ID   GSH1_SOLLC              Reviewed;         523 AA.
AC   O22493;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
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;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ohio state 4;
RA   Kovari I.A., Goldsbrough P.B.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- PTM: The Cys-187-Cys-407 disulfide bridge is known to modulate the
CC       enzyme activity according to the redox status. The oxidized form
CC       constitutes the active enzyme (By similarity). {ECO:0000250}.
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; AF017983; AAB71230.1; -; mRNA.
DR   PIR; T04332; T04332.
DR   RefSeq; NP_001234010.2; NM_001247081.2.
DR   AlphaFoldDB; O22493; -.
DR   SMR; O22493; -.
DR   STRING; 4081.Solyc08g081010.2.1; -.
DR   PaxDb; O22493; -.
DR   PRIDE; O22493; -.
DR   GeneID; 543536; -.
DR   KEGG; sly:543536; -.
DR   eggNOG; ENOG502QVEN; Eukaryota.
DR   InParanoid; O22493; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; O22493; baseline and differential.
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:0052544; P:defense response by callose deposition in cell wall; IEA:EnsemblPlants.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR   GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR   GO; GO:0002213; P:defense response to insect; IEA:EnsemblPlants.
DR   GO; GO:0009908; P:flower development; IEA:EnsemblPlants.
DR   GO; GO:0019761; P:glucosinolate biosynthetic process; IEA:EnsemblPlants.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009700; P:indole phytoalexin biosynthetic process; IEA:EnsemblPlants.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR   GO; GO:0009753; P:response to jasmonic acid; IEA:EnsemblPlants.
DR   GO; GO:0010193; P:response to ozone; IEA:EnsemblPlants.
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   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Disulfide bond; Glutathione biosynthesis; Ligase;
KW   Nucleotide-binding; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..523
FT                   /note="Glutamate--cysteine ligase, chloroplastic"
FT                   /id="PRO_0000013056"
FT   DISULFID        187..407
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   523 AA;  59057 MW;  4085500731066C1A CRC64;
     MALMSQAGSS HCIYSEKVRC ISGHRSIINN MDMFRMREIC FGVDISSRNA SRRVQGNYLN
     HIGVGSRRGD LTIVAASPPT EDAVVAAEPL TKEDLVGYLA SGCKSKEKWR IGTEHEKFGF
     EFGTLRPMKY DQIADLLNGI AERFDWEKVM EGDKIIGLKQ GKQSISLEPG GQFELSGAPL
     ETLHQTCAEV NSHLYQVKAV AEEMGIGFLG TGFQPKWGLK DIPIMPKGRY EIIRNYMPKV
     GSLGLDMMFR TCTVQVNLDF SSEADMIRKF RAGLALQPIA TALFANSPFT EGKPNGYLSK
     RSHIWTDTDN NRAGMLPFVF DDSFGFEQYV DYALDVPMYF VYRKKKYVDC TGLSFRDFMN
     GKLPPIPGEY PTLNDWENHL TTIFPEVRLK RYLEMRGADG GPWRRLCALP AFWVGILYDE
     GSLQSVLDMT FDWTAEERDM LRNKVPKSGL KTPFRDGLLM HVAQDVVKLA KEGLERRGFK
     ETGFLNEVAE VVKTGVTPAE KLLELYHGKW GQSVDPIFEE LLY