ID   DHE2_CLODI              Reviewed;         421 AA.
AC   P27346;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=NAD-specific glutamate dehydrogenase;
DE            Short=NAD-GDH;
DE            EC=1.4.1.2;
GN   Name=gluD;
OS   Clostridioides difficile (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=1496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1774279; DOI=10.1128/jcm.29.11.2639-2642.1991;
RA   Lyerly D.M., Barroso L.A., Wilkins T.D.;
RT   "Identification of the latex test-reactive protein of Clostridium difficile
RT   as glutamate dehydrogenase.";
RL   J. Clin. Microbiol. 29:2639-2642(1991).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC         NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; M65250; AAA62756.1; -; Genomic_DNA.
DR   PIR; S28829; S28829.
DR   RefSeq; WP_003420866.1; NZ_WUUI01000006.1.
DR   AlphaFoldDB; P27346; -.
DR   SMR; P27346; -.
DR   PRIDE; P27346; -.
DR   GeneID; 66352729; -.
DR   OMA; TNAWWWW; -.
DR   BRENDA; 1.4.1.2; 1473.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; ISS:UniProtKB.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..421
FT                   /note="NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182737"
FT   ACT_SITE        107
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            147
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   421 AA;  46016 MW;  31F0A09802F4AD94 CRC64;
     MSGKDVNVFE MAQSQVKNAC DKLGMEPAVY ELLKEPMRVI EVSIPVKMDD GSIKTFKGFR
     SQHNDAVGPT KGGIRFHQNV SRDEVKALSI WMTFKCSVTG IPYGGGKGGI IVDPSTLSQG
     ELERLSRGYI DGIYKLIGEK VDVPAPDVNT NGQIMSWMVD EYNKLTGQSS IGVITGKPVE
     FGGSLGRTAA TGFGVAVTAR EAAAKLGIDM KKAKIAVQGI GNVGSYTVLN CEKLGGTVVA
     MAEWCKSEGS YAIYNENGLD GQAMLDYMKE HGNLLNFPGA KRISLEEFWA SDVDIVIPAA
     LENSITKEVA ESIKAKLVCE AANGPTTPEA DEVFAERGIV LTPDILTNAG GVTVSYFEWV
     QNLYGYYWSE EEVEQKEEIA MVKAFESIWK IKEEYNVTMR EAAYMHSIKK VAEAMKLRGW
     Y