ID   DADA_KLEAE              Reviewed;         432 AA.
AC   O30745;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=D-amino acid dehydrogenase;
DE            EC=1.4.99.-;
DE   AltName: Full=D-alanine dehydrogenase;
GN   Name=dadA;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=W70;
RX   PubMed=9457858; DOI=10.1128/jb.180.3.563-570.1998;
RA   Janes B.K., Bender R.A.;
RT   "Alanine catabolism in Klebsiella aerogenes: molecular characterization of
RT   the dadAB operon and its regulation by the nitrogen assimilation control
RT   protein.";
RL   J. Bacteriol. 180:563-570(1998).
CC   -!- FUNCTION: Catalyzes the oxidative deamination of D-amino acids.
CC       Participates in the utilization of alanine as the sole source of carbon
CC       and nitrogen for growth. {ECO:0000269|PubMed:9457858}.
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;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC       pyruvate from D-alanine: step 1/1.
CC   -!- INDUCTION: By alanine; slightly repressed by glucose. Is activated by
CC       the Ntr system, mediated by the nitrogen assimilation control protein
CC       (NAC). {ECO:0000269|PubMed:9457858}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to use alanine as a
CC       carbon or nitrogen source and become sensitive to the presence of the
CC       amino acid in glucose-ammonium minimal medium. They exhibit a glutamate
CC       auxotrophy when ammonium is the sole source of nitrogen.
CC       {ECO:0000269|PubMed:9457858}.
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AF016253; AAC38139.1; -; Genomic_DNA.
DR   AlphaFoldDB; O30745; -.
DR   SMR; O30745; -.
DR   STRING; 548.EAG7_01002; -.
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   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..432
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_0000166134"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   432 AA;  47251 MW;  096986F47BDB4DD6 CRC64;
     MRVVILGSGV FGVASAWYLS QAGHDVTVID RQPGPAEETS AANAGQISPG YAAPWAAPGV
     PLKAIKWMFQ RHAPLAIGLD GTSFQLKWMW QMLRNCDTRH YMENKGRMVR LAEYSRDCLK
     ALRDTTGIQY EGRQGGTLQL FRTAKQYENA TRDIAVLEDA GVPYQLLEAK RLAEVEPALA
     EVSHKLTGGL RLPNDETGDC QLFTTRLAAM ADQAGVTFRF NTAVDALLHE GDRIAGVKCG
     MRIIKGDAYV MAFGSYSTAM LKGLVDIPVY PLKGYSLTIP IAQEDGAPVS TILDVTYTIA
     ITRFDQRIRV GGMAEIVGFN KTLLQPRRET LEMVVRDLFP RGGHVEQATF WTGLRPMTPD
     GTPVVGRTAY KNLWLNTGHG TLGWTMACGS GQLISDLISG RTPAIPYDDL AVARYSPGFT
     PARPQHLHGA HN