DHE3_SOLLC
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 03-AUG-2022, entry version 116.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.Solyc10g078550.1.1; -.
DR PaxDb; P93541; -.
DR GeneID; 544015; -.
DR KEGG; sly:544015; -.
DR eggNOG; KOG2250; Eukaryota.
DR InParanoid; P93541; -.
DR BioCyc; MetaCyc:MON-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 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 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