ID   DADA_NEIG1              Reviewed;         419 AA.
AC   Q5F5W1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=NGO1808;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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; AE004969; AAW90426.1; -; Genomic_DNA.
DR   RefSeq; WP_003690316.1; NC_002946.2.
DR   RefSeq; YP_208838.1; NC_002946.2.
DR   AlphaFoldDB; Q5F5W1; -.
DR   SMR; Q5F5W1; -.
DR   STRING; 242231.NGO_1808; -.
DR   EnsemblBacteria; AAW90426; AAW90426; NGO_1808.
DR   GeneID; 66754332; -.
DR   KEGG; ngo:NGO_1808; -.
DR   PATRIC; fig|242231.10.peg.2169; -.
DR   HOGENOM; CLU_007884_9_2_4; -.
DR   OMA; NDLYPRG; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000000535; 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; Reference proteome.
FT   CHAIN           1..419
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000066100"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   419 AA;  46845 MW;  F435775806AABDE3 CRC64;
     MKVLVLGAGV AGVSSVWYLA EAGHEVTVID RTEGVAMETS FANAGQLSYG YTTPWAAPGI
     PTKALKRLFK SHPPLLFRPD GGLYQIEWLW RMLQNCTATR YQINKERMVR ISEYSREMFR
     RFEAQTDMNF EGRKKGTLQI FRQTEEVEAA KQDIAVLERY GVPYRRLKPE ECAEFEPALA
     RVTAKIVGGL HLPADATGDC RLFTENLYKL CQEKGVRFYF NQTISRIDHN GLRIKAVETE
     TGRFETDAVV CALGCFSRTV LAQLDLNLPI YPVKGYSLTL PVTNSDGAPV STVLDESYKV
     AITRFDNRIR VGGMAELSGY ETKLPEKRRE TLALVVNDLF PEGGDLSQAL SWSGLRPMTP
     DSTPLIGRTR FENLFLNTGH GTLGWTMSPG SAKLTADIVS GKDTEIRSDD LSLSRYQKL