ID   DADA_PARXL              Reviewed;         429 AA.
AC   Q13VE3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Bxeno_A3408;
GN   ORFNames=Bxe_A1001;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE31946.1; -; Genomic_DNA.
DR   RefSeq; WP_011489462.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q13VE3; -.
DR   SMR; Q13VE3; -.
DR   STRING; 266265.Bxe_A1001; -.
DR   EnsemblBacteria; ABE31946; ABE31946; Bxe_A1001.
DR   KEGG; bxb:DR64_3162; -.
DR   KEGG; bxe:Bxe_A1001; -.
DR   PATRIC; fig|266265.5.peg.3579; -.
DR   eggNOG; COG0665; Bacteria.
DR   OMA; NDLYPRG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001817; Chromosome 1.
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..429
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000066086"
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;  46194 MW;  CDB9833D372207EB CRC64;
     MRVVVLGSGV VGVTSAYYLA RAGHEVTVID REAGPALETS FANAGQISPG YASPWAAPGV
     PLKAVKWMFQ KHAPLAIRLD GTQFQLQWMW QMLQNCTSSR YAVNKGRMVR LAEYSRDCLQ
     ALRAETGIQY EGRTGGTLQV FRTQQQFEGA AKDIAVLREA SVPYELLSPA ELAQAEPALA
     AVSHKLTGGL RLPGDETGDC QMFTTRLAAL AEQLGVKFRY NTPIDALAMA GDRIAGVKCG
     EELVRADSFV VALGSYSTQF LSGLVKIPVY PLKGYSITAP IVNEASAPVS TVLDETYKIA
     ITRFDDRIRV GGMAEIVGFD KSLREARRET LELCVNDLFP GGGDTSKATF WSGLRPMTPD
     GTPIVGRTPV ANLFLNTGHG TLGWTMSCGS GQLLADVMSG KQPAIKADDL SVHRYLGETR
     GAHRPAYAA