ID   DADA_BURVG              Reviewed;         428 AA.
AC   A4JCJ3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Bcep1808_0985;
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS   (strain R1808)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000614; ABO53996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4JCJ3; -.
DR   SMR; A4JCJ3; -.
DR   STRING; 269482.Bcep1808_0985; -.
DR   EnsemblBacteria; ABO53996; ABO53996; Bcep1808_0985.
DR   KEGG; bvi:Bcep1808_0985; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_4; -.
DR   OMA; NDLYPRG; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000002287; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..428
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000066085"
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;  46070 MW;  8FDCB6E1EEC743B7 CRC64;
     MRVVILGSGV VGVASAYYLA RAGHEVTVID REAGPALDTS FANAGQISPG YAAPWAAPGV
     PLKAVKWMFE KHAPLAIRLD GTRFQLQWMW QMLRNCTPER YAVNKGRMVR LAEYSRDCLQ
     ALRADTGIEY EGRTGGTLQL FRSQQQLDGA AKDIAVLREA NVPFELLSPA ELKNAEPALA
     AVSHKLTGGL RLPGDETGDC QLFTTRLAAL AESLGVKFRY NTPIDALAIA GGKIAGVQCG
     SETVRADAYV VALGSYSTNF VSKLMKIPVY PLKGYSITAP IVNEAAAPVS TVLDETYKIA
     ITRFDQRIRV GGMAEIVGFD KKLRAARRET LEMCVNDLFP GGGDTSKATF WTGLRPMTPD
     GTPIVGRTPV SNLFMNTGHG TLGWTMSCGS GQLLADLISG KKPAIQADDL SVHRYLNEVA
     GQTRPAYA