DHE1_ARATH
ID DHE1_ARATH Reviewed; 411 AA.
AC Q43314;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Glutamate dehydrogenase 1;
DE Short=GDH 1;
DE EC=1.4.1.3;
GN Name=GDH1; OrderedLocusNames=At5g18170; ORFNames=MRG7.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Thakkar S., Weisemann J.M., Turano F.J.;
RT "Arabidopsis glutamate dehydrogenase 1.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Melo-Oliveira R., Oliveira I., Coruzzi G.;
RT "Arabidopsis mutant analysis and gene regulation define a nonredundant role
RT for glutamate dehydrogenase in nitrogen assimilation.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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; U37771; AAA82615.1; -; mRNA.
DR EMBL; U53527; AAB08057.1; -; mRNA.
DR EMBL; AB012246; BAB09475.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92515.1; -; Genomic_DNA.
DR PIR; S71217; S71217.
DR RefSeq; NP_197318.1; NM_121822.4.
DR PDB; 6YEH; X-ray; 2.59 A; A/B/C/D/E/F=1-411.
DR PDB; 6YEI; X-ray; 2.02 A; A/B/C/D/E/F=1-411.
DR PDBsum; 6YEH; -.
DR PDBsum; 6YEI; -.
DR AlphaFoldDB; Q43314; -.
DR SMR; Q43314; -.
DR BioGRID; 17211; 7.
DR IntAct; Q43314; 2.
DR STRING; 3702.AT5G18170.1; -.
DR iPTMnet; Q43314; -.
DR PaxDb; Q43314; -.
DR PRIDE; Q43314; -.
DR ProteomicsDB; 224278; -.
DR EnsemblPlants; AT5G18170.1; AT5G18170.1; AT5G18170.
DR GeneID; 831935; -.
DR Gramene; AT5G18170.1; AT5G18170.1; AT5G18170.
DR KEGG; ath:AT5G18170; -.
DR Araport; AT5G18170; -.
DR TAIR; locus:2172309; AT5G18170.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_025763_1_2_1; -.
DR InParanoid; Q43314; -.
DR OMA; WIVDQYT; -.
DR OrthoDB; 692851at2759; -.
DR PhylomeDB; Q43314; -.
DR BioCyc; ARA:AT5G18170-MON; -.
DR BRENDA; 1.4.1.3; 399.
DR PRO; PR:Q43314; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q43314; baseline and differential.
DR Genevisible; Q43314; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
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:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:TAIR.
DR GO; GO:0009646; P:response to absence of light; IEP:TAIR.
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 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..411
FT /note="Glutamate dehydrogenase 1"
FT /id="PRO_0000182745"
FT ACT_SITE 102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 32..42
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 77..94
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6YEI"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 147..161
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6YEH"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:6YEI"
FT TURN 179..183
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:6YEI"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:6YEI"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 339..352
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 359..384
FT /evidence="ECO:0007829|PDB:6YEI"
FT HELIX 388..407
FT /evidence="ECO:0007829|PDB:6YEI"
SQ SEQUENCE 411 AA; 44524 MW; 4F14E31CEC52935E CRC64;
MNALAATNRN FKLAARLLGL DSKLEKSLLI PFREIKVECT IPKDDGTLAS FVGFRVQHDN
ARGPMKGGIR YHPEVDPDEV NALAQLMTWK TAVAKIPYGG AKGGIGCDPS KLSISELERL
TRVFTQKIHD LIGIHTDVPA PDMGTGPQTM AWILDEYSKF HGYSPAVVTG KPIDLGGSLG
RDAATGRGVM FGTEALLNEH GKTISGQRFV IQGFGNVGSW AAKLISEKGG KIVAVSDITG
AIKNKDGIDI PALLKHTKEH RGVKGFDGAD PIDPNSILVE DCDILVPAAL GGVINRENAN
EIKAKFIIEA ANHPTDPDAD EILSKKGVVI LPDIYANSGG VTVSYFEWVQ NIQGFMWEEE
KVNDELKTYM TRSFKDLKEM CKTHSCDLRM GAFTLGVNRV AQATILRGWG A
