ID   DHE2_BACFR              Reviewed;         445 AA.
AC   P94316; Q64Q53;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=NAD-specific glutamate dehydrogenase;
DE            Short=NAD-GDH;
DE            EC=1.4.1.2;
DE   AltName: Full=NADH-dependent glutamate dehydrogenase;
GN   Name=gdhB; OrderedLocusNames=BF3635;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BF1;
RX   PubMed=9639936; DOI=10.1099/00221287-144-6-1659;
RA   Abrahams G.L., Abratt V.R.;
RT   "The NADH-dependent glutamate dehydrogenase enzyme of Bacteroides fragilis
RT   Bf1 is induced by peptides in the growth medium.";
RL   Microbiology 144:1659-1667(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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   -!- INDUCTION: By high peptide concentrations.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; U78108; AAC26399.1; -; Genomic_DNA.
DR   EMBL; AP006841; BAD50378.1; -; Genomic_DNA.
DR   RefSeq; WP_011203378.1; NC_006347.1.
DR   RefSeq; YP_100912.1; NC_006347.1.
DR   AlphaFoldDB; P94316; -.
DR   SMR; P94316; -.
DR   STRING; 295405.BF3635; -.
DR   PRIDE; P94316; -.
DR   EnsemblBacteria; BAD50378; BAD50378; BF3635.
DR   KEGG; bfr:BF3635; -.
DR   PATRIC; fig|295405.11.peg.3488; -.
DR   HOGENOM; CLU_025763_2_1_10; -.
DR   OMA; PCFAAFP; -.
DR   Proteomes; UP000002197; Chromosome.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_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   2: Evidence at transcript level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..445
FT                   /note="NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182765"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         235..241
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        44
FT                   /note="S -> A (in Ref. 1; AAC26399)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   445 AA;  48390 MW;  E7462E4E6963217B CRC64;
     MNIEKIMSSL EAKHPGESEY LQAVKEVLLS IEDIYNQHPE FEKSKIIERL VEPDRIFTFR
     VTWVDDKGEV QTNLGYRVQF NNAIGPYKGG IRFHASVNLS ILKFLGFEQT FKNALTTLPM
     GGGKGGSDFS PRGKSDAEIM RFCQAFMLEL WRHLGPDMDV PAGDIGVGGR EVGYMFGMYK
     KLTREFTGTF TGKGLEFGGS LIRPEATGFG GLYFVNQMLQ TKGIDIKGKT VAISGFGNVA
     WGAATKATEL GAKVVTISGP DGYIYDPNGI SGEKIDYMLE LRASGNDIVA PYADEFPGST
     FVAGKRPWEV KADIALPCAT QNELNGEDAK NLIDNNVLCV GEISNMGCTP EAIDLFIEHK
     TMYAPGKAVN AGGVATSGLE MSQNAMHLSW SAAEVDEKLH SIMHGIHAQC VKYGTEPDGY
     INYVKGANIA GFMKVAHAMM GQGII