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Glutamate--cysteine ligase, chloroplastic (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase) (Protein ROOT MERISTEMLESS 1) (AtGCL) (Protein cadmium-sensitive 2) (Protein phytoalexin-deficient 2)

 GSH1_ARATH              Reviewed;         522 AA.
P46309; A0FGQ9; O82759; P92951; Q93ZQ6; Q944I8;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
25-OCT-2017, entry version 129.
RecName: Full=Glutamate--cysteine ligase, chloroplastic;
EC=6.3.2.2;
AltName: Full=Gamma-ECS;
Short=GCS;
AltName: Full=Gamma-glutamylcysteine synthetase;
AltName: Full=Protein ROOT MERISTEMLESS 1;
Short=AtGCL;
AltName: Full=Protein cadmium-sensitive 2;
AltName: Full=Protein phytoalexin-deficient 2;
Flags: Precursor;
Name=GSH1; Synonyms=CAD2, GCL, PAD2, RML1;
OrderedLocusNames=At4g23100; ORFNames=F7H19.290;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=7937837; DOI=10.1073/pnas.91.21.10059;
May M.J., Leaver C.J.;
"Arabidopsis thaliana gamma-glutamylcysteine synthetase is
structurally unrelated to mammalian, yeast, and Escherichia coli
homologs.";
Proc. Natl. Acad. Sci. U.S.A. 91:10059-10063(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-22, AND VARIANT ASN-48.
STRAIN=cv. Landsberg erecta;
Ullmann P., Gondet L., Bach T.J.;
"Isolation of an Aribidopsis thaliana cDNA encoding a putative gamma-
glutamylcysteine synthetase by complementation of a GSHI deficient
yeast mutant-glutamylcysteine synthetase.";
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9807829; DOI=10.1046/j.1365-313x.1998.00262.x;
Cobbett C.S., May M.J., Howden R., Rolls B.;
"The glutathione-deficient, cadmium-sensitive mutant, cad2-1, of
Arabidopsis thaliana is deficient in gamma-glutamylcysteine
synthetase.";
Plant J. 16:73-78(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-22.
STRAIN=cv. Sha;
Kopriva S., Mullineaux P.M.;
"Glutathione synthesis in Arabidopsis ecotypes.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[6]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[8]
FUNCTION.
PubMed=8090752; DOI=10.1073/pnas.91.19.8955;
Glazebrook J., Ausubel F.M.;
"Isolation of phytoalexin-deficient mutants of Arabidopsis thaliana
and characterization of their interactions with bacterial pathogens.";
Proc. Natl. Acad. Sci. U.S.A. 91:8955-8959(1994).
[9]
FUNCTION.
PubMed=7724670; DOI=10.1104/pp.107.2.365;
Cheng J.-C., Seeley K.A., Sung Z.R.;
"RML1 and RML2, Arabidopsis genes required for cell proliferation at
the root tip.";
Plant Physiol. 107:365-376(1995).
[10]
FUNCTION, AND MUTAGENESIS OF 237-PRO--VAL-239.
PubMed=7770518; DOI=10.1104/pp.107.4.1067;
Howden R., Andersen C.R., Goldsbrough P.B., Cobbett C.S.;
"A cadmium-sensitive, glutathione-deficient mutant of Arabidopsis
thaliana.";
Plant Physiol. 107:1067-1073(1995).
[11]
FUNCTION.
PubMed=8725243;
Glazebrook J., Rogers E.E., Ausubel F.M.;
"Isolation of Arabidopsis mutants with enhanced disease susceptibility
by direct screening.";
Genetics 143:973-982(1996).
[12]
FUNCTION, AND MUTAGENESIS OF ASP-258.
PubMed=10634910; DOI=10.1105/tpc.12.1.97;
Vernoux T., Wilson R.C., Seeley K.A., Reichheld J.-P., Muroy S.,
Brown S., Maughan S.C., Cobbett C.S., Van Montagu M., Inze D.,
May M.J., Sung Z.R.;
"The ROOT MERISTEMLESS1/CADMIUM SENSITIVE2 gene defines a glutathione-
dependent pathway involved in initiation and maintenance of cell
division during postembryonic root development.";
Plant Cell 12:97-110(2000).
