ID   DHE3_SOLLC              Reviewed;         412 AA.
AC   P93541;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   24-JAN-2024, entry version 122.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
DE   AltName: Full=Legdh1;
GN   Name=GDH1;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Pera;
RX   PubMed=9074503; DOI=10.1016/s0378-1119(96)00716-0;
RA   Purnell M.P., Stewart G.R., Botella J.R.;
RT   "Cloning and characterisation of a glutamate dehydrogenase cDNA from tomato
RT   (Lycopersicon esculentum L.).";
RL   Gene 186:249-254(1997).
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: In roots, stems, leaves and flowers but not in
CC       fruits.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; U48695; AAB39508.1; -; mRNA.
DR   PIR; JC6317; JC6317.
DR   RefSeq; NP_001233850.2; NM_001246921.2.
DR   AlphaFoldDB; P93541; -.
DR   SMR; P93541; -.
DR   STRING; 4081.P93541; -.
DR   PaxDb; 4081-Solyc10g078550-1-1; -.
DR   GeneID; 544015; -.
DR   KEGG; sly:544015; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   InParanoid; P93541; -.
DR   OrthoDB; 45283at2759; -.
DR   BioCyc; MetaCyc:MONOMER-15559; -.
DR   BRENDA; 1.4.1.2; 3101.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P93541; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
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; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF29; GLUTAMATE DEHYDROGENASE 3-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   2: Evidence at transcript level;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..412
FT                   /note="Glutamate dehydrogenase"
FT                   /id="PRO_0000182748"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   412 AA;  44813 MW;  83BC4138047A6BCA CRC64;
     MNALAATNRN FKLAARLLGL DSKLELSLLI PFREIKVECT IPKDDGTLAS FVGFRVQHDN
     ARGPMKGGIR YHPEVDPDEV NALAQLMTWK TAVANIPYGG AKGGIGCSPS DLSISELERL
     TRVFTQKIHD LIGIHTDVPA PDMGTNPQTM AWILDEYSKF HGYSPAVVTG KPVDLGGSLG
     RDAATGRGAL FATEALLNEH GKSVAGQRFV IQGFGNVGSW AAKLIHEQGG KVVAVSDITG
     AIKNEKGIDI ESLFKHVKET RGVKGFHDAH PIDANSILVE DCDVLIPAAL GGVINKDNHK
     LKIKAKYIIE AANHPTDPEA DEILSKKGVT ILPDIYANSG GVTVSYFEWV QNIQGFMWDE
     KKVNDELKTY MTRGFKDVKD MCKTHNCDLR MGAFTLGVNR VARATVLRGW EA
//