ID DHE3_ARATH Reviewed; 411 AA. AC Q9S7A0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 149. DE RecName: Full=Probable glutamate dehydrogenase 3; DE Short=GDH 3; DE EC=1.4.1.3; GN Name=GSH3; OrderedLocusNames=At3g03910; ORFNames=F20H23.4, T11I18.2; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). RN [2] 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; AC009540; AAF00627.1; -; Genomic_DNA. DR EMBL; AC011698; AAF05851.1; -; Genomic_DNA. DR EMBL; CP002686; AEE74011.1; -; Genomic_DNA. DR RefSeq; NP_187041.1; NM_111262.2. DR AlphaFoldDB; Q9S7A0; -. DR SMR; Q9S7A0; -. DR BioGRID; 6405; 5. DR STRING; 3702.Q9S7A0; -. DR PaxDb; 3702-AT3G03910-1; -. DR ProteomicsDB; 224243; -. DR EnsemblPlants; AT3G03910.1; AT3G03910.1; AT3G03910. DR GeneID; 821072; -. DR Gramene; AT3G03910.1; AT3G03910.1; AT3G03910. DR KEGG; ath:AT3G03910; -. DR Araport; AT3G03910; -. DR TAIR; AT3G03910; GDH3. DR eggNOG; KOG2250; Eukaryota. DR HOGENOM; CLU_025763_1_2_1; -. DR InParanoid; Q9S7A0; -. DR OMA; FNAYRVQ; -. DR OrthoDB; 45283at2759; -. DR PhylomeDB; Q9S7A0; -. DR BioCyc; ARA:AT3G03910-MONOMER; -. DR BRENDA; 1.4.1.3; 399. DR PRO; PR:Q9S7A0; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9S7A0; baseline and differential. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005739; C:mitochondrion; 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:0006520; P:amino acid metabolic process; IEA:InterPro. DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; 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: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. DR Genevisible; Q9S7A0; AT. PE 3: Inferred from homology; KW NAD; Oxidoreductase; Reference proteome. FT CHAIN 1..411 FT /note="Probable glutamate dehydrogenase 3" FT /id="PRO_0000182747" FT ACT_SITE 102 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011" SQ SEQUENCE 411 AA; 44528 MW; B972A0ABBDA87D59 CRC64; MNALAATNRN FKLASRLLGL DSKLEKSLLI PFREIKVECT IPKDDGTLAS FVGFRVQHDN ARGPMKGGIR YHPEVEPDEV NALAQLMTWK TAVAKIPYGG AKGGIGCDPS ELSLSELERL TRVFTQKIHD LIGIHTDVPA PDMGTGPQTM AWILDEYSKF HGHSPAVVTG KPIDLGGSLG RDAATGRGVL FATEALLNEH GKTISGQRFA IQGFGNVGSW AAKLISDKGG KIVAVSDVTG AIKNNNGIDI LSLLEHAEEN RGIKGFDGAD SIDPDSILVE DCDILVPAAL GGVINRENAN EIKAKFIIEG ANHPTDPEAD EILKKKGVMI LPDIYANSGG VTVSYFEWVQ NIQGFMWDEE KVNRELKTYM TRGFKDLKEM CQTHSCDLRM GAFTLGINRV AQATTIRGWG S //