ID   DADA_METNO              Reviewed;         421 AA.
AC   B8IJ86;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Mnod_1094;
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001349; ACL56101.1; -; Genomic_DNA.
DR   RefSeq; WP_015927799.1; NC_011894.1.
DR   AlphaFoldDB; B8IJ86; -.
DR   SMR; B8IJ86; -.
DR   STRING; 460265.Mnod_1094; -.
DR   EnsemblBacteria; ACL56101; ACL56101; Mnod_1094.
DR   KEGG; mno:Mnod_1094; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; NDLYPRG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000008207; 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..421
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000164642"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   421 AA;  45409 MW;  12901DB29CE164F0 CRC64;
     MRVLVLGGGV VGVASAYYLA RAGHEVTVLD RQPGAGLETS FANAGQVSPG YSAPWAAPGI
     PLKAMKWLMM RHRPLVLWPR LEPRLYGWLA QMLANCTEEA YRRNKGRMVR LAEFSRDALR
     ELRAETGIAY DHREKGTLQL FRTRKQLDHV GEDTSVLDEY GVAYEVLDEG GCIAAEPALA
     RVRGGFVGGL RLPGDETGDA HLFTQRLAAI CARRGVSFRY GVTVARLRHE AGRITGVETG
     TGEVLTADAY VAAMGSYTPA LLRPLGLALP VYPVKGYSLT LPVTDESAAP VSTVMDETFK
     VAITRLGDRI RVGGTAELAG FSGTLRGPRR ATLERSLRDL FPAGGDARQA QFWTGLRPMT
     PDGTPIVGPT VYDNLYTNTG HGTLGWTMAC GSGRLLADLI TGRAPEIAHE DLSGARYLKA
     A