ID   GSH1_SALTI              Reviewed;         518 AA.
AC   Q8Z4D6;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 119.
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};
GN   OrderedLocusNames=STY2944, t2715;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD05929.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70281.1; -; Genomic_DNA.
DR   RefSeq; NP_457216.1; NC_003198.1.
DR   RefSeq; WP_000611827.1; NZ_WSUR01000031.1.
DR   AlphaFoldDB; Q8Z4D6; -.
DR   SMR; Q8Z4D6; -.
DR   STRING; 220341.16503900; -.
DR   EnsemblBacteria; AAO70281; AAO70281; t2715.
DR   KEGG; stt:t2715; -.
DR   KEGG; sty:STY2944; -.
DR   PATRIC; fig|220341.7.peg.2997; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
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..518
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192538"
SQ   SEQUENCE   518 AA;  58426 MW;  58417A53B90F45D6 CRC64;
     MIPDVSQALA WLEKHPQALK GIQRGLERET LRVNADGTLA TTVHPEALGS ALTHKWITTD
     FAEALLEFIT PVDGDIQHML TFMRDLHRYT ARKLGDERMW PLSMPCYIAE GQDIELAQYG
     TSNTGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPMAFW QAKCGVTEGE AAKEKISAGY
     FRLIRNYYRF GWVIPYLFGA SPAICSSFLQ GKPTTLPFEK TDCGMYYLPY ATSLRLSDLG
     YTNKSQSNLG ITFNDLHEYV AGLKRAIKTP SEEYARIGVE KDGKRLQINS NVLQIENELY
     APIRPKRVTR SGESPSDALL RGGIEYIEVR SLDINPFSPI GVDEQQVRFL DLFMVWCVLA
     DAPEMSSDEL LCTRTNWNRV ILEGRKPGLT LGIGCETAQF PLPKVGKDLF RDLKRVAQTL
     DSIHGGEEYQ KVCDELVACF DNPELTFSAR ILRSMIDEGI GGTGKAFGEA YRNLLREEPL
     EILQEEEFIA ERDASVRRQQ EIEAADTEPF AAWLAKHA