ID   DADA_XYLF2              Reviewed;         435 AA.
AC   B2I8Y3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=XfasM23_1924;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
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; CP001011; ACB93324.1; -; Genomic_DNA.
DR   RefSeq; WP_004088180.1; NC_010577.1.
DR   AlphaFoldDB; B2I8Y3; -.
DR   SMR; B2I8Y3; -.
DR   EnsemblBacteria; ACB93324; ACB93324; XfasM23_1924.
DR   GeneID; 58017344; -.
DR   KEGG; xfn:XfasM23_1924; -.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; FWYKEDG; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001698; 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..435
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138675"
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;  47540 MW;  F30FC0AD17106A5E CRC64;
     MRVLILGSGV IGTTSAWYLS KAGCEVVVVD RQSGAGLETS YANGGQLSFG YTSPWAAPGV
     PLKAVRWLFE RHAPLSIRPT TDWNQYVWLA RMLRHCSAER YAVNKSRMLR LSEYSREALE
     ALSAETGITF EGRRLGTIQL FRTQQQLDGA VRDIELLTQY GIPYEVLSPH QLAKFEPGLA
     DGSVRFVGAL RLPHDQTGDC CLFTQRLAAL AAKRGVEFRY GCTVQRLEVD GPRVTGAWIN
     GALERADCCV VALGSYSPLL LAPLGLRLPV YPLKGFSLTL PMIDASRAPV STVLDESYKV
     AVTRFDERIR VAGMAEVSGY DVSLNPRRRS TLEMVVQDVY PGCGDLGRGE FWTGLRPATP
     DGTPVIGATP YQGLFLNTGH GTLGWTMSSG SGRYLADLIC CRPCEISSEG LDMFRYLVST
     IPCPQECAPC VPPTP