OXDD1_CAEEL
ID OXDD1_CAEEL Reviewed; 334 AA.
AC O45307;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=D-aspartate oxidase 1;
DE Short=DASOX 1;
DE Short=DDO-1;
DE EC=1.4.3.1;
GN Name=ddo-1; ORFNames=C47A10.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAF34314.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:BAF34314.1};
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] {ECO:0000312|EMBL:CAB03970.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX 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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, STEREOSPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20564561; DOI=10.1002/cbdv.200900294;
RA Katane M., Saitoh Y., Seida Y., Sekine M., Furuchi T., Homma H.;
RT "Comparative characterization of three D-aspartate oxidases and one D-amino
RT acid oxidase from Caenorhabditis elegans.";
RL Chem. Biodivers. 7:1424-1434(2010).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=22393259; DOI=10.1128/mcb.06513-11;
RA Saitoh Y., Katane M., Kawata T., Maeda K., Sekine M., Furuchi T.,
RA Kobuna H., Sakamoto T., Inoue T., Arai H., Nakagawa Y., Homma H.;
RT "Spatiotemporal localization of D-amino acid oxidase and D-aspartate
RT oxidases during development in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 32:1967-1983(2012).
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:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561,
CC ECO:0000269|PubMed:22393259}.
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; Evidence={ECO:0000269|PubMed:20564561,
CC ECO:0000305};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P31228};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.02 mM for D-Asp {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=0.23 mM for D-Glu {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=0.84 mM for NMDA {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=5.54 mM for D-Asp {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=1.06 mM for D-Glu {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=14.6 mM for NMDA {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC Vmax=6.16 umol/min/mg enzyme with D-Asp as substrate
CC {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
CC Vmax=7.62 umol/min/mg enzyme with D-Glu as substrate
CC {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
CC Vmax=8.80 umol/min/mg enzyme with NMDA as substrate
CC {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17140416,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestinal cells, hypodermis and
CC in unidentified cells in the head in adult hermaphrodites.
CC {ECO:0000269|PubMed:22393259}.
CC -!- DEVELOPMENTAL STAGE: Expression detected in the intestinal cells from
CC 3-fold stage embryo to adult stages, and also in the hypodermis and in
CC unidentified cells in the head from larval to adult stages.
CC {ECO:0000269|PubMed:22393259}.
CC -!- DISRUPTION PHENOTYPE: Mutant worms have decreased egg-laying capacity
CC at 20 degrees Celsius and decreased hatching rate and smaller brood
CC size at 25 degrees Celsius. Mutant worms have high D-Asp and D-Glu
CC content at both egg and young adult stage but do not show any change in
CC physical appearance. Mutant worms also exhibit decreased fertilization
CC rates. {ECO:0000269|PubMed:22393259}.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000255}.
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DR EMBL; AB275891; BAF34314.1; -; mRNA.
DR EMBL; Z81484; CAB03970.2; -; Genomic_DNA.
DR PIR; T19979; T19979.
DR RefSeq; NP_001256757.1; NM_001269828.1.
DR AlphaFoldDB; O45307; -.
DR SMR; O45307; -.
DR STRING; 6239.C47A10.5a; -.
DR BindingDB; O45307; -.
DR ChEMBL; CHEMBL3351210; -.
DR EPD; O45307; -.
DR PaxDb; O45307; -.
DR PeptideAtlas; O45307; -.
DR EnsemblMetazoa; C47A10.5a.1; C47A10.5a.1; WBGene00008127.
DR GeneID; 183530; -.
DR KEGG; cel:CELE_C47A10.5; -.
DR UCSC; C47A10.5; c. elegans.
DR CTD; 183530; -.
DR WormBase; C47A10.5a; CE36691; WBGene00008127; ddo-1.
DR eggNOG; KOG3923; Eukaryota.
DR GeneTree; ENSGT00390000018635; -.
DR HOGENOM; CLU_034311_0_2_1; -.
DR InParanoid; O45307; -.
DR OMA; TEYYDDR; -.
DR OrthoDB; 1363414at2759; -.
DR PhylomeDB; O45307; -.
DR BRENDA; 1.4.3.1; 1045.
DR Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-CEL-9033241; Peroxisomal protein import.
DR SABIO-RK; O45307; -.
DR PRO; PR:O45307; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00008127; Expressed in larva and 1 other tissue.
DR ExpressionAtlas; O45307; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IBA:GO_Central.
DR GO; GO:0008445; F:D-aspartate oxidase activity; IDA:UniProtKB.
DR GO; GO:0047821; F:D-glutamate oxidase activity; IDA:WormBase.
DR GO; GO:0071949; F:FAD binding; IDA: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 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..334
FT /note="D-aspartate oxidase 1"
FT /id="PRO_0000317123"
FT MOTIF 332..334
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 5..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P31228"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 42..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 47..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 307..311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
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