[13]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=10995473; DOI=10.1073/pnas.190334497;
Gutierrez-Alcala G., Gotor C., Meyer A.J., Fricker M., Vega J.M.,
Romero L.C.;
"Glutathione biosynthesis in Arabidopsis trichome cells.";
Proc. Natl. Acad. Sci. U.S.A. 97:11108-11113(2000).
[14]
FUNCTION.
PubMed=11722772; DOI=10.1046/j.1365-313X.2001.01148.x;
Roetschi A., Si-Ammour A., Belbahri L., Mauch F., Mauch-Mani B.;
"Characterization of an Arabidopsis-Phytophthora pathosystem:
resistance requires a functional PAD2 gene and is independent of
salicylic acid, ethylene and jasmonic acid signalling.";
Plant J. 28:293-305(2001).
[15]
FUNCTION.
PubMed=11402187; DOI=10.1104/pp.126.2.564;
Xiang C., Werner B.L., Christensen E.M., Oliver D.J.;
"The biological functions of glutathione revisited in arabidopsis
transgenic plants with altered glutathione levels.";
Plant Physiol. 126:564-574(2001).
[16]
FUNCTION.
PubMed=12848825; DOI=10.1046/j.1365-313X.2003.01794.x;
Ferrari S., Plotnikova J.M., De Lorenzo G., Ausubel F.M.;
"Arabidopsis local resistance to Botrytis cinerea involves salicylic
acid and camalexin and requires EDS4 and PAD2, but not SID2, EDS5 or
PAD4.";
Plant J. 35:193-205(2003).
[17]
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND SUBUNIT.
PubMed=15180996; DOI=10.1074/jbc.M405127200;
Jez J.M., Cahoon R.E., Chen S.;
"Arabidopsis thaliana glutamate-cysteine ligase: functional
properties, kinetic mechanism, and regulation of activity.";
J. Biol. Chem. 279:33463-33470(2004).
[18]
FUNCTION, AND MUTAGENESIS OF ARG-228.
PubMed=15308753; DOI=10.1105/tpc.104.022608;
Ball L., Accotto G.-P., Bechtold U., Creissen G., Funck D.,
Jimenez A., Kular B., Leyland N., Mejia-Carranza J., Reynolds H.,
Karpinski S., Mullineaux P.M.;
"Evidence for a direct link between glutathione biosynthesis and
stress defense gene expression in Arabidopsis.";
Plant Cell 16:2448-2462(2004).
[19]
FUNCTION.
PubMed=14749480; DOI=10.1093/pcp/pch008;
Ogawa K., Hatano-Iwasaki A., Yanagida M., Iwabuchi M.;
"Level of glutathione is regulated by ATP-dependent ligation of
glutamate and cysteine through photosynthesis in Arabidopsis thaliana:
mechanism of strong interaction of light intensity with flowering.";
Plant Cell Physiol. 45:1-8(2004).
[20]
SUBCELLULAR LOCATION.
PubMed=15610346; DOI=10.1111/j.1365-313X.2004.02269.x;
Wachter A., Wolf S., Steininger H., Bogs J., Rausch T.;
"Differential targeting of GSH1 and GSH2 is achieved by multiple
transcription initiation: implications for the compartmentation of
glutathione biosynthesis in the Brassicaceae.";
Plant J. 41:15-30(2005).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16531482; DOI=10.1104/pp.106.077982;
Cairns N.G., Pasternak M., Wachter A., Cobbett C.S., Meyer A.J.;
"Maturation of Arabidopsis seeds is dependent on glutathione
biosynthesis within the embryo.";
Plant Physiol. 141:446-455(2006).
[22]
DISULFIDE BONDS, AND MUTAGENESIS OF CYS-186; CYS-349; CYS-364 AND
CYS-406.
PubMed=17766407; DOI=10.1105/tpc.107.052597;
Hicks L.M., Cahoon R.E., Bonner E.R., Rivard R.S., Sheffield J.,
Jez J.M.;
"Thiol-based regulation of redox-active glutamate-cysteine ligase from
Arabidopsis thaliana.";
Plant Cell 19:2653-2661(2007).
[23]
FUNCTION, INDUCTION, AND MUTAGENESIS OF SER-298.
PubMed=17144898; DOI=10.1111/j.1365-313X.2006.02938.x;
Parisy V., Poinssot B., Owsianowski L., Buchala A., Glazebrook J.,
Mauch F.;
"Identification of PAD2 as a gamma-glutamylcysteine synthetase
highlights the importance of glutathione in disease resistance of
Arabidopsis.";
Plant J. 49:159-172(2007).
