ID   GSH1_PSESY              Reviewed;         535 AA.
AC   P61379;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00578};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00578};
DE            Short=GCS {ECO:0000255|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00578};
GN   Name=gshA {ECO:0000255|HAMAP-Rule:MF_00578};
OS   Pseudomonas syringae pv. syringae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B301D;
RA   Lu S.-E., Soule J.D., Gross D.C.;
RL   Submitted (AUG-2003) 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         Evidence={ECO:0000255|HAMAP-Rule:MF_00578};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00578}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC       Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00578}.
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; AY374326; AAQ82441.1; -; Genomic_DNA.
DR   AlphaFoldDB; P61379; -.
DR   SMR; P61379; -.
DR   PATRIC; fig|321.64.peg.3982; -.
DR   UniPathway; UPA00142; UER00209.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00578; Glu_cys_ligase; 1.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006334; Glut_cys_ligase.
DR   PANTHER; PTHR38761; PTHR38761; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding.
FT   CHAIN           1..535
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192535"
SQ   SEQUENCE   535 AA;  60446 MW;  59DEB88E773FBC66 CRC64;
     MKDYTLSEFL NRRLALLGER NNLSLLEQCL HGIERECLRV TATAELACTP HPQALGAALT
     NGQVTTDYSE SLLEFITPAL KNPAETIDNL DRIHRFVYSK LGDELLWSPS MPCPLPDEEH
     IPIAYYGTSN IGKLKYVYRK GLALRYGKTM QCIAGIHYNF SLPEDAWALL KQTEDFAGDA
     RDYQSHSYIA LIRNFRRYSW LLMYLFGASP ALDAGFLRGR KHQLEQHFDA DTLYLPYATS
     LRMSDLGYQS DAQADLTPCY NDLVSYTDSL RKAVATPYKP YVEVGTHDQN GEWVQLNTNV
     LQIENEYYSN IRPKRVTYSG ERPIQALVAR GVQYVEVRCL DINPFLPTGI SLEQSRFIDA
     FVLYCALEES QQLARHECSN ASSNFLSVVK EGRRPGLSLM RDNRPVDLKI WATELMEKIT
     PIARLLDQAQ GTDEHLKSIA VQQAKIDDTA LTPSAQVLAS MEAHNEGFTA FSLRQSQVHA
     EYFRTHPLSA QEQADFEAQA KTSIEEQAEL EATEEVVDFD TFVGSYQASI LSISN