ID   DHE3_SINFN              Reviewed;         443 AA.
AC   Q53199;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Probable glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
GN   OrderedLocusNames=NGR_a01340; ORFNames=y4uF;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8796346; DOI=10.1101/gr.6.7.590;
RA   Freiberg C., Perret X., Broughton W.J., Rosenthal A.;
RT   "Sequencing the 500-kb GC-rich symbiotic replicon of Rhizobium sp. NGR234
RT   using dye terminators and a thermostable 'sequenase': a beginning.";
RL   Genome Res. 6:590-600(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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   -!- 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   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; Z68203; CAA92406.1; -; Genomic_DNA.
DR   EMBL; U00090; AAB91878.1; -; Genomic_DNA.
DR   RefSeq; NP_444091.1; NC_000914.2.
DR   AlphaFoldDB; Q53199; -.
DR   SMR; Q53199; -.
DR   STRING; 394.NGR_a01340; -.
DR   EnsemblBacteria; AAB91878; AAB91878; NGR_a01340.
DR   KEGG; rhi:NGR_a01340; -.
DR   PATRIC; fig|394.7.peg.117; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_1_0_5; -.
DR   OMA; WNPRGID; -.
DR   OrthoDB; 1184827at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:RHEA.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
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; 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.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN           1..443
FT                   /note="Probable glutamate dehydrogenase"
FT                   /id="PRO_0000182753"
FT   ACT_SITE        86
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   443 AA;  48845 MW;  3D61C9122A9523BE CRC64;
     MSFLDLPEGL PERIIQCNSP YTVRFGVRLR GRMYSFIGWR SVREHCEPVK GDIRYASNAD
     AEEVEALAAL MTLKCSLVDV PFGGSKGALK IDPRGWTPQE LEHITRRFTQ EMNKRPDRAR
     RQCVGSDIGT GEREMAWMMD EFRRANPTDV VTSGACVTGK PLSKGGIAGR AESTGRGVQF
     AIQSSLRDTR TPGLDGRRNL KGASTVIQGF GNVGYHAARF LSEEDDARVT VLAERDGYVA
     NPEGLSIEAL KQHQIRTGSI LGFDGAKSIA GDMCGVEQPC DVLIPAAMEN AIHAENAERM
     KAHLVVEAAN GPVTFEADEI LRSRGVTILP DLYVNAGGVV VSYFERVKNL THIPFGLMER
     RRRERGNHTI ATALERMTGK ESPADMRDEF LEGGAEIDLV RSGLEDVMRS TWTRIADLME
     QQPELGDYRT AAYVASIRQV ADL