ID   GSH1_MEDTR              Reviewed;         508 AA.
AC   Q9ZNX6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 111.
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   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10694062; DOI=10.1080/10715769900301531;
RA   Frendo P., Mathieu C., Van de Sype G., Herouart D., Puppo A.;
RT   "Characterisation of a cDNA encoding gamma-glutamylcysteine synthetase in
RT   Medicago truncatula.";
RL   Free Radic. Res. 31:S213-S218(1999).
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-172-Cys-392 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}.
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DR   EMBL; AF041340; AAC82334.1; -; mRNA.
DR   RefSeq; XP_003630512.1; XM_003630464.2.
DR   AlphaFoldDB; Q9ZNX6; -.
DR   SMR; Q9ZNX6; -.
DR   STRING; 3880.AET04988; -.
DR   PRIDE; Q9ZNX6; -.
DR   EnsemblPlants; AET04988; AET04988; MTR_8g098350.
DR   GeneID; 11441054; -.
DR   Gramene; AET04988; AET04988; MTR_8g098350.
DR   eggNOG; ENOG502QVEN; Eukaryota.
DR   HOGENOM; CLU_026610_0_0_1; -.
DR   OMA; DYVEWAL; -.
DR   OrthoDB; 397529at2759; -.
DR   UniPathway; UPA00142; UER00209.
DR   ExpressionAtlas; Q9ZNX6; 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:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniPathway.
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; Transit peptide.
FT   TRANSIT         1..59
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           60..508
FT                   /note="Glutamate--cysteine ligase, chloroplastic"
FT                   /id="PRO_0000013057"
FT   DISULFID        172..392
FT                   /evidence="ECO:0000250"
FT   DISULFID        335..350
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   508 AA;  57677 MW;  28C67950D3EC1A5A CRC64;
     MTTIFRLASS SSPSLRHDAT PHNFHIRKTS ISNTFSFSSK NSLSFKRILT SGGSRRFIVA
     ASPPTEDAVV ATEPLTKQDL IDYLASGCKT KDKWRIGTEH EKFGFELGSL RPMKYEQISE
     LLNGIAERFD WDKVMEGDNI IGLKQGKQSI SLEPGGQFEL SGAPLETLHQ TCAEVNSHLY
     QVKAVAEEMG IGFLGIGFQP KWERKDIPMM PKGRYEIMKK YMPKVGSLGL DMMFRTCTVQ
     VNLDFSSEAD MIRKFRAGLA LQPIATALFA NSPFTDGKPN GFVSMRSHIW TDTDKDRTGM
     LPFVFDDSFG FEQYVDFALD VPMYFVYRKK KYIDCTGMTF RDFLAGKLPC IPGELPTLND
     WENHLTTIFP EVRLKRYLEM RGADGGPWRR LCALPAFWVG ILYDEVSLQR VLDMTADWTL
     EEREMLRNKV TVTGLKTPFR DGLLKHVAEE VLELAKDGLE RRGFKESGFL NAVAEVVRTG
     VTPAERLLEL YHGKWEQSVD HVFDELLY