GSH1_BRAJU
ID GSH1_BRAJU Reviewed; 514 AA.
AC O23736; Q43389; Q546C7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Glutamate--cysteine ligase, chloroplastic;
DE EC=6.3.2.2;
DE AltName: Full=Gamma-ECS;
DE Short=GCS;
DE AltName: Full=Gamma-glutamylcysteine synthetase;
DE Flags: Precursor;
GN Name=GSH1; Synonyms=ECS1;
OS Brassica juncea (Indian mustard) (Sinapis juncea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RC STRAIN=cv. Vittasso; TISSUE=Root;
RX PubMed=9620267; DOI=10.1023/a:1005929022061;
RA Schaefer H.J., Haag-Kerwer A., Rausch T.H.;
RT "cDNA cloning and expression analysis of genes encoding GSH synthesis in
RT roots of the heavy-metal accumulator Brassica juncea L.: evidence for Cd-
RT induction of a putative mitochondrial gamma-glutamylcysteine synthetase
RT isoform.";
RL Plant Mol. Biol. 37:87-97(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wachter A., Steininger H., Rausch T., Bogs J.;
RT "Compartmentation of GSH synthesis in plants: in Arabidopsis thaliana and
RT in Brassica juncea, gamma-glutamylcysteine synthetase (GSH1), the key
RT enzyme of glutathione synthesis, is exclusively localized in plastids.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 126-342, FUNCTION, AND INDUCTION.
RC STRAIN=cv. Vittasso; TISSUE=Leaf;
RX PubMed=9119067; DOI=10.1016/s0014-5793(97)00132-4;
RA Schaefer H.J., Greiner S., Rausch T., Haag-Kerwer A.;
RT "In seedlings of the heavy metal accumulator Brassica juncea, Cu(2+)
RT differentially affects transcript amounts for gamma-glutamylcysteine
RT synthetase (gamma-ECS) and metallothionein (MT2).";
RL FEBS Lett. 404:216-220(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 66-514, DISULFIDE BONDS,
RP MUTAGENESIS OF CYS-178; ARG-220; CYS-341 AND CYS-356, AND SUBUNIT.
RX PubMed=16766527; DOI=10.1074/jbc.m602770200;
RA Hothorn M., Wachter A., Gromes R., Stuwe T., Rausch T., Scheffzek K.;
RT "Structural basis for the redox control of plant glutamate cysteine
RT ligase.";
RL J. Biol. Chem. 281:27557-27565(2006).
CC -!- FUNCTION: Participates in the detoxification process.
CC {ECO:0000269|PubMed:9119067, ECO:0000269|PubMed:9620267}.
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 -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2.
CC -!- SUBUNIT: Homodimer or monomer when oxidized or reduced, respectively.
CC {ECO:0000269|PubMed:16766527}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by cadmium and cu(2+).
CC {ECO:0000269|PubMed:9119067, ECO:0000269|PubMed:9620267}.
CC -!- PTM: The Cys-178-Cys-398 disulfide bridge is known to modulate the
CC enzyme activity according to the redox status. The oxidized form
CC constitutes the active enzyme.
CC -!- SIMILARITY: Belongs to the carboxylate-amine ligase family. Glutamate--
CC cysteine ligase type 2 subfamily. {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; Y10848; CAA71801.1; -; mRNA.
DR EMBL; AJ563921; CAD91712.1; -; mRNA.
DR EMBL; X95563; CAA64808.1; -; mRNA.
DR PDB; 2GWC; X-ray; 2.18 A; A/B/C/D/E/F/G/H=66-514.
DR PDB; 2GWD; X-ray; 2.09 A; A=66-514.
DR PDB; 6GMO; X-ray; 1.75 A; A/B=72-514.
DR PDBsum; 2GWC; -.
DR PDBsum; 2GWD; -.
DR PDBsum; 6GMO; -.
DR AlphaFoldDB; O23736; -.
DR SMR; O23736; -.
DR BRENDA; 6.3.2.2; 941.
DR UniPathway; UPA00142; UER00209.
DR EvolutionaryTrace; O23736; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0043436; P:oxoacid metabolic process; IEA:UniProt.
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 3D-structure; ATP-binding; Chloroplast; Disulfide bond;
KW Glutathione biosynthesis; Ligase; Nucleotide-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..514
FT /note="Glutamate--cysteine ligase, chloroplastic"
FT /id="PRO_0000013055"
FT DISULFID 178..398
FT /evidence="ECO:0000269|PubMed:16766527"
FT DISULFID 341..356
FT /evidence="ECO:0000269|PubMed:16766527"
FT MUTAGEN 178
FT /note="C->S: Decreased activity."
FT /evidence="ECO:0000269|PubMed:16766527"
FT MUTAGEN 220
FT /note="R->K: Reduces activity with cysteine as substrate."
FT /evidence="ECO:0000269|PubMed:16766527"
FT MUTAGEN 341
FT /note="C->S: Decreased activity."
FT /evidence="ECO:0000269|PubMed:16766527"
FT MUTAGEN 356
FT /note="C->A: Decreased activity."
FT /evidence="ECO:0000269|PubMed:16766527"
FT CONFLICT 139
FT /note="K -> R (in Ref. 2; CAA64808)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="T -> I (in Ref. 2; CAA64808)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="M -> T (in Ref. 2; CAA64808)"
FT /evidence="ECO:0000305"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 102..112
FT /evidence="ECO:0007829|PDB:6GMO"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 174..192
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 254..274
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:2GWD"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 364..371
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 377..386
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 394..408
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 411..421
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 426..439
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:6GMO"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 450..468
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 473..476
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 477..485
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 489..497
FT /evidence="ECO:0007829|PDB:6GMO"
FT TURN 498..503
FT /evidence="ECO:0007829|PDB:6GMO"
FT HELIX 508..511
FT /evidence="ECO:0007829|PDB:6GMO"
SQ SEQUENCE 514 AA; 57903 MW; 07C71CB13E785FA8 CRC64;
MALLSQAGGA YTVPSGHVSS RTGTKTVSGC VNVLRMKETY VSSYSRTLST KSMLKRSKRG
HQLIVAASPP TEEAVVATEP LTREDLIAYL ASGCKSKEKW RIGTEHEKFG FEVNTLRPMK
YDQIAELLNS IAERFEWEKV MEGDKIIGLK QGKQSISLEP GGQFELSGAP LETLHQTCAE
VNSHLYQVKA VAEEMGIGFL GMGFQPKWRR EDIPTMPKGR YDIMRNYMPK VGSLGLDMML
RTCTVQVNLD FSSEADMIRK FRAGLALQPI ATALFANSPF TEGKPNGFLS MRSHIWTDTD
KDRTGMLPFV FDDSFGFEQY VDYALDVPMY FAYRNGKYVD CTGMTFRQFL AGKLPCLPGE
LPTYNDWENH LTTIFPEVRL KRYMEMRGAD GGPWRRLCAL PAFWVGLLYD EDVLQSVLDL
TADWTPAERE MLRNKVPVTG LKTPFRDGLL KHVAEDVLKL AKDGLERRGY KEVGFLNAVT
EVVRTGVTPA ENLLEMYNGE WGQSVDPVFQ ELLY
