ID   DADA_ENT38              Reviewed;         432 AA.
AC   A4WBF2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Ent638_2363;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(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}.
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DR   EMBL; CP000653; ABP61032.1; -; Genomic_DNA.
DR   RefSeq; WP_012017746.1; NC_009436.1.
DR   AlphaFoldDB; A4WBF2; -.
DR   SMR; A4WBF2; -.
DR   STRING; 399742.Ent638_2363; -.
DR   PRIDE; A4WBF2; -.
DR   EnsemblBacteria; ABP61032; ABP61032; Ent638_2363.
DR   KEGG; ent:Ent638_2363; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; FWYKEDG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000000230; 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_1000066093"
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;  47363 MW;  A2499274FEC70BC6 CRC64;
     MRVVVLGSGV VGVTSAWYLC QAGHEVTVID REPGSALETS AANAGQISPG YAAPWAAPGV
     PLKAIKWMFQ RHAPLAISLD GTPSQLKWMW QMLRNCDTRH YMENKGRMVR LAEYSRDCLK
     TLRASTGIEY EGRQGGTLQL FRTAQQYENA TRDIAVLEDA GVPYQLLDAS QLAQVEPALA
     EVAHKLTGGL RLPNDETGDC QLFTQRLAKM CEQAGVTFRY NTPVDKLLSE GGKIYGVKCG
     DEVIKADSYV MAFGSYSTAM LKGLLDIPVY PLKGYSLTIP VKEDNGAPVS TILDETYKIA
     ITRFDNRIRV GGMAEIVGFN TELLQPRRET LEMVVRDLFP RGGFIEQATF WTGLRPMTPD
     GTPIVGRTPF KNLWTNTGHG TLGWTMACGS GQLLSDLISG RTPAIPFDDL SAARYQSGFS
     PSRPQHLHGA HN