ID   DADA_XANCB              Reviewed;         429 AA.
AC   B0RWG2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=xcc-b100_3834;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(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; AM920689; CAP53201.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RWG2; -.
DR   SMR; B0RWG2; -.
DR   KEGG; xca:xcc-b100_3834; -.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; NDLYPRG; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001188; Chromosome.
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..429
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138673"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   429 AA;  46718 MW;  85081FFB91026E4F CRC64;
     MRVLILGSGV IGTTTAWYLA QSGCEVTVVD RQPASGLETS YANAGQLSFG YTSPWAAPGV
     PGKAVKWLFE QHAPLSIRPT RDLRQLAWLS QMLRNCTAER YAVNKARMVR LSDYSRDCLN
     ELRASTGLEF EGRQLGTTQL FRTQQQLDAA AQDIEVLAQY GVPYELLSPA QIAQYEPGLA
     GGGAQMAGAL HLPEDQTGDC RLFTQRLADL ATQAGVQFRY GQQIERLEHA GGEITGVQID
     GRLVTADRYV LALGSYSADL LLSLGLHLPV YPLKGYSLTI PIVDAQRAPT STVLDESYKI
     ALTRFDERIR VGGMAEVAGF DLSLNPRRRA TLEMVVNDLF PGAGDLAQAE FWTGLRPATP
     DGTPVVGATP YANLFLNTGH GTLGWTMACG SGRYLADLMQ GRTPEIDTEG LDVFRYLSTR
     STRPHREAA