ID   DADA_EDWI9              Reviewed;         417 AA.
AC   C5B9W5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=NT01EI_1632;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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; CP001600; ACR68816.1; -; Genomic_DNA.
DR   RefSeq; WP_015870972.1; NC_012779.2.
DR   AlphaFoldDB; C5B9W5; -.
DR   SMR; C5B9W5; -.
DR   STRING; 67780.B6E78_01350; -.
DR   EnsemblBacteria; ACR68816; ACR68816; NT01EI_1632.
DR   GeneID; 7961960; -.
DR   KEGG; eic:NT01EI_1632; -.
DR   PATRIC; fig|634503.3.peg.1463; -.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; FWYKEDG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001485; 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; Reference proteome.
FT   CHAIN           1..417
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000213847"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   417 AA;  45367 MW;  BE0AF9800E22D68D CRC64;
     MRVVILGSGV IGVTSAWYLA QAGHQVTVVD RQEGPGLETS AANAGQISPG YAAPWAAPGI
     PLKALKWLFQ RHAPLAMSLD GSLFQLRWLW QMLRNCDSTH YAQNKARMVR LAEYSRDCLA
     QLRRTTTIDY EGRQLGTLQL FRTPQQYENA ARDIAVLREA GVPYRLLPTA QLSTVEPALA
     VAGVRLSGGL HLPHDETGDC QLFTRHLAQQ AAQSGVHFIF STQVLRLLRS GARIQGVQCG
     HDTLVADAYV VALGAYSTGL LQDIVAIPVY PLKGYSLTLP IDDPDAAPRS TVLDESYKVA
     ITRFDRRIRV GGMAEVVGFD MSLPLARRRT LERVVRDLYP RGGLLPQASF WSGLRPATPD
     GTPLVGATPL ENLYLNTGHG TLGWTMACGS GQLLADIISG VTPTIRVDDL SVSRYTA