ID   DADA_YERPB              Reviewed;         434 AA.
AC   B2K3Q3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
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}; OrderedLocusNames=YPTS_2136;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL   Submitted (APR-2008) 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; CP001048; ACC89099.1; -; Genomic_DNA.
DR   RefSeq; WP_002211686.1; NZ_CP009780.1.
DR   AlphaFoldDB; B2K3Q3; -.
DR   SMR; B2K3Q3; -.
DR   GeneID; 66841493; -.
DR   KEGG; ypb:YPTS_2136; -.
DR   PATRIC; fig|502801.10.peg.1526; -.
DR   OMA; FWYKEDG; -.
DR   BioCyc; YPSE502801:YPTS_RS10825-MON; -.
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_1000138677"
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