ID   DADA_METS4              Reviewed;         421 AA.
AC   B0UBI8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=M446_2122;
OS   Methylobacterium sp. (strain 4-46).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4-46;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL   Submitted (FEB-2008) 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; CP000943; ACA16584.1; -; Genomic_DNA.
DR   RefSeq; WP_012331993.1; NC_010511.1.
DR   AlphaFoldDB; B0UBI8; -.
DR   SMR; B0UBI8; -.
DR   STRING; 426117.M446_2122; -.
DR   EnsemblBacteria; ACA16584; ACA16584; M446_2122.
DR   KEGG; met:M446_2122; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; FWYKEDG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
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..421
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138658"
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;  45749 MW;  2209BC09E83C775F CRC64;
     MRVLVLGGGV VGVTSAYYLA RAGHEVTVLD RQPGAGLETS FANAGQVSPG YSAPWAAPGI
     PLKAMKWLMM RHRPLVLWPQ LEPRLYGWLA RMLANCTQEA YQRNKGRMVR LAEFSRDALR
     DLRGETGIAY DHREKGTLQL FRTRKQLDHV GDDTRVLDAY GVAYEVLDPE GCIAAEPALA
     RVRDTFVGGL RLPGDETGDA HLFTQRLAAL CADRGVRFRF GVAVARLHHE AGRVTGVETA
     TGEVLRAEAY VAAMGSYTPA LLRPLGLSLP VYPVKGYSLT LPVTDEGSAP VSTVMDETYK
     VAITRLGDRI RVGGTAELAG FSQALRGPRR ATLERSLTDL FPAGGDLSRA TFWTGLRPMT
     PDGTPIVGAT AYGNLYTNTG HGTLGWTMAC GSGRMLADLI TGRHPEIAHE DFAERRYRRA
     A