ID   DAO_MYCTO               Reviewed;         320 AA.
AC   P9WP26; L0T817; O07727; Q7D7T4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Probable D-amino-acid oxidase;
DE            Short=DAAO;
DE            Short=DAMOX;
DE            Short=DAO;
DE            EC=1.4.3.3;
GN   Name=aao; OrderedLocusNames=MT1956;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46227.1; -; Genomic_DNA.
DR   PIR; F70518; F70518.
DR   RefSeq; WP_003899072.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP26; -.
DR   SMR; P9WP26; -.
DR   EnsemblBacteria; AAK46227; AAK46227; MT1956.
DR   KEGG; mtc:MT1956; -.
DR   PATRIC; fig|83331.31.peg.2105; -.
DR   HOGENOM; CLU_034311_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
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; 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   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..320
FT                   /note="Probable D-amino-acid oxidase"
FT                   /id="PRO_0000427025"
FT   BINDING         8..22
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         159
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         299..304
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  34108 MW;  906914A84ACC3993 CRC64;
     MAIGEQQVIV IGAGVSGLTS AICLAEAGWP VRVWAAALPQ QTTSAVAGAV WGPRPKEPVA
     KVRGWIEQSL HVFRDLAKDP ATGVRMTPAL SVGDRIETGA MPPGLELIPD VRPADPADVP
     GGFRAGFHAT LPMIDMPQYL DCLTQRLAAT GCEIETRPLR SLAEAAEAAP IVINCAGLGA
     RELAGDATVW PRFGQHVVLT NPGLEQLFIE RTGGSEWICY FAHPQRVVCG GISIPGRWDP
     TPEPEITERI LQRCRRIQPR LAEAAVIETI TGLRPDRPSV RVEAEPIGRA LCIHNYGHGG
     DGVTLSWGCA REVVNLVGGG