ID   DHE3_VITVI              Reviewed;         411 AA.
AC   P52596;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
GN   Name=GDH;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sultanina; TISSUE=Shoot;
RX   PubMed=8626071; DOI=10.1016/0378-1119(96)83097-6;
RA   Syntichaki K.M., Loulakakis K.A., Roubelakis-Angelakis K.A.;
RT   "The amino-acid sequence similarity of plant glutamate dehydrogenase to the
RT   extremophilic archaeal enzyme conforms to its stress-related function.";
RL   Gene 168:87-92(1996).
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; X86924; CAA60507.1; -; mRNA.
DR   PIR; S54797; S54797.
DR   RefSeq; NP_001268039.1; NM_001281110.1.
DR   AlphaFoldDB; P52596; -.
DR   SMR; P52596; -.
DR   STRING; 29760.VIT_16s0039g02750.t01; -.
DR   PRIDE; P52596; -.
DR   GeneID; 100257914; -.
DR   KEGG; vvi:100257914; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   OrthoDB; 692851at2759; -.
DR   ExpressionAtlas; P52596; baseline and differential.
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"
FT                   /id="PRO_0000182752"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   411 AA;  44546 MW;  A6C8F63237CF06B5 CRC64;
     MNALAATNRN FRHASRILGL DSKLEKSLLI PFREIKVECT IPKDDGSLAT YVGFRVQHDN
     ARGPMKGGIR YHPEVDPDEV NALAQLMTWK TAVVDIPYGG AKGGIGCTPK DLSMSELERL
     TRVFTQKIHD LIGTHTDVPA PDMGTNAQTM AWILDEYSKF HGHSPAVVTG KPIALGGSLG
     REAATGRGVV FATEALLAQH GKSIKGLTFV IQGFGNVGSW VARLIGERGG KIIAVSDVTG
     AVKNQNGLDI VDLLRHKEET GCLTNFSGGD HMDPNELLTH ECDVLIPCAL GGVLNKENAA
     DVKAKFIIEA ANHPTDPEAD EILSKKGGVI LPDIYANAGG VTVSYFEWVQ NIQGFMWEEE
     KVNNELQKYM TKAFHNIKAM CQSHNCSLRM GAFTLAVNRV ACATTLRGWE A