BE766D5D2E7FBD CRC64;
MLPKIAVIGE GVIGCTSALQ IAKAIPNSKI TIFHDKPFEN SCSAGPAGLF RIDYEENTEY
GRASFAWFSH LYRTTKGAET GVKLVSGHIQ SDNLESLKQQ QRAYGDIVYN FRFLDDRERL
DIFPSPSKHC IHYTAYASEG NKYVPYLKRL LLEQKVEFQQ KNVENLDTIA DAGYDVIVNC
AGLYGGKLAG DDDQCYPIRG VILEVDAPWH KHFNYRDFTT FTIPKENSVV IGSTKQDNRW
DLEITDEDRN DILSRYIELH PGMREPKILK EWSALRPGRK HVRIESQQRK TTETGKEYTV
VHHYGHGSNG FTLGWGTAIE ATKLVKKALG L
