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D-amino-acid oxidase (DAAO) (DAMOX) (DAO) (EC 1.4.3.3)

 OXDA_CAEEL              Reviewed;         322 AA.
Q95XG9;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 2.
12-SEP-2018, entry version 110.
RecName: Full=D-amino-acid oxidase;
Short=DAAO;
Short=DAMOX;
Short=DAO;
EC=1.4.3.3;
Flags: Precursor;
Name=daao-1; ORFNames=Y69A2AR.5;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305, ECO:0000312|EMBL:BAF34313.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
SPECIFICITY, STEREOSPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=Bristol N2 {ECO:0000312|EMBL:BAF34313.1};
PubMed=17140416; DOI=10.1111/j.1742-4658.2006.05571.x;
Katane M., Seida Y., Sekine M., Furuchi T., Homma H.;
"Caenorhabditis elegans has two genes encoding functional D-aspartate
oxidases.";
FEBS J. 274:137-149(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
STEREOSPECIFICITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=20564561; DOI=10.1002/cbdv.200900294;
Katane M., Saitoh Y., Seida Y., Sekine M., Furuchi T., Homma H.;
"Comparative characterization of three D-aspartate oxidases and one D-
amino acid oxidase from Caenorhabditis elegans.";
Chem. Biodivers. 7:1424-1434(2010).
[4]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
STRAIN=Bristol N2;
PubMed=22393259; DOI=10.1128/MCB.06513-11;
Saitoh Y., Katane M., Kawata T., Maeda K., Sekine M., Furuchi T.,
Kobuna H., Sakamoto T., Inoue T., Arai H., Nakagawa Y., Homma H.;
"Spatiotemporal localization of D-amino acid oxidase and D-aspartate
oxidases during development in Caenorhabditis elegans.";
Mol. Cell. Biol. 32:1967-1983(2012).
-!- FUNCTION: Catalyzes oxidative deamination of D-amino acids, in
particular D-alanine, and could be responsible for the degradation
of diet-derived D-alanine in the intestine. Acts on a variety of
D-amino acids with greater preference towards those with basic and
aromatic groups followed by those bearing neutral groups. Has no
activity against acidic D-amino acids, L-amino acids or N-methyl-
L-aspartic acid. May play a role in egg-laying events and early
development. {ECO:0000269|PubMed:17140416,
ECO:0000269|PubMed:20564561, ECO:0000269|PubMed:22393259}.
-!- CATALYTIC ACTIVITY: A D-amino acid + H(2)O + O(2) = a 2-oxo acid +
NH(3) + H(2)O(2). {ECO:0000269|PubMed:17140416,
ECO:0000269|PubMed:20564561}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:20564561};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.72 mM for D-Ala {ECO:0000269|PubMed:17140416,
ECO:0000269|PubMed:20564561};
KM=6.89 mM for D-Ala {ECO:0000269|PubMed:17140416,
ECO:0000269|PubMed:20564561};
KM=0.11 mM for D-Arg {ECO:0000269|PubMed:17140416,
ECO:0000269|PubMed:20564561};
KM=1.01 mM for D-Arg {ECO:0000269|PubMed:17140416,
ECO:0000269|PubMed:20564561};
KM=1.22 mM for D-Met {ECO:0000269|PubMed:17140416,
ECO:0000269|PubMed:20564561};
KM=2.72 mM for D-Phe {ECO:0000269|PubMed:17140416,
ECO:0000269|PubMed:20564561};
KM=20.0 mM for D-Ser {ECO:0000269|PubMed:17140416,
ECO:0000269|PubMed:20564561};
KM=2.89 mM for D-His {ECO:0000269|PubMed:17140416,
ECO:0000269|PubMed:20564561};
Vmax=5.41 umol/min/mg enzyme with D-Ala as substrate
{ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
Vmax=2.52 umol/min/mg enzyme with D-Arg as substrate
{ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
Vmax=7.43 umol/min/mg enzyme with D-Met as substrate
{ECO:0000269|PubMed:17140416, ECO:0000269|PubMed:20564561};
Note=The values given here are for the recombinant protein.;
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14920}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17140416,
ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed exclusively in the intestine.
