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 27-MAR-2024, entry version 159. 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}. 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; 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; 3. DR STRING; 3702.Q43314; -. DR iPTMnet; Q43314; -. DR PaxDb; 3702-AT5G18170-1; -. 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; AT5G18170; GDH1. DR eggNOG; KOG2250; Eukaryota. DR HOGENOM; CLU_025763_1_2_1; -. DR InParanoid; Q43314; -. DR OMA; WGPEKIV; -. DR OrthoDB; 45283at2759; -. DR PhylomeDB; Q43314; -. DR BioCyc; ARA:AT5G18170-MONOMER; -. DR BRENDA; 1.4.1.3; 399. DR PRO; PR:Q43314; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q43314; baseline and differential. 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; IEA:RHEA. 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:0006520; P:amino acid metabolic process; IEA:InterPro. 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 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:SF30; GLUTAMATE DEHYDROGENASE 1; 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. DR Genevisible; Q43314; AT. 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 //