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DHE3_ARATH
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   03-AUG-2022, entry version 142.
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}.
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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.AT3G03910.1; -.
DR   PaxDb; Q9S7A0; -.
DR   PRIDE; Q9S7A0; -.
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; locus:2079364; AT3G03910.
DR   eggNOG; KOG2250; Eukaryota.
DR   HOGENOM; CLU_025763_1_2_1; -.
DR   InParanoid; Q9S7A0; -.
DR   OMA; MAWMYDE; -.
DR   OrthoDB; 692851at2759; -.
DR   PhylomeDB; Q9S7A0; -.
DR   BioCyc; ARA:AT3G03910-MON; -.
DR   BRENDA; 1.4.1.3; 399.
DR   PRO; PR:Q9S7A0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9S7A0; baseline and differential.
DR   Genevisible; Q9S7A0; AT.
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; IBA:GO_Central.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   GO; GO:0051171; P:regulation of nitrogen compound metabolic process; 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   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
 
 
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