ID   DADA_PARP8              Reviewed;         428 AA.
AC   B2JF25;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Bphy_0765;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC69954.1; -; Genomic_DNA.
DR   RefSeq; WP_012400174.1; NZ_CADFGH010000007.1.
DR   AlphaFoldDB; B2JF25; -.
DR   SMR; B2JF25; -.
DR   STRING; 391038.Bphy_0765; -.
DR   EnsemblBacteria; ACC69954; ACC69954; Bphy_0765.
DR   KEGG; bph:Bphy_0765; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_4; -.
DR   OMA; NDLYPRG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001192; 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..428
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138645"
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;  46107 MW;  5699B6C501B030DB CRC64;
     MRVVVLGSGV VGVTSAYYLA RAGHEVTVID REAGPALETS FANAGQISPG YAAPWAAPGV
     PLKAVKWMFQ KHAPLAIRLD GTQFQLQWMW QMLQNCTSAR YAVNKGRMVR LAEYSRDCLQ
     ALRAETGIQY EGRTGGTLQL FRTQQQLDGA AKDIAVLEEA NVPYELLMPA DLARAEPALA
     ATSHKLTGGL RLPGDETGDC QLFTTRLAAL AEQLGVKFRY NTPIDALAME GGRIAGVKCG
     NEMVRADNFV VALGSYSTQF LSGLVKIPVY PLKGYSITAP IVDAKSAPVS TVLDETYKIA
     ITRFDDRIRV GGMAEIVGFD KKLKQARRET LEMCVNDLFP GGGDTSKATF WTGLRPMTPD
     GTPIVGRTPV SNLFLNTGHG TLGWTMSCGS GQLLADLISG KRPAIQSGDL SVHRYLGETA
     GQTRPAYA