ID   DHE3_BACTN              Reviewed;         444 AA.
AC   P94598;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
DE   AltName: Full=NAD(P)H-utilizing glutamate dehydrogenase;
GN   Name=gdhA; OrderedLocusNames=BT_1970;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=8955404; DOI=10.1128/jb.178.24.7212-7220.1996;
RA   Baggio L., Morrison M.;
RT   "The NAD(P)H-utilizing glutamate dehydrogenase of Bacteroides
RT   thetaiotaomicron belongs to enzyme family I, and its activity is affected
RT   by trans-acting gene(s) positioned downstream of gdhA.";
RL   J. Bacteriol. 178:7212-7220(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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=1.4.1.3;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10011};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC         NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10011};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB40143.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U82241; AAB40143.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE015928; AAO77077.1; -; Genomic_DNA.
DR   RefSeq; NP_810883.1; NC_004663.1.
DR   RefSeq; WP_011108072.1; NC_004663.1.
DR   AlphaFoldDB; P94598; -.
DR   SMR; P94598; -.
DR   STRING; 226186.BT_1970; -.
DR   PaxDb; 226186-BT_1970; -.
DR   EnsemblBacteria; AAO77077; AAO77077; BT_1970.
DR   GeneID; 60927954; -.
DR   KEGG; bth:BT_1970; -.
DR   PATRIC; fig|226186.12.peg.2018; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_2_1_10; -.
DR   InParanoid; P94598; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:RHEA.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..444
FT                   /note="Glutamate dehydrogenase"
FT                   /id="PRO_0000182766"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   444 AA;  49017 MW;  6563EB81F0746095 CRC64;
     MNAAKVLDDL KRRFPNEPEY HQAVEEVLST IEEEYNKHPE FDKANLIERL CIPDRVFQFR
     VTWMDDKGNI QTNMGYRVQH NNAIGPYKGG IRFHASVNLS ILKFLAFEQT FKNSLTTLPM
     GGGKGGSDFS PRGKSNAEVM RFVQAFMLEL WRHIGPETDV PAGDIGVGGR EVGFMFGMYK
     KLAHEFTGTF TGKGREFGGS LIRPEATGYG NIYFLMEMLK TKGTDLKGKV CLVSGSGNVA
     QYTIEKVIEL GGKVVTCSDS DGYIYDPDGI DREKLDYIME LKNLYRGRIR EYAEKYGCKY
     VEGAKPWGEK CDIALPSATQ NELNGDHARQ LVANGCIAVS EGANMPSTPE AVRVFQDAKI
     LYAPGKAANA GGVSVSGLEM TQNSIKLSWS AEEVDEKLKS IMKNIHEACV QYGTEADGYV
     NYVKGANVAG FMKVAKAMMA QGIV
//