ID   DHEB_NICPL              Reviewed;         411 AA.
AC   Q9LEC8; O24119;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Glutamate dehydrogenase B;
DE            Short=GDH B;
DE            EC=1.4.1.3;
GN   Name=GDHB;
OS   Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=10353219; DOI=10.1093/oxfordjournals.pcp.a029547;
RA   Ficarelli A., Tassi F., Restivo F.M.;
RT   "Isolation and characterization of two cDNA clones encoding for glutamate
RT   dehydrogenase in Nicotiana plumbaginifolia.";
RL   Plant Cell Physiol. 40:339-342(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RA   Restivo F.M., Panizzi N., De Monte G., Ficarelli A.;
RT   "Genomic organisation of GDH genes in Nicotiana plumbaginifolia.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; Y08293; CAA69601.2; -; Genomic_DNA.
DR   EMBL; AJ277950; CAB94837.1; -; Genomic_DNA.
DR   PIR; T16982; T16982.
DR   AlphaFoldDB; Q9LEC8; -.
DR   SMR; Q9LEC8; -.
DR   BRENDA; 1.4.1.3; 3640.
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; 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..411
FT                   /note="Glutamate dehydrogenase B"
FT                   /id="PRO_0000182751"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   CONFLICT        92
FT                   /note="A -> R (in Ref. 1; CAA69601)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        368
FT                   /note="A -> D (in Ref. 1; CAA69601)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   411 AA;  44508 MW;  236D4915B8B670AE CRC64;
     MNALAATNRN FKLASRLLGL DSKLEQCLLI PFREIKVECT IPKDDGSLAT FIGFRVQHDN
     ARGPMKGGIR YHPEVDPDEV NALAQLMTWK TAVANIPYGG AKGGIGCSPS DLSISELERL
     TRVFTQKIHD LIGVHTDVPA PDMGTNPQTM AWILDEYSKF HGYSPAVVTG KPIDLGGSLG
     RDAATGRGVL FAAEALLRDH GKSIAGQRFV VQGFGNVGSW AAQLITEQGG KIVAVSDITG
     AIKNKNGIDI ASLLKHVKEN RGVKGFHGAD SIDPNSILVE DCDVLIPAAL GGVINRDNAK
     DIKAKFIVEA ANHPTDPEAD EILAKKGVVI LPDIYANSGG VTVSYFEWVQ NIQGFMWDEE
     RVNTELKAYM NRGFKDVKDM CKTHNCDLRM GAFTLGVNRV ARATTLRGWE A