ID   DADA_XYLFM              Reviewed;         435 AA.
AC   B0U4V3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, 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};
GN   OrderedLocusNames=Xfasm12_2000;
OS   Xylella fastidiosa (strain M12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(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; CP000941; ACA12870.1; -; Genomic_DNA.
DR   RefSeq; WP_012338080.1; NC_010513.1.
DR   AlphaFoldDB; B0U4V3; -.
DR   SMR; B0U4V3; -.
DR   KEGG; xfm:Xfasm12_2000; -.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; FWYKEDG; -.
DR   OrthoDB; 573710at2; -.
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..435
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138676"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   435 AA;  47625 MW;  46A02AFD6EA71DAC CRC64;
     MRVLILGSGV IGTTSAWYLS KAGCEVVVVD RQSGAGLETS YANGGQLSFG YTSPWAAPGV
     PLKAVRWLFE RHAPLSIRPT TDWNQYVWLA RMLRHCSAER YAVNKSRMLR LSEYSREALE
     ALSAETGITF EGRRLGTIQL FRTQQQLDAA VRDIELLTQY GIPYEVLSPH QLAKFEPGLV
     DGSVRFAGAL RLPHDQTGDC YLFTQRLAAL AAKRGVEFRY GCKVQRLEVD GPRVTGAWIN
     GALERADCCV VALGSYSPLL LAPLGLRLPV YPLKGFSLTL PMIDASRAPV STVLDESYKV
     AVTRFDERIR VAGMAEVSGY DVSLNPRRRA TLEMVVQDVY PGCGDLGRGE FWTGLRPATP
     DGTPVIGATP YQGLFLNTGH GTLGWTMSSG SGRYLADLIC CRPCEISSEG LDMFRYLVST
     IPCPQECAPC VPPTP