ID   DADA_BRUA1              Reviewed;         416 AA.
AC   B2SDA2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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};
GN   OrderedLocusNames=BAbS19_II02950;
OS   Brucella abortus (strain S19).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=430066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S19;
RX   PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA   Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA   Bricker B., Yu G., Du L., Sobral B.W.;
RT   "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT   virulent strains yields candidate virulence genes.";
RL   PLoS ONE 3:E2193-E2193(2008).
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   -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC       pyruvate from D-alanine: step 1/1.
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01202}.
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DR   EMBL; CP000888; ACD73806.1; -; Genomic_DNA.
DR   RefSeq; WP_002965723.1; NC_010740.1.
DR   AlphaFoldDB; B2SDA2; -.
DR   SMR; B2SDA2; -.
DR   EnsemblBacteria; ACD73806; ACD73806; BAbS19_II02950.
DR   GeneID; 45126234; -.
DR   KEGG; bmc:BAbS19_II02950; -.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; NDLYPRG; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000002565; Chromosome 2.
DR   GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0055130; P:D-alanine catabolic process; IEA:UniProtKB-UniPathway.
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_1000138640"
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