ID   DADA_KLEP3              Reviewed;         432 AA.
AC   B5XQ81;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=KPK_1985;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(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; CP000964; ACI11038.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XQ81; -.
DR   SMR; B5XQ81; -.
DR   EnsemblBacteria; ACI11038; ACI11038; KPK_1985.
DR   KEGG; kpe:KPK_1985; -.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; NDLYPRG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001734; 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..432
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138656"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   432 AA;  47206 MW;  B435F1BF156C218C CRC64;
     MRVVILGSGV VGVASAWYLS QAGHEVTVID RQPGPAEETS AANAGQISPG YAAPWAAPGV
     PLKAIKWMFQ RHAPLAIGLD GTSFQLKWMW QMLRNCDTRH YMENKGRMVR LAEYSRDCLK
     ALRDTTGIQY EGRQGGTLQL FRTAKQYENA TRDIAVLEDA GVPYQLLEAK RLAEVEPALA
     EVSHKLTGGL RLPNDETGDC QLFTTRLAAM AEQAGVTFRF NTAVDALLQE GDRIAGVKCG
     DEIIKGDAYV MAFGSYSTAM LKGLVDIPVY PLKGYSLTIP IAQEDGAPVS TILDETYKIA
     ITRFDQRIRV GGMAEIVGFN KALLQPRRET LEMVVRDLFP RGGHVEQATF WTGLRPMTPD
     GTPVVGRTAY KNLWLNTGHG TLGWTMACGS GQLISDLISG RTPAIPYDDL AVARYSPGFT
     PARPQHLHGA HN