OXDD2_CAEEL
ID OXDD2_CAEEL Reviewed; 334 AA.
AC Q19564; Q08I99; Q8I7K8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=D-aspartate oxidase 2;
DE Short=DASOX 2;
DE Short=DDO-2;
DE EC=1.4.3.1;
GN Name=ddo-2; ORFNames=F18E3.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), 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], AND ALTERNATIVE SPLICING.
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,
RP COFACTOR, AND 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;
CC Evidence={ECO:0000269|PubMed:20564561};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:20564561};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 mM for D-Asp {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=0.25 mM for D-Glu {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=1.84 mM for NMDA {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=4.20 mM for D-Asp {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=0.80 mM for D-Glu {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=9.23 mM for NMDA {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC Vmax=4.40 umol/min/mg enzyme with D-Asp as substrate
CC {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
CC Vmax=3.03 umol/min/mg enzyme with D-Glu as substrate
CC {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
CC Vmax=4.31 umol/min/mg enzyme with NMDA as substrate
CC {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q19564-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q19564-2; Sequence=VSP_014356, VSP_014357, VSP_014358,
CC VSP_014359;
CC -!- TISSUE SPECIFICITY: Expressed in the intestinal cells, pharyngeal
CC muscles, and body wall muscles in adult hermaphrodites.
CC {ECO:0000269|PubMed:22393259}.
CC -!- DEVELOPMENTAL STAGE: Expression detected in the intestinal cells from
CC comma-stage embryo to adult stages, and also in the pharyngeal and body
CC wall muscles from larva to adult stages. {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 also exhibit decreased
CC fertilization rates but do not show any change in physical appearance.
CC {ECO:0000269|PubMed:22393259}.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR EMBL; AB275892; BAF34315.1; -; mRNA.
DR EMBL; FO081172; CCD69662.1; -; Genomic_DNA.
DR EMBL; FO081172; CCD69663.1; -; Genomic_DNA.
DR PIR; T29219; T29219.
DR RefSeq; NP_504908.1; NM_072507.4.
DR AlphaFoldDB; Q19564; -.
DR SMR; Q19564; -.
DR BioGRID; 44175; 22.
DR STRING; 6239.F18E3.7a; -.
DR BindingDB; Q19564; -.
DR ChEMBL; CHEMBL3351209; -.
DR EPD; Q19564; -.
DR PaxDb; Q19564; -.
DR PeptideAtlas; Q19564; -.
DR PRIDE; Q19564; -.
DR EnsemblMetazoa; F18E3.7a.1; F18E3.7a.1; WBGene00017565. [Q19564-1]
DR EnsemblMetazoa; F18E3.7a.2; F18E3.7a.2; WBGene00017565. [Q19564-1]
DR GeneID; 179130; -.
DR UCSC; F18E3.7b; c. elegans. [Q19564-1]
DR CTD; 179130; -.
DR WormBase; F18E3.7a; CE07083; WBGene00017565; ddo-2. [Q19564-1]
DR eggNOG; KOG3923; Eukaryota.
DR GeneTree; ENSGT00390000018635; -.
DR HOGENOM; CLU_034311_0_2_1; -.
DR InParanoid; Q19564; -.
DR OMA; PGMREPK; -.
DR OrthoDB; 1363414at2759; -.
DR PhylomeDB; Q19564; -.
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; Q19564; -.
DR PRO; PR:Q19564; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00017565; Expressed in larva and 4 other tissues.
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; IDA:UniProtKB.
DR GO; GO:0047821; F:D-glutamate oxidase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0006533; P:aspartate catabolic process; 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 PROSITE; PS00677; DAO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; FAD; Flavoprotein; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..334
FT /note="D-aspartate oxidase 2"
FT /id="PRO_0000162772"
FT BINDING 8..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 38..39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 45..46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 50..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 310..314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..222
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_014356"
FT VAR_SEQ 223..228
FT /note="TFTIPK -> MCQIFR (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_014357"
FT VAR_SEQ 268..273
FT /note="EPKIIK -> VRISFF (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_014358"
FT VAR_SEQ 274..334
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_014359"
SQ SEQUENCE 334 AA; 37608 MW; 90B1731A702BB6FD CRC64;
MANIIPKIAI IGEGVIGCTS ALQISKAIPN AKITVLHDKP FKKSCSAGPA GLFRIDYEEN
TEYGRASFAW FSHLYRTTKG SETGVKLVSG HIQSDNLESL KQQQRAYGDI VYNFRFLDDR
ERLDIFPEPS KHCIHYTAYA SEGNKYVPYL KNLLLEQKIE FKQQEVTSLD AVADAGYDVI
VNCAGLYGGK LAGDDDTCYP IRGVILEVDA PWHKHFNYRD FTTFTIPKEH SVVVGSTKQD
NRWDLEITDE DRNDILKRYI ALHPGMREPK IIKEWSALRP GRKHVRIEAQ KRTSVGNSKD
YMVVHHYGHG SNGFTLGWGT AIEATKLVKT ALGL
