GSH1_ARATH
ID GSH1_ARATH Reviewed; 522 AA.
AC P46309; A0FGQ9; O82759; P92951; Q93ZQ6; Q944I8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Glutamate--cysteine ligase, chloroplastic {ECO:0000303|PubMed:15180996};
DE EC=6.3.2.2 {ECO:0000269|PubMed:15180996};
DE AltName: Full=Gamma-ECS;
DE Short=GCS;
DE AltName: Full=Gamma-glutamylcysteine synthetase;
DE AltName: Full=Protein ROOT MERISTEMLESS 1;
DE Short=AtGCL;
DE AltName: Full=Protein cadmium-sensitive 2;
DE AltName: Full=Protein phytoalexin-deficient 2;
DE Flags: Precursor;
GN Name=GSH1; Synonyms=CAD2, GCL, PAD2, RML1; OrderedLocusNames=At4g23100;
GN ORFNames=F7H19.290;
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].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7937837; DOI=10.1073/pnas.91.21.10059;
RA May M.J., Leaver C.J.;
RT "Arabidopsis thaliana gamma-glutamylcysteine synthetase is structurally
RT unrelated to mammalian, yeast, and Escherichia coli homologs.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:10059-10063(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-22, AND VARIANT ASN-48.
RC STRAIN=cv. Landsberg erecta;
RA Ullmann P., Gondet L., Bach T.J.;
RT "Isolation of an Arabidopsis thaliana cDNA encoding a putative gamma-
RT glutamylcysteine synthetase by complementation of a GSHI deficient yeast
RT mutant-glutamylcysteine synthetase.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9807829; DOI=10.1046/j.1365-313x.1998.00262.x;
RA Cobbett C.S., May M.J., Howden R., Rolls B.;
RT "The glutathione-deficient, cadmium-sensitive mutant, cad2-1, of
RT Arabidopsis thaliana is deficient in gamma-glutamylcysteine synthetase.";
RL Plant J. 16:73-78(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-22.
RC STRAIN=cv. Sha;
RA Kopriva S., Mullineaux P.M.;
RT "Glutathione synthesis in Arabidopsis ecotypes.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [6]
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).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [8]
RP FUNCTION.
RX PubMed=8090752; DOI=10.1073/pnas.91.19.8955;
RA Glazebrook J., Ausubel F.M.;
RT "Isolation of phytoalexin-deficient mutants of Arabidopsis thaliana and
RT characterization of their interactions with bacterial pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8955-8959(1994).
RN [9]
RP FUNCTION.
RX PubMed=7724670; DOI=10.1104/pp.107.2.365;
RA Cheng J.-C., Seeley K.A., Sung Z.R.;
RT "RML1 and RML2, Arabidopsis genes required for cell proliferation at the
RT root tip.";
RL Plant Physiol. 107:365-376(1995).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF 237-PRO--VAL-239.
RX PubMed=7770518; DOI=10.1104/pp.107.4.1067;
RA Howden R., Andersen C.R., Goldsbrough P.B., Cobbett C.S.;
RT "A cadmium-sensitive, glutathione-deficient mutant of Arabidopsis
RT thaliana.";
RL Plant Physiol. 107:1067-1073(1995).
RN [11]
RP FUNCTION.
RX PubMed=8725243; DOI=10.1093/genetics/143.2.973;
RA Glazebrook J., Rogers E.E., Ausubel F.M.;
RT "Isolation of Arabidopsis mutants with enhanced disease susceptibility by
RT direct screening.";
RL Genetics 143:973-982(1996).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF ASP-258.
RX PubMed=10634910; DOI=10.2307/3871032;
RA Vernoux T., Wilson R.C., Seeley K.A., Reichheld J.-P., Muroy S., Brown S.,
RA Maughan S.C., Cobbett C.S., Van Montagu M., Inze D., May M.J., Sung Z.R.;
RT "The ROOT MERISTEMLESS1/CADMIUM SENSITIVE2 gene defines a glutathione-
RT dependent pathway involved in initiation and maintenance of cell division
RT during postembryonic root development.";
RL Plant Cell 12:97-110(2000).
RN [13]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10995473; DOI=10.1073/pnas.190334497;
RA Gutierrez-Alcala G., Gotor C., Meyer A.J., Fricker M., Vega J.M.,
RA Romero L.C.;
RT "Glutathione biosynthesis in Arabidopsis trichome cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11108-11113(2000).
RN [14]
RP FUNCTION.
RX PubMed=11722772; DOI=10.1046/j.1365-313x.2001.01148.x;
RA Roetschi A., Si-Ammour A., Belbahri L., Mauch F., Mauch-Mani B.;
RT "Characterization of an Arabidopsis-Phytophthora pathosystem: resistance
RT requires a functional PAD2 gene and is independent of salicylic acid,
RT ethylene and jasmonic acid signalling.";
RL Plant J. 28:293-305(2001).
