ID   DADA_PARPJ              Reviewed;         428 AA.
AC   B2T612;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Bphyt_2982;
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX   PubMed=21551308; DOI=10.1128/jb.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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; CP001052; ACD17376.1; -; Genomic_DNA.
DR   RefSeq; WP_012433955.1; NC_010681.1.
DR   AlphaFoldDB; B2T612; -.
DR   SMR; B2T612; -.
DR   STRING; 398527.Bphyt_2982; -.
DR   EnsemblBacteria; ACD17376; ACD17376; Bphyt_2982.
DR   KEGG; bpy:Bphyt_2982; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_4; -.
DR   OMA; NDLYPRG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001739; 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.
FT   CHAIN           1..428
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138646"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   428 AA;  46075 MW;  F1A427A232E8BE00 CRC64;
     MRVVVLGSGV VGVTSAYYLA RAGHEVTVID REAGPALETS FANAGQISPG YASPWAAPGV
     PLKAVKWMFQ KHAPLAIRLD GTQFQLQWMW QMLQNCTSSR YAVNKGRMVR LAEYSRDCLQ
     ALRAETGIQY EGRTGGTLQV FRTQQQFDGA AKDIAVLQEA NVPYELLSPA ELARAEPALA
     AVSHKLTGGL RLPGDETGDC QMFTTRLAAL AEELGVKFRY NTPIDALAMA GDRIAGVKCG
     EELVRADSFV VALGSYSTQF LSGLVKIPVY PLKGYSITAP IVNEASAPVS TVLDETYKIA
     ITRFDDRIRV GGMAEIVGFD KSLRQARRET LELCVNDLFP GGGDTSKATF WTGLRPMTPD
     GTPIVGRTPV PNLFLNTGHG TLGWTMSCGS GQLLADVMSG KQPAIKADDL SVHRYLGEVG
     GAHRPAYA