ID   DADA_GRABC              Reviewed;         418 AA.
AC   Q0BUV2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=GbCGDNIH1_0502;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI61400.1; -; Genomic_DNA.
DR   RefSeq; WP_011631210.1; NC_008343.2.
DR   AlphaFoldDB; Q0BUV2; -.
DR   SMR; Q0BUV2; -.
DR   STRING; 391165.GbCGDNIH1_0502; -.
DR   EnsemblBacteria; ABI61400; ABI61400; GbCGDNIH1_0502.
DR   KEGG; gbe:GbCGDNIH1_0502; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; FWYKEDG; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001963; 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..418
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000066096"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   418 AA;  45968 MW;  3CD0EAA45807C3A2 CRC64;
     MRVLILGSGV VGVATAYYLS REGHEVVVAD RRDGPGMETS FANAGQVSPG YSSPWAAPGI
     PLKVLRWMTQ PRSPFVLRPK LDWAQWRWMT QMLGNCTANA YARNKARMVR LAEYSRDQLR
     DLRDETGIAY DNRERGTLQL FRTQKQMDHT ADDIAVLKSY GVAYEVLDRA GCIAAEPGLQ
     WAQVPLVGGL RLPGDETGDA HLFTRELARI CMERGVSFLF GTQIHGFSTQ GDKITAIRSS
     RGDLMADAYV CALGSYSPLL LKQIGIAAPI YPVKGYSMTI PITDETHAPV STVMDETYKI
     AITRLGNRIR VGGTAELAGY DTRLRQERRM TLEGSVKELF PDSGDLPAAT FWSGLRPMTP
     DGTPIIGPTR YRNLHLNTGH GTLGWTMSCG SGRLLADMIS GKRPNIDHAD LAIARYAG