ID   DADA_BURM7              Reviewed;         428 AA.
AC   A3MHR1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=BMA10247_0222;
OS   Burkholderia mallei (strain NCTC 10247).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10247;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000548; ABO05709.1; -; Genomic_DNA.
DR   RefSeq; WP_004189387.1; NZ_CP007802.1.
DR   AlphaFoldDB; A3MHR1; -.
DR   SMR; A3MHR1; -.
DR   GeneID; 56596462; -.
DR   KEGG; bmaz:BM44_2770; -.
DR   KEGG; bmn:BMA10247_0222; -.
DR   PATRIC; fig|320389.8.peg.3128; -.
DR   OMA; NDLYPRG; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000002284; Chromosome I.
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..428
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000066075"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   428 AA;  46175 MW;  0AC24145CC22B8EE CRC64;
     MRVVILGSGV VGVASAYYLA RAGHEVTVID REAGPALDTS FANAGQISPG YAAPWAAPGV
     PLKAVKWMFE KHAPLAIRLD GTRFQLQWMW QMLRNCTTER YALNKGRMVR LAEYSRDCLQ
     ALRAETAIQY EGRTGGTLQV FRTQQQLDGA AKDIAVLREA NVPFELLSSD ELKKAEPALA
     AVSHKLTGGL RLPGDETGDC QLFTTRLAAL AEQLGVKFRF NTRIDALAVA GGKIAGVQCG
     GEMVRADAYV VALGSYSTNL VASLVKIPVY PLKGYSITAP IVDAAKAPVS TVLDETYKIA
     ITRFDDRIRV GGMAEIVGFD KRLRDARRGT LEMCVNDLFP GGGDTAKATF WTGLRPMTPD
     GTPIVGRTPV PNLFLNTGHG TLGWTMSCGS GQLLADLMSG KKPAIRADDL SVHRYLSETD
     GEHRPAYA