RN [15]
RP FUNCTION.
RX PubMed=11402187; DOI=10.1104/pp.126.2.564;
RA Xiang C., Werner B.L., Christensen E.M., Oliver D.J.;
RT "The biological functions of glutathione revisited in arabidopsis
RT transgenic plants with altered glutathione levels.";
RL Plant Physiol. 126:564-574(2001).
RN [16]
RP FUNCTION.
RX PubMed=12848825; DOI=10.1046/j.1365-313x.2003.01794.x;
RA Ferrari S., Plotnikova J.M., De Lorenzo G., Ausubel F.M.;
RT "Arabidopsis local resistance to Botrytis cinerea involves salicylic acid
RT and camalexin and requires EDS4 and PAD2, but not SID2, EDS5 or PAD4.";
RL Plant J. 35:193-205(2003).
RN [17]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP PATHWAY, AND SUBUNIT.
RX PubMed=15180996; DOI=10.1074/jbc.m405127200;
RA Jez J.M., Cahoon R.E., Chen S.;
RT "Arabidopsis thaliana glutamate-cysteine ligase: functional properties,
RT kinetic mechanism, and regulation of activity.";
RL J. Biol. Chem. 279:33463-33470(2004).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF ARG-228.
RX PubMed=15308753; DOI=10.1105/tpc.104.022608;
RA Ball L., Accotto G.-P., Bechtold U., Creissen G., Funck D., Jimenez A.,
RA Kular B., Leyland N., Mejia-Carranza J., Reynolds H., Karpinski S.,
RA Mullineaux P.M.;
RT "Evidence for a direct link between glutathione biosynthesis and stress
RT defense gene expression in Arabidopsis.";
RL Plant Cell 16:2448-2462(2004).
RN [19]
RP FUNCTION.
RX PubMed=14749480; DOI=10.1093/pcp/pch008;
RA Ogawa K., Hatano-Iwasaki A., Yanagida M., Iwabuchi M.;
RT "Level of glutathione is regulated by ATP-dependent ligation of glutamate
RT and cysteine through photosynthesis in Arabidopsis thaliana: mechanism of
RT strong interaction of light intensity with flowering.";
RL Plant Cell Physiol. 45:1-8(2004).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=15610346; DOI=10.1111/j.1365-313x.2004.02269.x;
RA Wachter A., Wolf S., Steininger H., Bogs J., Rausch T.;
RT "Differential targeting of GSH1 and GSH2 is achieved by multiple
RT transcription initiation: implications for the compartmentation of
RT glutathione biosynthesis in the Brassicaceae.";
RL Plant J. 41:15-30(2005).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16531482; DOI=10.1104/pp.106.077982;
RA Cairns N.G., Pasternak M., Wachter A., Cobbett C.S., Meyer A.J.;
RT "Maturation of Arabidopsis seeds is dependent on glutathione biosynthesis
RT within the embryo.";
RL Plant Physiol. 141:446-455(2006).
RN [22]
RP INDUCTION BY CADMIUM.
RC STRAIN=cv. Columbia;
RX PubMed=16502469; DOI=10.1002/pmic.200500543;
RA Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
RA Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C.,
RA Ezan E., Garin J., Bourguignon J.;
RT "The early responses of Arabidopsis thaliana cells to cadmium exposure
RT explored by protein and metabolite profiling analyses.";
RL Proteomics 6:2180-2198(2006).
RN [23]
RP DISULFIDE BONDS, AND MUTAGENESIS OF CYS-186; CYS-349; CYS-364 AND CYS-406.
RX PubMed=17766407; DOI=10.1105/tpc.107.052597;
RA Hicks L.M., Cahoon R.E., Bonner E.R., Rivard R.S., Sheffield J., Jez J.M.;
RT "Thiol-based regulation of redox-active glutamate-cysteine ligase from
RT Arabidopsis thaliana.";
RL Plant Cell 19:2653-2661(2007).
RN [24]
RP FUNCTION, INDUCTION, AND MUTAGENESIS OF SER-298.
RX PubMed=17144898; DOI=10.1111/j.1365-313x.2006.02938.x;
RA Parisy V., Poinssot B., Owsianowski L., Buchala A., Glazebrook J.,
RA Mauch F.;
RT "Identification of PAD2 as a gamma-glutamylcysteine synthetase highlights
RT the importance of glutathione in disease resistance of Arabidopsis.";
RL Plant J. 49:159-172(2007).
