ID   DADA_XANCP              Reviewed;         429 AA.
AC   Q8P4Q9;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=XCC3648;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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   -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01202}.
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DR   EMBL; AE008922; AAM42918.1; -; Genomic_DNA.
DR   RefSeq; NP_638994.1; NC_003902.1.
DR   RefSeq; WP_011038731.1; NC_003902.1.
DR   AlphaFoldDB; Q8P4Q9; -.
DR   SMR; Q8P4Q9; -.
DR   STRING; 340.xcc-b100_3834; -.
DR   EnsemblBacteria; AAM42918; AAM42918; XCC3648.
DR   KEGG; xcc:XCC3648; -.
DR   PATRIC; fig|190485.4.peg.3907; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; NDLYPRG; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0055130; P:D-alanine catabolic process; IBA:GO_Central.
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..429
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_0000166156"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   429 AA;  46660 MW;  82DEDFF9521FC3F8 CRC64;
     MRVLILGSGV IGTTTAWYLA QSGCEVTVVD RQPASGLETS YANAGQLSFG YTSPWAAPGV
     PGKAVKWLFE QHAPLSIRPT RDLRQLAWLS QMLRNCTAER YAVNKARMVR LSDYSRDCLN
     ALRASTGLEF EGRQLGTTQL FRTQQQLDAA AQDIEVLAQY GVPYELLSPA QIAQYEPGLA
     GGGAQMAGAL HLPEDQTGDC RLFTQRLADL ATQAGVQFRY GQQIERLEHA GGEITGVQID
     GRLVTADRYV LALGSYSADL LLSLGLHLPV YPLKGYSLTI PIVDAQRAPT STVLDESYKI
     ALTRFDERIR VGGMAEVAGF DLSLNPRRRA TLEMVVNDLF PGAGDLAQAE FWTGLRPATP
     DGTPVVGATP YANLFLNTGH GTLGWTMACG SGRYLADLMQ GRTPEIDTEG LDVFRYLSTR
     STRPHREAA