OXDA_TRIVR
ID OXDA_TRIVR Reviewed; 356 AA.
AC Q99042;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=D-amino-acid oxidase;
DE Short=DAAO;
DE Short=DAMOX;
DE Short=DAO;
DE EC=1.4.3.3;
GN Name=DAO1;
OS Trigonopsis variabilis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trigonopsidaceae; Trigonopsis.
OX NCBI_TaxID=34364;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CBS 4095;
RX PubMed=9434346;
RX DOI=10.1002/(sici)1097-0061(199712)13:15<1399::aid-yea187>3.0.co;2-7;
RA Gonzalez F.J., Montes J., Martin F., Lopez M.C., Ferminan E., Catalan J.,
RA Galan M.A., Dominguez A.;
RT "Molecular cloning of TvDAO1, a gene encoding a D-amino acid oxidase from
RT Trigonopsis variabilis and its expression in Saccharomyces cerevisiae and
RT Kluyveromyces lactis.";
RL Yeast 13:1399-1408(1997).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR EMBL; Z50019; CAA90322.1; -; Genomic_DNA.
DR PIR; S39437; S39437.
DR AlphaFoldDB; Q99042; -.
DR SMR; Q99042; -.
DR PRIDE; Q99042; -.
DR BRENDA; 1.4.3.3; 6488.
DR SABIO-RK; Q99042; -.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
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 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..356
FT /note="D-amino-acid oxidase"
FT /id="PRO_0000162768"
FT BINDING 4..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 32..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 43..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 48..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 329..333
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 39301 MW; A2935E9DB71A49FC CRC64;
MAKIVVIGAG VAGLTTALQL LRKGHEVTIV SEFTPGDLSI GYTSPWAGAN WLTFYDGGKL
ADYDAVSYPI LRELARSSPE AGIRLISQRS HVLKRDLPKL EVAMSAICQR NPWFKNTVDS
FEIIEDRSRI VHDDVAYLVE FRSVCIHTGV YLNWLMSQCL SLGATVVKRR VNHIKDANLL
HSSGSRPDVI VNCSGLFARF LGGVEDKKMY PIRGQVVLVR NSLPFMASFS STPEKENEDE
ALYIMTRFDG TSIIGGCFQP NNWSSEPDPS LTHRILSRAL DRFPELTKDG PLDIVRECVG
HRPGREGGPR VELEKIPGVG FVVHNYGAAG AGYQSSYGMA DEAVSYVERA LTRPNL