CC -!- FUNCTION: Seems to play an important role in controlling the expression
CC of resistance responses like the regulation of salicylic acid (SA) and
CC phytoalexin (camalexin) production. Involved in resistance to fungal
CC and bacterial pathogens. Required for the regulation of cell
CC proliferation in root apical meristems through the GSH-dependent
CC developmental pathway. Also participates in the detoxification process,
CC the antioxidant response and is essential for embryo development and
CC proper seed maturation. {ECO:0000269|PubMed:10634910,
CC ECO:0000269|PubMed:11402187, ECO:0000269|PubMed:11722772,
CC ECO:0000269|PubMed:12848825, ECO:0000269|PubMed:14749480,
CC ECO:0000269|PubMed:15308753, ECO:0000269|PubMed:16531482,
CC ECO:0000269|PubMed:17144898, ECO:0000269|PubMed:7724670,
CC ECO:0000269|PubMed:7770518, ECO:0000269|PubMed:8090752,
CC ECO:0000269|PubMed:8725243}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC Evidence={ECO:0000269|PubMed:15180996};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13286;
CC Evidence={ECO:0000269|PubMed:15180996};
CC -!- ACTIVITY REGULATION: Feedback inhibition by glutathione. Inhibited by
CC buthionine sulfoximine and cystamine. {ECO:0000269|PubMed:15180996}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.1 mM for glutamate {ECO:0000269|PubMed:15180996};
CC KM=1.6 mM for cysteine {ECO:0000269|PubMed:15180996};
CC KM=2.7 mM for ATP {ECO:0000269|PubMed:15180996};
CC Vmax=120 nmol/min/mg enzyme {ECO:0000269|PubMed:15180996};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000269|PubMed:15180996}.
CC -!- SUBUNIT: Homodimer or monomer when oxidized or reduced, respectively.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15610346}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P46309-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Abundant in leaves and roots. Expressed to a high
CC level in leaf trichomes of mature plant. {ECO:0000269|PubMed:10995473}.
CC -!- INDUCTION: Down-regulated in leaf trichomes under salt treatment. Up-
CC regulated by the fungal pathogen Phytophthora porri. Induced by cadmium
CC (PubMed:16502469). {ECO:0000269|PubMed:10995473,
CC ECO:0000269|PubMed:16502469, ECO:0000269|PubMed:17144898}.
CC -!- PTM: The Cys-186-Cys-406 disulfide bridge is known to modulate the
CC enzyme activity according to the redox status. The oxidized form
CC constitutes the active enzyme.
CC -!- DISRUPTION PHENOTYPE: Plants are characterized by a recessive embryo-
CC lethal phenotype. {ECO:0000269|PubMed:16531482}.
CC -!- SIMILARITY: Belongs to the carboxylate-amine ligase family. Glutamate--
CC cysteine ligase type 2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82626.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z29490; CAA82626.1; ALT_FRAME; mRNA.
DR EMBL; Y09944; CAA71075.1; -; mRNA.
DR EMBL; AF068299; AAD14544.1; -; Genomic_DNA.
DR EMBL; DQ993178; ABJ98542.1; -; mRNA.
DR EMBL; AL031018; CAA19826.1; -; Genomic_DNA.
DR EMBL; AL161558; CAB79265.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84706.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84708.1; -; Genomic_DNA.
DR EMBL; AF419576; AAL31908.1; -; mRNA.
DR EMBL; AF428393; AAL16161.1; -; mRNA.
DR EMBL; AY056372; AAL08228.1; -; mRNA.
DR EMBL; AY143970; AAN28909.1; -; mRNA.
DR PIR; T05142; T05142.
DR RefSeq; NP_001190808.1; NM_001203879.2. [P46309-1]
DR RefSeq; NP_194041.1; NM_118439.4. [P46309-1]
DR AlphaFoldDB; P46309; -.
DR SMR; P46309; -.
DR BioGRID; 13698; 11.
DR STRING; 3702.AT4G23100.3; -.
DR MetOSite; P46309; -.
DR PaxDb; P46309; -.
DR PRIDE; P46309; -.
DR ProteomicsDB; 248493; -. [P46309-1]
DR EnsemblPlants; AT4G23100.1; AT4G23100.1; AT4G23100. [P46309-1]
DR EnsemblPlants; AT4G23100.3; AT4G23100.3; AT4G23100. [P46309-1]
DR GeneID; 828409; -.
DR Gramene; AT4G23100.1; AT4G23100.1; AT4G23100. [P46309-1]
DR Gramene; AT4G23100.3; AT4G23100.3; AT4G23100. [P46309-1]
DR KEGG; ath:AT4G23100; -.
DR Araport; AT4G23100; -.
DR TAIR; locus:2127173; AT4G23100.
DR eggNOG; ENOG502QVEN; Eukaryota.
DR HOGENOM; CLU_026610_0_0_1; -.
DR InParanoid; P46309; -.