-!- FUNCTION: Seems to play an important role in controlling the
expression of resistance responses like the regulation of
salicylic acid (SA) and phytoalexin (camalexin) production.
Involved in resistance to fungal and bacterial pathogens. Required
for the regulation of cell proliferation in root apical meristems
through the GSH-dependent developmental pathway. Also participates
in the detoxification process, the antioxidant response and is
essential for embryo development and proper seed maturation.
{ECO:0000269|PubMed:10634910, ECO:0000269|PubMed:11402187,
ECO:0000269|PubMed:11722772, ECO:0000269|PubMed:12848825,
ECO:0000269|PubMed:14749480, ECO:0000269|PubMed:15308753,
ECO:0000269|PubMed:16531482, ECO:0000269|PubMed:17144898,
ECO:0000269|PubMed:7724670, ECO:0000269|PubMed:7770518,
ECO:0000269|PubMed:8090752, ECO:0000269|PubMed:8725243}.
-!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP +
phosphate + gamma-L-glutamyl-L-cysteine.
-!- ENZYME REGULATION: Feedback inhibition by glutathione. Inhibited
by buthionine sulfoximine and cystamine.
{ECO:0000269|PubMed:15180996}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=9.1 mM for glutamate {ECO:0000269|PubMed:15180996};
KM=1.6 mM for cysteine {ECO:0000269|PubMed:15180996};
KM=2.7 mM for ATP {ECO:0000269|PubMed:15180996};
Vmax=120 nmol/min/mg enzyme {ECO:0000269|PubMed:15180996};
-!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
from L-cysteine and L-glutamate: step 1/2.
-!- SUBUNIT: Homodimer or monomer when oxidized or reduced,
respectively. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:15610346}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=P46309-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Abundant in leaves and roots. Expressed to a
high level in leaf trichomes of mature plant.
{ECO:0000269|PubMed:10995473}.
-!- INDUCTION: Down-regulated in leaf trichomes under salt treatment.
Up-regulated by the fungal pathogen Phytophthora porri.
{ECO:0000269|PubMed:10995473, ECO:0000269|PubMed:17144898}.
-!- PTM: The Cys-186-Cys-406 disulfide bridge is known to modulate the
enzyme activity according to the redox status. The oxidized form
constitutes the active enzyme.
-!- DISRUPTION PHENOTYPE: Plants are characterized by a recessive
embryo-lethal phenotype. {ECO:0000269|PubMed:16531482}.
-!- SIMILARITY: Belongs to the carboxylate-amine ligase family.
Glutamate--cysteine ligase type 2 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA82626.1; Type=Frameshift; Positions=490; Evidence={ECO:0000305};
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EMBL; Z29490; CAA82626.1; ALT_FRAME; mRNA.
EMBL; Y09944; CAA71075.1; -; mRNA.
EMBL; AF068299; AAD14544.1; -; Genomic_DNA.
EMBL; DQ993178; ABJ98542.1; -; mRNA.
EMBL; AL031018; CAA19826.1; -; Genomic_DNA.
EMBL; AL161558; CAB79265.1; -; Genomic_DNA.
EMBL; CP002687; AEE84706.1; -; Genomic_DNA.
EMBL; CP002687; AEE84708.1; -; Genomic_DNA.
EMBL; AF419576; AAL31908.1; -; mRNA.
EMBL; AF428393; AAL16161.1; -; mRNA.
EMBL; AY056372; AAL08228.1; -; mRNA.
EMBL; AY143970; AAN28909.1; -; mRNA.
PIR; T05142; T05142.
RefSeq; NP_001190808.1; NM_001203879.2. [P46309-1]
RefSeq; NP_194041.1; NM_118439.4. [P46309-1]
UniGene; At.25074; -.
ProteinModelPortal; P46309; -.
SMR; P46309; -.
BioGrid; 13698; 1.
STRING; 3702.AT4G23100.1; -.
PaxDb; P46309; -.
PRIDE; P46309; -.
EnsemblPlants; AT4G23100.1; AT4G23100.1; AT4G23100. [P46309-1]
EnsemblPlants; AT4G23100.3; AT4G23100.3; AT4G23100. [P46309-1]
GeneID; 828409; -.
Gramene; AT4G23100.1; AT4G23100.1; AT4G23100.
Gramene; AT4G23100.3; AT4G23100.3; AT4G23100.
