OXDD3_CAEEL
ID OXDD3_CAEEL Reviewed; 383 AA.
AC O01739; Q08I98;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=D-aspartate oxidase 3;
DE Short=DASOX 3;
DE Short=DDO-3;
DE EC=1.4.3.1;
DE Flags: Precursor;
GN Name=ddo-3; ORFNames=F20H11.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-271, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-152 AND ASN-271, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [5]
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 [6]
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. Has no
CC activity towards L-amino acids or N-methyl-L-aspartic acid. May play a
CC role in the egg-laying events and maturation processes of the
CC reproductive organs. {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=3.81 mM for D-Asp {ECO:0000269|PubMed:20564561};
CC KM=0.68 mM for D-Glu {ECO:0000269|PubMed:20564561};
CC KM=8.87 mM for NMDA {ECO:0000269|PubMed:20564561};
CC Note=The values given are for the recombinant protein.;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in probable head mesodermal cells and
CC unidentified cells in the head, vulval muscles, hypodermis and the
CC gonad sheath cells in adult hermaphrodites. Also expressed in the
CC seminal vesicle and tail cells in adult males.
CC {ECO:0000269|PubMed:22393259}.
CC -!- DEVELOPMENTAL STAGE: Expression in head mesodermal cells detected from
CC L3 stage to adult stages, and in vulval muscles from L4 stage to adult
CC 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. They also show delay in growth to adulthood
CC and an extended life span. Mutant worms have high D-Glu content at both
CC egg and young adult stages and a high L-Trp level at young adult stage
CC 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; AB275893; BAF34316.1; -; mRNA.
DR EMBL; FO081189; CCD69778.1; -; Genomic_DNA.
DR PIR; F88486; F88486.
DR RefSeq; NP_498453.1; NM_066052.4.
DR AlphaFoldDB; O01739; -.
DR SMR; O01739; -.
DR BioGRID; 49534; 4.
DR DIP; DIP-25818N; -.
DR IntAct; O01739; 1.
DR STRING; 6239.F20H11.5; -.
DR BindingDB; O01739; -.
DR ChEMBL; CHEMBL3351211; -.
DR iPTMnet; O01739; -.
DR EPD; O01739; -.
DR PaxDb; O01739; -.
DR PeptideAtlas; O01739; -.
DR EnsemblMetazoa; F20H11.5.1; F20H11.5.1; WBGene00017648.
DR GeneID; 184746; -.
DR KEGG; cel:CELE_F20H11.5; -.
DR UCSC; F20H11.5; c. elegans.
DR CTD; 184746; -.
DR WormBase; F20H11.5; CE09514; WBGene00017648; ddo-3.
DR eggNOG; KOG3923; Eukaryota.
DR GeneTree; ENSGT00390000018635; -.
DR HOGENOM; CLU_034311_0_2_1; -.
DR InParanoid; O01739; -.
DR OMA; YKVVHNY; -.
DR OrthoDB; 1363414at2759; -.
DR PhylomeDB; O01739; -.
DR Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-CEL-9033241; Peroxisomal protein import.
DR SABIO-RK; O01739; -.
DR PRO; PR:O01739; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00017648; Expressed in germ line (C elegans) and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; 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; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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 FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..383
FT /note="D-aspartate oxidase 3"
FT /id="PRO_0000248529"
FT BINDING 20..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 55..56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 62..63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 67..69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 334..338
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 383 AA; 42502 MW; CECAB15AEC1E93B5 CRC64;
MLYALLLLFG GVSTVSSLRV AVVGEGVIGL STATAILDLA EKRNIPAPEI HIFHHKPFEK
ILSRHIAGLF RIDSGSEIDR KYGYDTFEKL ATLWREYGGL SGVQLVSGHI LSDSKTKLDS
QRESYGSLVY NYRDLAEPEL FGPTSLFDLP RNTTTRGIHY TAYTSEGLRF CPFLKKELMT
KGVRFTQRRI GNLEELGAEF DVVVNSAGLL GGVLAGDDAG NMKPIRGVLI RVDAPWQKHF
LYRDFSTITI PVIDHVYMGT VKQEGAFGPN NVTSADIQDI TSRYVALQPS FKRVHMLSSF
VGYRPGRKQV RVEKQIRETN GSKKFTVVHN YGHSGNGFTL GYGSAVHAAH IVLDLPLDAY
HGLVPEPLPI NATISEWVKY LDD
