OXDA_CAEEL
ID OXDA_CAEEL Reviewed; 322 AA.
AC Q95XG9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=D-amino-acid oxidase;
DE Short=DAAO;
DE Short=DAMOX;
DE Short=DAO;
DE EC=1.4.3.3;
DE Flags: Precursor;
GN Name=daao-1; ORFNames=Y69A2AR.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:BAF34313.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, STEREOSPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:BAF34313.1};
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]
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,
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: Catalyzes oxidative deamination of D-amino acids, in
CC particular D-alanine, and could be responsible for the degradation of
CC diet-derived D-alanine in the intestine. Acts on a variety of D-amino
CC acids with greater preference towards those with basic and aromatic
CC groups followed by those bearing neutral groups. Has no activity
CC against acidic D-amino acids, L-amino acids or N-methyl-L-aspartic
CC acid. May play a role in egg-laying events and early development.
CC {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561,
CC ECO:0000269|PubMed:22393259}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:17140416,
CC 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=1.72 mM for D-Ala {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=6.89 mM for D-Ala {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=0.11 mM for D-Arg {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=1.01 mM for D-Arg {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=1.22 mM for D-Met {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=2.72 mM for D-Phe {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=20.0 mM for D-Ser {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC KM=2.89 mM for D-His {ECO:0000269|PubMed:17140416,
CC ECO:0000269|PubMed:20564561};
CC Vmax=5.41 umol/min/mg enzyme with D-Ala as substrate
CC {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
CC Vmax=2.52 umol/min/mg enzyme with D-Arg as substrate
CC {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
CC Vmax=7.43 umol/min/mg enzyme with D-Met as substrate
CC {ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
CC Note=The values given here are for the recombinant protein.;
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14920}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17140416,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the intestine.
CC {ECO:0000269|PubMed:22393259}.
CC -!- DEVELOPMENTAL STAGE: Expression detected initially in the gastrula-
CC stage embryos and continuing throughout all developmental stages to
CC adulthood. {ECO:0000269|PubMed:22393259}.
CC -!- DISRUPTION PHENOTYPE: Mutant worms (tm3673) exhibit decreased egg-
CC laying capacity with smaller brood size and lower hatching rates at 25
CC degrees Celsius. Worms do not show any change in physical appearance.
CC {ECO:0000269|PubMed:22393259}.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000255}.
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DR EMBL; AB275890; BAF34313.1; -; mRNA.
DR EMBL; FO081818; CCD74112.1; -; Genomic_DNA.
DR RefSeq; NP_500234.3; NM_067833.5.
DR AlphaFoldDB; Q95XG9; -.
DR SMR; Q95XG9; -.
DR STRING; 6239.Y69A2AR.5; -.
DR BindingDB; Q95XG9; -.
DR ChEMBL; CHEMBL3351208; -.
DR PaxDb; Q95XG9; -.
DR PeptideAtlas; Q95XG9; -.
DR EnsemblMetazoa; Y69A2AR.5.1; Y69A2AR.5.1; WBGene00022076.
DR GeneID; 3565775; -.
DR KEGG; cel:CELE_Y69A2AR.5; -.
DR UCSC; Y69A2AR.5; c. elegans.
DR CTD; 3565775; -.
DR WormBase; Y69A2AR.5; CE36371; WBGene00022076; daao-1.
DR eggNOG; KOG3923; Eukaryota.
DR GeneTree; ENSGT00390000018635; -.
DR HOGENOM; CLU_034311_0_2_1; -.
DR InParanoid; Q95XG9; -.
DR OMA; DEKCYPT; -.
DR OrthoDB; 1363414at2759; -.
DR PhylomeDB; Q95XG9; -.
DR Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-CEL-9033241; Peroxisomal protein import.
DR SABIO-RK; Q95XG9; -.
DR PRO; PR:Q95XG9; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00022076; Expressed in adult organism and 2 other tissues.
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; IDA:WormBase.
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 PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR PROSITE; PS00677; DAO; 1.
PE 1: Evidence at protein level;
KW Developmental protein; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Peroxisome; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..322
FT /note="D-amino-acid oxidase"
FT /id="PRO_0000317125"
FT MOTIF 320..322
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 4..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 34..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 41..42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 46..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 293..297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 322 AA; 36117 MW; 862044F6523AD76E CRC64;
MPKIAVLGAG INGIASALAI QERLPNCEVT IIAEKFSPNT TSDVAAGLIE PFLCDDDVDR
IINWTSATIS RIHEYQADGN PGAEEQSGYW LQSVKSEPKW LKLMKNVHIL TDAEMKQVAR
RPEHKFGIFY TTWYLEPTPY IKWCTDKFLK NGGKFKKQKI ENIDDVARSY DVTVNCTGLG
SRALIGDKEV YPTRGQILKV SCPRVKHFFI DDKYYALLND STITLGGTFE AHQWDLTINS
ELSQKILKEN IHNIPSLRTA QILSSHVDMR PSRGTVRLQA ELGRSLVHNY GHGGSGITLH
WGCALECAEI VENVLKMKKS KL
