ID   DADA2_RHILO             Reviewed;         416 AA.
AC   Q98B75;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=D-amino acid dehydrogenase 2;
DE            EC=1.4.99.-;
GN   Name=dadA2; OrderedLocusNames=mlr5698;
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   -!- SIMILARITY: Belongs to the DadA oxidoreductase family. {ECO:0000305}.
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DR   EMBL; BA000012; BAB52097.1; -; Genomic_DNA.
DR   RefSeq; WP_010913435.1; NC_002678.2.
DR   AlphaFoldDB; Q98B75; -.
DR   SMR; Q98B75; -.
DR   STRING; 266835.14025497; -.
DR   EnsemblBacteria; BAB52097; BAB52097; BAB52097.
DR   KEGG; mlo:mlr5698; -.
DR   PATRIC; fig|266835.9.peg.4531; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; GIHYDER; -.
DR   OrthoDB; 573710at2; -.
DR   Proteomes; UP000000552; Chromosome.
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.
FT   CHAIN           1..416
FT                   /note="D-amino acid dehydrogenase 2"
FT                   /id="PRO_0000166146"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   416 AA;  45097 MW;  AA232E66BF541723 CRC64;
     MKITVLGAGV VGTAAAYYLA ADGHEVTVIE RHAAPARGTS QSNAGLVSPG DATAWASPAA
     LKTFLRGLYN HDLGIKVRLR FDPYFLAWSL RFLRQCTVAR LRANSQVKLR LALYSRDCIN
     AISADTGIHY DERKKGILYF FRSQHSLNTG TDNYRYLAEH GLPIEIVGRD RLVELEPGLA
     GVKEKIAGGV YSPIDQTGDS RLFVDNLAAY ASEKLGVKFL FGTTVEGLDI QGDRVRAVMT
     SAGPVTGDAV VISMGPESGL LGRRYGIDLP VYPVKGYTAT IPLEDESKGP TIGGADEDQL
     MAYSRLGNRL RLASTAEFTG FDRTHKPSDF TTMFRTARDL FPGAFDEKKA ELWAGLRPMM
     PGSVPVIGQA RYKNLYLDTG HGHVGWTMAC GSGKFLADLV AGRKPEIDPQ GLVYGG