KEGG; ath:AT4G23100; -.
Araport; AT4G23100; -.
TAIR; locus:2127173; AT4G23100.
eggNOG; ENOG410IK1F; Eukaryota.
eggNOG; COG3572; LUCA.
HOGENOM; HOG000009857; -.
InParanoid; P46309; -.
KO; K01919; -.
OMA; DYVEWAL; -.
OrthoDB; EOG093606AY; -.
PhylomeDB; P46309; -.
BioCyc; ARA:AT4G23100-MONOMER; -.
BioCyc; MetaCyc:AT4G23100-MONOMER; -.
BRENDA; 6.3.2.2; 399.
SABIO-RK; P46309; -.
UniPathway; UPA00142; UER00209.
PRO; PR:P46309; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P46309; baseline and differential.
Genevisible; P46309; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004357; F:glutamate-cysteine ligase activity; IDA:TAIR.
GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0009816; P:defense response to bacterium, incompatible interaction; IMP:TAIR.
GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
GO; GO:0002213; P:defense response to insect; IMP:TAIR.
GO; GO:0009908; P:flower development; IMP:TAIR.
GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
GO; GO:0006750; P:glutathione biosynthetic process; IDA:TAIR.
GO; GO:0009700; P:indole phytoalexin biosynthetic process; IMP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IMP:TAIR.
GO; GO:0009408; P:response to heat; IMP:TAIR.
GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
GO; GO:0010193; P:response to ozone; IEP:TAIR.
InterPro; IPR035434; GCL_bact_plant.
InterPro; IPR006336; GCS2.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
InterPro; IPR011556; Glut_cys_lig_pln_type.
PANTHER; PTHR34378:SF1; PTHR34378:SF1; 1.
Pfam; PF04107; GCS2; 1.
PIRSF; PIRSF017901; GCL; 1.
SUPFAM; SSF55931; SSF55931; 2.
TIGRFAMs; TIGR01436; glu_cys_lig_pln; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Chloroplast; Complete proteome;
Disulfide bond; Glutathione biosynthesis; Ligase; Nucleotide-binding;
Plant defense; Plastid; Reference proteome; Transit peptide.
TRANSIT 1 ? Chloroplast. {ECO:0000255}.
CHAIN ? 522 Glutamate--cysteine ligase,
chloroplastic.
/FTId=PRO_0000013054.
DISULFID 186 406 {ECO:0000269|PubMed:17766407}.
DISULFID 349 364 {ECO:0000269|PubMed:17766407}.
VARIANT 22 22 A -> T (in strain: cv. Landsberg erecta
and cv. Sha). {ECO:0000269|Ref.2,
ECO:0000269|Ref.4}.
VARIANT 48 48 Y -> N (in strain: cv. Landsberg erecta).
{ECO:0000269|Ref.2}.
MUTAGEN 186 186 C->S: 20-fold decreased activity.
Abrogates the response to changes in
redox environment.
{ECO:0000269|PubMed:17766407}.
MUTAGEN 228 228 R->K: In rax1-1; reduced GSH level. Up-
regulates APX activity.
{ECO:0000269|PubMed:15308753}.
MUTAGEN 237 239 PKV->L: In cad2-1; reduced GSH level.
Cadmium-sensitive.
{ECO:0000269|PubMed:7770518}.
MUTAGEN 258 258 D->N: In rml1; GSH defective. Enhanced
susceptibility to P.syringae.
{ECO:0000269|PubMed:10634910}.
MUTAGEN 298 298 S->N: In pad2-1; reduced GSH level.
Camalexin defective. Enhanced
susceptibility to P.porri.
{ECO:0000269|PubMed:17144898}.
MUTAGEN 349 349 C->S: 2-fold decreased activity.
{ECO:0000269|PubMed:17766407}.
MUTAGEN 364 364 C->S: 2-fold decreased activity.
{ECO:0000269|PubMed:17766407}.
MUTAGEN 406 406 C->S: 20-fold decreased activity.
Abrogates the response to changes in
redox environment.
{ECO:0000269|PubMed:17766407}.
CONFLICT 355 356 RQ -> SA (in Ref. 7; AAL16161).
{ECO:0000305}.
CONFLICT 413 413 V -> L (in Ref. 7; AAL08228).
{ECO:0000305}.
CONFLICT 493 493 T -> S (in Ref. 4; ABJ98542).
{ECO:0000305}.
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


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