DHE3_MAIZE
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 03-AUG-2022, entry version 121.
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.GRMZM2G178415_P01; -.
DR PaxDb; Q43260; -.
DR PRIDE; Q43260; -.
DR GeneID; 542220; -.
DR KEGG; zma:542220; -.
DR MaizeGDB; 12238; -.
DR eggNOG; KOG2250; Eukaryota.
DR OrthoDB; 692851at2759; -.
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 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 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