ID   DADA_NEIM0              Reviewed;         418 AA.
AC   A9M3T2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=NMCC_1976;
OS   Neisseria meningitidis serogroup C (strain 053442).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=374833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=053442;
RX   PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA   Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA   Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA   Liang X., Xu J., Jin Q.;
RT   "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT   clone.";
RL   Genomics 91:78-87(2008).
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; CP000381; ABX74100.1; -; Genomic_DNA.
DR   RefSeq; WP_012222126.1; NC_010120.1.
DR   AlphaFoldDB; A9M3T2; -.
DR   SMR; A9M3T2; -.
DR   EnsemblBacteria; ABX74100; ABX74100; NMCC_1976.
DR   KEGG; nmn:NMCC_1976; -.
DR   HOGENOM; CLU_007884_9_2_4; -.
DR   OMA; NDLYPRG; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001177; 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"
FT                   /id="PRO_1000085513"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   418 AA;  46625 MW;  30A3C96B4816B626 CRC64;
     MKVLVLGAGV AGVSSAWYLA EAGHEVTVID RAEGVAMETS FANAGQLSYG YTTPWAAPGI
     PTKALKWLFK SHPPLLFRPD GSLYQIEWLW QMLQNCTAAH YQTNKERMVR ISEYSREMFR
     RFEAQTGMNF EERKKGTLQI FRQTKEVEAA EQDIAVLERY GVPYRRLKPE ECAEFEPALA
     RVTAKIASGL HLPADATGDC RLFTENLYKL CQEKGVRFHF NQTISRIDHN GLRIKTVETE
     TGRFEADAVV CALGCFSRTV LAQLDLNLPI YPVKGYSLTL PVTNSDGAPV STVLDESYKV
     AITRFDNRIR VGGMAELSGY EIKLPEKRRE TLALVVNDLF PEGGDLSQAS FWSGLRPMTP
     DSTPLIGRTR FDNLFLNTGH GTLGWTMSLG SAKLTADIVS GKDTEIRSDD LSLSRYQA