ID   DADA_BRUAB              Reviewed;         416 AA.
AC   Q579E2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
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=BruAb2_0309;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; Evidence={ECO:0000255|HAMAP-
CC         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; AE017224; AAX75742.1; -; Genomic_DNA.
DR   RefSeq; WP_002965723.1; NC_006933.1.
DR   AlphaFoldDB; Q579E2; -.
DR   SMR; Q579E2; -.
DR   EnsemblBacteria; AAX75742; AAX75742; BruAb2_0309.
DR   GeneID; 45126234; -.
DR   KEGG; bmb:BruAb2_0309; -.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000000540; Chromosome II.
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; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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   PANTHER; PTHR13847:SF280; D-AMINO ACID DEHYDROGENASE; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..416
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000066070"
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
//