ID   DADA_BRUME              Reviewed;         416 AA.
AC   Q8YD04;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=D-amino acid dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01202};
DE            EC=1.4.99.- {ECO:0000255|HAMAP-Rule:MF_01202};
GN   Name=dadA {ECO:0000255|HAMAP-Rule:MF_01202}; OrderedLocusNames=BMEII0373;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC   -!- FUNCTION: Oxidative deamination of D-amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01202}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + a D-alpha-amino acid + H2O = a 2-oxocarboxylate + AH2 +
CC         NH4(+); Xref=Rhea:RHEA:18125, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:59871; Evidence={ECO:0000255|HAMAP-Rule:MF_01202};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01202};
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01202}.
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DR   EMBL; AE008918; AAL53615.1; -; Genomic_DNA.
DR   PIR; AD3556; AD3556.
DR   RefSeq; WP_002965723.1; NZ_GG703779.1.
DR   AlphaFoldDB; Q8YD04; -.
DR   SMR; Q8YD04; -.
DR   STRING; 224914.BMEII0373; -.
DR   EnsemblBacteria; AAL53615; AAL53615; BMEII0373.
DR   GeneID; 45126234; -.
DR   KEGG; bme:BMEII0373; -.
DR   PATRIC; fig|224914.52.peg.3003; -.
DR   eggNOG; COG0665; Bacteria.
DR   OMA; NDLYPRG; -.
DR   PhylomeDB; Q8YD04; -.
DR   Proteomes; UP000000419; Chromosome II.
DR   GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_01202; DadA; 1.
DR   InterPro; IPR023080; DadA.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..416
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_0000166128"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   416 AA;  45110 MW;  7480382FF5614CA2 CRC64;
     MQITILGSGV IGVTTAYYLA KLGHEVTVID REEGPALETS FANAGQVSPG YASPWAAPGI
     PLKAAKWLFQ KHAPLILRLT TDPVQYRWLL QMLANCTDSR YKINKTRMVR VAEYSRDCLI
     ELRKDTGIEY DQRSQGTLQL FREQYQLDGI GKDIEVLRQD GVPFEVLDRD GCVNVEPALA
     HAKDKFVGGL RLPNDETGDC FKFTNALAKI AEGLGVKFRF GVNIKSLLMS GGKISGVETS
     EGIVTAERYV VALGSYTPAL IKALGLNAPI YPVKGYSITA PIVDESRAPV STVLDESYKI
     AITRLGDRIR VGGMAEVSGF TDDLPAARRA TLDLSVTDLF PGGDLKAATF WSGLRPMTPD
     STPIIGGTRY DNLFINAGHG TLGWTMACGS GRLLADLISG NKADIRADDL GIARYN