ID   DADA3_RHILO             Reviewed;         412 AA.
AC   Q981X2;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=D-amino acid dehydrogenase 3;
DE            EC=1.4.99.-;
GN   Name=dadA3; OrderedLocusNames=mlr9201;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OG   Plasmid pMLa.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- FUNCTION: Oxidative deamination of D-amino acids. {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family. {ECO:0000305}.
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DR   EMBL; BA000013; BAB54587.1; -; Genomic_DNA.
DR   RefSeq; WP_010915866.1; NC_002679.1.
DR   AlphaFoldDB; Q981X2; -.
DR   SMR; Q981X2; -.
DR   PRIDE; Q981X2; -.
DR   EnsemblBacteria; BAB54587; BAB54587; BAB54587.
DR   KEGG; mlo:mlr9201; -.
DR   PATRIC; fig|266835.9.peg.7006; -.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; KLSWFAE; -.
DR   OrthoDB; 573710at2; -.
DR   Proteomes; UP000000552; Plasmid pMLa.
DR   GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
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; Plasmid.
FT   CHAIN           1..412
FT                   /note="D-amino acid dehydrogenase 3"
FT                   /id="PRO_0000166147"
FT   BINDING         4..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  45555 MW;  5D3D0C94AC37C72C CRC64;
     MPKIVVIGAG IAGVSTAYAL LEQGYDVTVV ERRRYAAMET SFANGGQLSA SNAEVWNHWS
     TVLKGIKWML RRDAPLLMNP TPSWHKYSWL LEFVSNISRY RENTIETTRL AIAARKHLFE
     IADREGIDFD HVRRGILHVY WDKDGFDHAL KVNEMLNEGG LDRRSVTPSE FAGIEPALHG
     KFYGGFYTPS DSTGDIHKYC AGLEKACTKR GAQFIYDAAV TRIERRDRFN IVCATDGADQ
     TLVADGIVVC AGTNSRDIAA MFGDRINIYP VKGYSITVEL DGAAADSSAP WVSILDDRAK
     IVTSRLGAAR LRVAGTAEFN GVNFDIREDR IRPLVDWTRM MFPKVATEHV VPWAGLRPMM
     PNMMPRVGKS RVPGVFYNTG HGHLGWTLSA ATSAMLATVV ATDLPIDARL AA