ID B4F9J5_MAIZE Unreviewed; 411 AA.
AC B4F9J5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=542220 {ECO:0000313|EnsemblPlants:Zm00001eb060520_P001};
GN ORFNames=ZEAMMB73_Zm00001d034420 {ECO:0000313|EMBL:ONM10205.1};
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 {ECO:0000313|EMBL:ACF78788.1};
RN [1] {ECO:0000313|EMBL:ACG34153.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [2] {ECO:0000313|EMBL:ACF78788.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACF78788.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [3] {ECO:0000313|EMBL:ONM10205.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb060520_P001,
RC ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM10205.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblPlants:Zm00001eb060520_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb060520_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
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:0000256|ARBA:ARBA00023525};
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:0000256|ARBA:ARBA00023549};
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC ECO:0000256|RuleBase:RU004417}.
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DR EMBL; BT033783; ACF78788.1; -; mRNA.
DR EMBL; BT035038; ACF80043.1; -; mRNA.
DR EMBL; BT039326; ACF84331.1; -; mRNA.
DR EMBL; BT040327; ACF85332.1; -; mRNA.
DR EMBL; EU962035; ACG34153.1; -; mRNA.
DR EMBL; BT061963; ACN26660.1; -; mRNA.
DR EMBL; BT064210; ACN28907.1; -; mRNA.
DR EMBL; BT067687; ACN34584.1; -; mRNA.
DR EMBL; CM007647; ONM10205.1; -; Genomic_DNA.
DR EMBL; CM007647; ONM10212.1; -; Genomic_DNA.
DR EMBL; CM007647; ONM10213.1; -; Genomic_DNA.
DR RefSeq; NP_001105301.1; NM_001111831.1.
DR RefSeq; NP_001241710.1; NM_001254781.1.
DR RefSeq; XP_008648531.1; XM_008650309.1.
DR RefSeq; XP_008648535.1; XM_008650313.1.
DR RefSeq; XP_008648541.1; XM_008650319.1.
DR AlphaFoldDB; B4F9J5; -.
DR SMR; B4F9J5; -.
DR IntAct; B4F9J5; 1.
DR STRING; 4577.B4F9J5; -.
DR EnsemblPlants; Zm00001eb060520_T001; Zm00001eb060520_P001; Zm00001eb060520.
DR EnsemblPlants; Zm00001eb060520_T004; Zm00001eb060520_P004; Zm00001eb060520.
DR EnsemblPlants; Zm00001eb060520_T005; Zm00001eb060520_P005; Zm00001eb060520.
DR GeneID; 542220; -.
DR Gramene; Zm00001eb060520_T001; Zm00001eb060520_P001; Zm00001eb060520.
DR Gramene; Zm00001eb060520_T004; Zm00001eb060520_P004; Zm00001eb060520.
DR Gramene; Zm00001eb060520_T005; Zm00001eb060520_P005; Zm00001eb060520.
DR KEGG; zma:542220; -.
DR HOGENOM; CLU_025763_1_2_1; -.
DR InParanoid; B4F9J5; -.
DR OMA; CTHEADI; -.
DR OrthoDB; 45283at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; B4F9J5; 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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000185-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B4F9J5};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT DOMAIN 178..408
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 142
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 411 AA; 44069 MW; E3F058788779DC2F 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 VQLVKHSAEN KGIKGFKGGD AIAPDSLLTE ECDVLIPAAL GGVINKDNAN
DIKAKYIIEA ANHPTDPEAD EILSKKGVLI LPDILANSGG VTVSYFEWVQ NIQGFMWDEE
KVNAELRTYM TRAFGDVKQM CRSHSCDLRM GAFTLGVNRV ARATVLRGWE A
//
