ID   DHE3_MAIZE              Reviewed;         411 AA.
AC   Q43260; O04871; O04872;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 128.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
GN   Name=GDH1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Golden cross Bantam T51; TISSUE=Root;
RX   PubMed=7551585; DOI=10.1093/oxfordjournals.pcp.a078823;
RA   Sakakibara H., Fujii K., Sugiyama T.;
RT   "Isolation and characterization of a cDNA that encodes maize glutamate
RT   dehydrogenase.";
RL   Plant Cell Physiol. 36:789-797(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND MUTANT GDH1.
RC   STRAIN=cv. P-10 Inbred; TISSUE=Shoot;
RA   Ju G.C.;
RT   "Characterization of a GDH1-mutant in maize.";
RL   Submitted (MAR-1997) 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; D49475; BAA08445.1; -; mRNA.
DR   EMBL; U93560; AAB51595.1; -; mRNA.
DR   EMBL; U93561; AAB51596.1; -; mRNA.
DR   PIR; T03294; T03294.
DR   PIR; T04342; T04342.
DR   RefSeq; NP_001105301.1; NM_001111831.1.
DR   AlphaFoldDB; Q43260; -.
DR   SMR; Q43260; -.
DR   STRING; 4577.Q43260; -.
DR   PaxDb; 4577-GRMZM2G178415_P01; -.
DR   GeneID; 542220; -.
DR   KEGG; zma:542220; -.
DR   MaizeGDB; 12238; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   InParanoid; Q43260; -.
DR   OrthoDB; 45283at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q43260; baseline and differential.
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:0006995; P:cellular response to nitrogen starvation; IEA:EnsemblPlants.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   GO; GO:1901698; P:response to nitrogen compound; IEA:EnsemblPlants.
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   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..411
FT                   /note="Glutamate dehydrogenase"
FT                   /id="PRO_0000182749"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   VARIANT         18
FT                   /note="L -> V (in strain: cv. P-10 Inbred)"
FT   VARIANT         370
FT                   /note="I -> M (in strain: cv. P-10 Inbred)"
FT   VARIANT         376
FT                   /note="N -> D (in strain: cv. P-10 Inbred)"
FT   MUTAGEN         188
FT                   /note="G->R: In GDH1."
FT   MUTAGEN         246
FT                   /note="D->G: In GDH1."
FT   MUTAGEN         252..253
FT                   /note="QL->EV: In GDH1."
FT   MUTAGEN         367
FT                   /note="R->Q: In GDH1."
SQ   SEQUENCE   411 AA;  44022 MW;  648C67A9338922CF CRC64;
     MNALAATSRN FKQAAKLLGL DSKLEKSLLI PFREIKVECT IPKDDGTLAS YVGFRVQHDN
     ARGPMKGGIR YHHEVDPDEV NALAQLMTWK TAVANIPYGG AKGGIGCSPG DLSISELERL
     TRVFTQKIHD LIGIHTDVPA PDMGTNSQTM AWILDEYSKF HGYSPAVVTG KPVDLGGSLG
     RDAATGRGVL FATEALLAEH GKGIAGQRFV IQGFGNVGSW AAQLISEAGG KVIAISDVTG
     AVKNVDGLDI AQLVKHSAEN KGIKGFKGGD AIAPDSLLTE ECDVLIPAAL GGVINKDNAN
     DIKAKYIIEA ANHPTDPEAD EILSKKGVLI LPDILANSGG VTVSYFEWVQ NIQGFMWDEE
     KVNAELRTYI TRAFGNVKQM CRSHSCDLRM GAFTLGVNRV ARATVLRGWE A
//