DR OMA; DYVEWAL; -.
DR OrthoDB; 397529at2759; -.
DR PhylomeDB; P46309; -.
DR BioCyc; ARA:AT4G23100-MON; -.
DR BioCyc; MetaCyc:AT4G23100-MON; -.
DR BRENDA; 6.3.2.2; 399.
DR SABIO-RK; P46309; -.
DR UniPathway; UPA00142; UER00209.
DR PRO; PR:P46309; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P46309; baseline and differential.
DR Genevisible; P46309; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IDA:TAIR.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0002213; P:defense response to insect; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:0006750; P:glutathione biosynthetic process; IDA:TAIR.
DR GO; GO:0009700; P:indole phytoalexin biosynthetic process; IMP:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
DR InterPro; IPR035434; GCL_bact_plant.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR011556; Glut_cys_lig_pln_type.
DR PANTHER; PTHR34378; PTHR34378; 1.
DR Pfam; PF04107; GCS2; 1.
DR PIRSF; PIRSF017901; GCL; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR01436; glu_cys_lig_pln; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chloroplast; Disulfide bond;
KW Glutathione biosynthesis; Ligase; Nucleotide-binding; Plant defense;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..522
FT /note="Glutamate--cysteine ligase, chloroplastic"
FT /id="PRO_0000013054"
FT DISULFID 186..406
FT /evidence="ECO:0000269|PubMed:17766407"
FT DISULFID 349..364
FT /evidence="ECO:0000269|PubMed:17766407"
FT VARIANT 22
FT /note="A -> T (in strain: cv. Landsberg erecta and cv.
FT Sha)"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.4"
FT VARIANT 48
FT /note="Y -> N (in strain: cv. Landsberg erecta)"
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 186
FT /note="C->S: 20-fold decreased activity. Abrogates the
FT response to changes in redox environment."
FT /evidence="ECO:0000269|PubMed:17766407"
FT MUTAGEN 228
FT /note="R->K: In rax1-1; reduced GSH level. Up-regulates APX
FT activity."
FT /evidence="ECO:0000269|PubMed:15308753"
FT MUTAGEN 237..239
FT /note="PKV->L: In cad2-1; reduced GSH level. Cadmium-
FT sensitive."
FT /evidence="ECO:0000269|PubMed:7770518"
FT MUTAGEN 258
FT /note="D->N: In rml1; GSH defective. Enhanced
FT susceptibility to P.syringae."
FT /evidence="ECO:0000269|PubMed:10634910"
FT MUTAGEN 298
FT /note="S->N: In pad2-1; reduced GSH level. Camalexin
FT defective. Enhanced susceptibility to P.porri."
FT /evidence="ECO:0000269|PubMed:17144898"
FT MUTAGEN 349
FT /note="C->S: 2-fold decreased activity."
FT /evidence="ECO:0000269|PubMed:17766407"
FT MUTAGEN 364
FT /note="C->S: 2-fold decreased activity."
FT /evidence="ECO:0000269|PubMed:17766407"
FT MUTAGEN 406
FT /note="C->S: 20-fold decreased activity. Abrogates the
FT response to changes in redox environment."
FT /evidence="ECO:0000269|PubMed:17766407"
FT CONFLICT 355..356
FT /note="RQ -> SA (in Ref. 7; AAL16161)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="V -> L (in Ref. 7; AAL08228)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="T -> S (in Ref. 4; ABJ98542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 58562 MW; CCBF13C6F44E0EF7 CRC64;
MALLSQAGGS YTVVPSGVCS KAGTKAVVSG GVRNLDVLRM KEAFGSSYSR SLSTKSMLLH
SVKRSKRGHQ LIVAASPPTE EAVVATEPLT REDLIAYLAS GCKTKDKYRI GTEHEKFGFE
VNTLRPMKYD QIAELLNGIA ERFEWEKVME GDKIIGLKQG KQSISLEPGG QFELSGAPLE
TLHQTCAEVN SHLYQVKAVA EEMGIGFLGI GFQPKWRRED IPIMPKGRYD IMRNYMPKVG
TLGLDMMLRT CTVQVNLDFS SEADMIRKFR AGLALQPIAT ALFANSPFTE GKPNGFLSMR
SHIWTDTDKD RTGMLPFVFD DSFGFEQYVD YALDVPMYFA YRKNKYIDCT GMTFRQFLAG
KLPCLPGELP SYNDWENHLT TIFPEVRLKR YLEMRGADGG PWRRLCALPA FWVGLLYDDD
SLQAILDLTA DWTPAEREML RNKVPVTGLK TPFRDGLLKH VAEDVLKLAK DGLERRGYKE
AGFLNAVDEV VRTGVTPAEK LLEMYNGEWG QSVDPVFEEL LY
