ID   DADA_YERPG              Reviewed;         434 AA.
AC   A9R9D3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=YpAngola_A2361;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000901; ABX85105.1; -; Genomic_DNA.
DR   RefSeq; WP_002211686.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R9D3; -.
DR   SMR; A9R9D3; -.
DR   GeneID; 66841493; -.
DR   KEGG; ypg:YpAngola_A2361; -.
DR   PATRIC; fig|349746.12.peg.3374; -.
DR   OMA; FWYKEDG; -.
DR   UniPathway; UPA00043; UER00498.
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..434
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138678"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   434 AA;  47204 MW;  75737D0371EC3345 CRC64;
     MRVVILGSGV VGVTSAWYLA KEGHDVTVID RQDGPAQETS AGNAGQISPG YAAPWAAPGV
     PLKAIKWMFQ RHAPLAIRLD GSSLQLRWMW QMLRNCDTSH YMVNKSRMVR LAEYSRDCLK
     DLRAATGIQY EGRQGGTLQL FRTEQQFDNA AKDIAVLDDA GVPYSLLTAE QLATVEPALA
     KVAHKLTGGL RLPNDETGDC KLFTERLAKM AEQAGVKFIF NRSVDKLLVE GDQIAGVLCG
     DDIIKADAYV VAFGAYSTAL LAGLVSIPVY PLKGYSLTIP ITDPASAPFS TVLDETYKIA
     ITRFDDRIRV GGMAEIVGFN TQLAPARRET LEMVVRDLYP HGGDISQAVF WSGLRPMTPD
     GTPIVGRTPL KNLYLNTGHG TLGWTMACGS GQLLADIIQG RRPAIVADDL SVARYRAGFQ
     PLNIAPLHDI HPIR