{ECO:0000269|PubMed:22393259}.
-!- DEVELOPMENTAL STAGE: Expression detected initially in the
gastrula-stage embryos and continuing throughout all developmental
stages to adulthood. {ECO:0000269|PubMed:22393259}.
-!- DISRUPTION PHENOTYPE: Mutant worms (tm3673) exhibit decreased egg-
laying capacity with smaller brood size and lower hatching rates
at 25 degrees Celsius. Worms do not show any change in physical
appearence. {ECO:0000269|PubMed:22393259}.
-!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000255}.
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EMBL; AB275890; BAF34313.1; -; mRNA.
EMBL; FO081818; CCD74112.1; -; Genomic_DNA.
RefSeq; NP_500234.3; NM_067833.5.
UniGene; Cel.20197; -.
ProteinModelPortal; Q95XG9; -.
SMR; Q95XG9; -.
STRING; 6239.Y69A2AR.5; -.
BindingDB; Q95XG9; -.
ChEMBL; CHEMBL3351208; -.
PaxDb; Q95XG9; -.
PeptideAtlas; Q95XG9; -.
EnsemblMetazoa; Y69A2AR.5; Y69A2AR.5; WBGene00022076.
GeneID; 3565775; -.
KEGG; cel:CELE_Y69A2AR.5; -.
UCSC; Y69A2AR.5; c. elegans.
CTD; 3565775; -.
WormBase; Y69A2AR.5; CE36371; WBGene00022076; daao-1.
eggNOG; KOG3923; Eukaryota.
eggNOG; COG0665; LUCA.
GeneTree; ENSGT00390000018635; -.
HOGENOM; HOG000046303; -.
InParanoid; Q95XG9; -.
KO; K00273; -.
OMA; PERGQNV; -.
OrthoDB; EOG091G0G0Y; -.
PhylomeDB; Q95XG9; -.
Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
SABIO-RK; Q95XG9; -.
PRO; PR:Q95XG9; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00022076; Expressed in 2 organ(s), highest expression level in adult organism.
GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
GO; GO:0003884; F:D-amino-acid oxidase activity; IDA:WormBase.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0046416; P:D-amino acid metabolic process; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0055114; P:oxidation-reduction process; IDA:WormBase.
InterPro; IPR006181; D-amino_acid_oxidase_CS.
InterPro; IPR023209; DAO.
InterPro; IPR006076; FAD-dep_OxRdtase.
PANTHER; PTHR11530; PTHR11530; 1.
Pfam; PF01266; DAO; 1.
PIRSF; PIRSF000189; D-aa_oxidase; 1.
PROSITE; PS00677; DAO; 1.
1: Evidence at protein level;
Complete proteome; Developmental protein; FAD; Flavoprotein;
Glycoprotein; Oxidoreductase; Peroxisome; Reference proteome; Signal.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 322 D-amino-acid oxidase.
/FTId=PRO_0000317125.
NP_BIND 4 18 FAD. {ECO:0000250}.
NP_BIND 34 35 FAD. {ECO:0000250}.
NP_BIND 41 42 FAD. {ECO:0000250}.
NP_BIND 46 48 FAD. {ECO:0000250}.
NP_BIND 293 297 FAD. {ECO:0000250}.
MOTIF 320 322 Microbody targeting signal.
{ECO:0000255}.
BINDING 160 160 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 177 177 FAD. {ECO:0000250}.
BINDING 215 215 Substrate. {ECO:0000250}.
BINDING 270 270 Substrate. {ECO:0000250}.
BINDING 294 294 Substrate; via carbonyl oxygen.
{ECO:0000250}.
BINDING 298 298 FAD. {ECO:0000250}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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