OXDA_CAEBR
ID OXDA_CAEBR Reviewed; 329 AA.
AC A8XJ44;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=D-amino-acid oxidase {ECO:0000312|WormBase:CBG13882a};
DE Short=DAAO {ECO:0000250|UniProtKB:Q95XG9};
DE Short=DAMOX {ECO:0000250|UniProtKB:Q95XG9};
DE Short=DAO {ECO:0000250|UniProtKB:Q95XG9};
DE EC=1.4.3.3 {ECO:0000250|UniProtKB:Q95XG9};
DE Flags: Precursor;
GN Name=daao-1 {ECO:0000312|WormBase:CBG13882a};
GN ORFNames=CBG13882 {ECO:0000312|WormBase:CBG13882a};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
RN [2] {ECO:0000305}
RP SEQUENCE REVISION.
RC STRAIN=AF16;
RG The C.briggsae Sequencing Consortium;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q95XG9}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q95XG9};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q95XG9};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14920}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q95XG9}.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000255}.
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DR EMBL; HE601467; CAP32671.3; -; Genomic_DNA.
DR RefSeq; XP_002634783.1; XM_002634737.1.
DR AlphaFoldDB; A8XJ44; -.
DR SMR; A8XJ44; -.
DR STRING; 6238.CBG13882; -.
DR PRIDE; A8XJ44; -.
DR EnsemblMetazoa; CBG13882a.1; CBG13882a.1; WBGene00034568.
DR GeneID; 8576775; -.
DR KEGG; cbr:CBG_13882; -.
DR CTD; 8576775; -.
DR WormBase; CBG13882a; CBP09519; WBGene00034568; Cbr-daao-1.
DR eggNOG; KOG3923; Eukaryota.
DR HOGENOM; CLU_034311_0_2_1; -.
DR InParanoid; A8XJ44; -.
DR OMA; DEKCYPT; -.
DR OrthoDB; 1363414at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
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; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0019478; P:D-amino acid catabolic process; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Developmental protein; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Peroxisome; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..329
FT /note="D-amino-acid oxidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000317124"
FT MOTIF 327..329
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|UniProtKB:P14920"
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 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 298..302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 303
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 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ 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
