ID   DADA1_RHILO             Reviewed;         418 AA.
AC   Q98F08;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=D-amino acid dehydrogenase 1;
DE            EC=1.4.99.-;
GN   Name=dadA1; OrderedLocusNames=mll3992;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
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   -!- 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. {ECO:0000305}.
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DR   EMBL; BA000012; BAB50759.1; -; Genomic_DNA.
DR   RefSeq; WP_010912102.1; NC_002678.2.
DR   AlphaFoldDB; Q98F08; -.
DR   SMR; Q98F08; -.
DR   STRING; 266835.14024155; -.
DR   PRIDE; Q98F08; -.
DR   EnsemblBacteria; BAB50759; BAB50759; BAB50759.
DR   KEGG; mlo:mll3992; -.
DR   PATRIC; fig|266835.9.peg.3170; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; FWYKEDG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000000552; 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.
FT   CHAIN           1..418
FT                   /note="D-amino acid dehydrogenase 1"
FT                   /id="PRO_0000166145"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  46018 MW;  E3F633DB2909E29C CRC64;
     MQIMVLGGGV IGVTTAYYLA EAGHEVTVLD RQKGPALETS FANAGEISPG YASPWAGPGI
     PLKAIKWLLM KHGPLVVRPA FDPHMWTWLV KMLRNCTTER YAINKSRMVP LAEYSRDTLK
     ALREATGITY DERTQGTLQL FRTQKQLDGT GGDVEVLKKY GVSYEILDQD GCIAAEPALG
     GVREKFVGGL RLPHDETGDC KMFTEKLAEL CVARGVKFEY DTTIWRVLRS RNRVANLSTS
     KGFKASEAYV MALGSYSAGF MRRMKRSIPV YPVKGYSITV PIKDADVAPV STVMDETYKV
     AITRLGDRIR VGGTAEISGF DLRLHESRRR TLEHSVGDLF PGAGAMREAT FWCGLRPMTP
     DGPPLIGRTE LSNLFLNTGH GTLGWTMACG SAKVLADIMS NKVPEIDARA LAQERYLK