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

 OXDA_CAEBR              Reviewed;         329 AA.
A8XJ44;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 1.
23-MAY-2018, entry version 71.
RecName: Full=D-amino-acid oxidase {ECO:0000312|WormBase:CBG13882a};
Short=DAAO {ECO:0000250|UniProtKB:Q95XG9};
Short=DAMOX {ECO:0000250|UniProtKB:Q95XG9};
Short=DAO {ECO:0000250|UniProtKB:Q95XG9};
EC=1.4.3.3 {ECO:0000250|UniProtKB:Q95XG9};
Flags: Precursor;
Name=daao-1 {ECO:0000312|WormBase:CBG13882a};
ORFNames=CBG13882 {ECO:0000312|WormBase:CBG13882a};
Caenorhabditis briggsae.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6238;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AF16;
PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A.,
D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E.,
Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R.,
Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P.,
Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M.,
Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M.,
Waterston R.H.;
"The genome sequence of Caenorhabditis briggsae: a platform for
comparative genomics.";
PLoS Biol. 1:166-192(2003).
[2] {ECO:0000305}
SEQUENCE REVISION.
STRAIN=AF16;
The C.briggsae Sequencing Consortium;
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000250|UniProtKB:Q95XG9}.
-!- CATALYTIC ACTIVITY: A D-amino acid + H(2)O + O(2) = a 2-oxo acid +
NH(3) + H(2)O(2). {ECO:0000250|UniProtKB:Q95XG9}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:Q95XG9};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14920}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q95XG9}.
-!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000255}.
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EMBL; HE601467; CAP32671.3; -; Genomic_DNA.
RefSeq; XP_002634783.1; XM_002634737.1.
ProteinModelPortal; A8XJ44; -.
SMR; A8XJ44; -.
STRING; 6238.CBG13882; -.
PRIDE; A8XJ44; -.
EnsemblMetazoa; CBG13882a; CBG13882a; WBGene00034568.
GeneID; 8576775; -.
KEGG; cbr:CBG13882; -.
CTD; 8576775; -.
WormBase; CBG13882a; CBP09519; WBGene00034568; Cbr-daao-1.
eggNOG; KOG3923; Eukaryota.
eggNOG; COG0665; LUCA.
HOGENOM; HOG000046303; -.
InParanoid; A8XJ44; -.
KO; K00273; -.
OMA; PERGQNV; -.
OrthoDB; EOG091G0G0Y; -.
Proteomes; UP000008549; Chromosome IV.
Proteomes; UP000008549; Unassembled WGS sequence.
GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
GO; GO:0003884; F:D-amino-acid oxidase activity; IBA:GO_Central.
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.
InterPro; IPR023209; DAO.
InterPro; IPR006076; FAD-dep_OxRdtase.
PANTHER; PTHR11530; PTHR11530; 1.
Pfam; PF01266; DAO; 1.
PIRSF; PIRSF000189; D-aa_oxidase; 1.
3: Inferred from homology;
Complete proteome; Developmental protein; FAD; Flavoprotein;
Glycoprotein; Oxidoreductase; Peroxisome; Reference proteome; Signal.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 329 D-amino-acid oxidase. {ECO:0000255}.
/FTId=PRO_0000317124.
NP_BIND 4 18 FAD. {ECO:0000250|UniProtKB:P14920}.
NP_BIND 34 35 FAD. {ECO:0000250}.
NP_BIND 41 42 FAD. {ECO:0000250}.
NP_BIND 46 48 FAD. {ECO:0000250}.
NP_BIND 298 302 FAD. {ECO:0000250}.
MOTIF 327 329 Microbody targeting signal.
{ECO:0000255}.
BINDING 162 162 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 182 182 FAD. {ECO:0000250}.
BINDING 220 220 Substrate. {ECO:0000250}.
BINDING 275 275 Substrate. {ECO:0000250}.
BINDING 299 299 Substrate; via carbonyl oxygen.
{ECO:0000250}.
BINDING 303 303 FAD. {ECO:0000250}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 180 180 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 329 AA; 36808 MW; 6D7B7F6CE3625886 CRC64;
MPRICVLGAG IMGVSTALAI QERIPDSVVT IIAEKFSPNT TSDVAAGLIE PYLCDDDVDR
VISWTKSTIQ RIQEYMNEGN PGAESQEQSG YWLQSVKSVP KWLEVMKNVK ILTGNELKMV
AKRPEHKFGI FYTTWYLEPT PYIKWESDKF LKNGGKIKNS KIQKIEDVEK EFGLFDVILN
CTGIGARHLI GDNEVFPTRG QILKVKCPSV KHFFIDDQFY ALLNDTTITL GGTADRHQWD
RTINPKISEK IFQENCKNIP SLRSAQVISS HVDLRPSRVT VRLEAEPDSK VIHNNGHGGS
GITLHWGCAL ECVELVKKVL AGKPGISKI


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