ID   Q8DUL2_STRMU            Unreviewed;       449 AA.
AC   Q8DUL2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN   OrderedLocusNames=SMU_913 {ECO:0000313|EMBL:AAN58621.1};
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58621.1, ECO:0000313|Proteomes:UP000002512};
RN   [1] {ECO:0000313|EMBL:AAN58621.1, ECO:0000313|Proteomes:UP000002512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA   Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC       ECO:0000256|RuleBase:RU004417}.
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DR   EMBL; AE014133; AAN58621.1; -; Genomic_DNA.
DR   RefSeq; NP_721315.1; NC_004350.2.
DR   RefSeq; WP_002263849.1; NC_004350.2.
DR   AlphaFoldDB; Q8DUL2; -.
DR   STRING; 210007.SMU_913; -.
DR   GeneID; 66817661; -.
DR   KEGG; smu:SMU_913; -.
DR   PATRIC; fig|210007.7.peg.815; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_2_1_9; -.
DR   OrthoDB; 9803297at2; -.
DR   PhylomeDB; Q8DUL2; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   PANTHER; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT   DOMAIN          205..447
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         212
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            169
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   449 AA;  48233 MW;  C949B97D343B114A CRC64;
     MTTGKEYVAS VFEKVKAQNA HEPEFLQAVE EVFESLIPVF DNYPKYIEEN LLERLVEPER
     IVSFRVPWVD DKGQVQVNRG FRVQFSSAIG PYKGGLRFHP SVNQSIIKFL GFEQIFKNSL
     TGQPIGGGKG GSNFDPKGKS DNEIMRFCQS FMTELSKHIG ADTDVPAGDI GVGGREIGYL
     YGQYKRLRNE YTGVLTGKGL TWGGSLARTE ATGYGAVYFA EQMLKARGQD FAGKTAIVSG
     SGNVAIYATE KLQTLGAKVV AVSDSSGYVY DPDGIDVALL KELKEVQRAR IIKYADARPN
     ASFTPAGGDS IWTIKADLAF PCATQNELNE ADAKTLVANG VIAVSEGANM PSTLEAIDVF
     LKAGVSFGPA KAANAGGVAV SALEMAQNSQ RTAWTFEEVD RKLYDIMKGI YDNSAAAAKS
     FGQEGNLVVG ANIAGFLKVA DAMSAQGIV
//