ID   GSHB_SALTY              Reviewed;         315 AA.
AC   P58580;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   02-SEP-2026, entry version 124.
DE   RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE            EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00162};
DE   AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE            Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00162};
DE            Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00162};
DE   AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00162};
GN   Name=gshB {ECO:0000255|HAMAP-Rule:MF_00162};
GN   OrderedLocusNames=STM3095;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-L-glutamyl-L-cysteine + glycine + ATP = glutathione +
CC         ADP + phosphate + H(+); Xref=Rhea:RHEA:13557, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00162};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00162}.
CC   -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00162}.
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DR   EMBL; AE006468; AAL21970.1; -; Genomic_DNA.
DR   RefSeq; NP_462011.1; NC_003197.2.
DR   RefSeq; WP_000593248.1; NC_003197.2.
DR   AlphaFoldDB; P58580; -.
DR   SMR; P58580; -.
DR   STRING; 99287.STM3095; -.
DR   PaxDb; 99287-STM3095; -.
DR   GeneID; 1254618; -.
DR   KEGG; stm:STM3095; -.
DR   PATRIC; fig|99287.12.peg.3280; -.
DR   HOGENOM; CLU_068239_0_0_6; -.
DR   OMA; IWMRKDP; -.
DR   PhylomeDB; P58580; -.
DR   BioCyc; SENT99287:STM3095-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004363; F:glutathione synthase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   FunFam; 3.30.1490.20:FF:000009; Glutathione synthetase; 1.
DR   FunFam; 3.30.470.20:FF:000010; Glutathione synthetase; 1.
DR   FunFam; 3.40.50.20:FF:000009; Glutathione synthetase; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   HAMAP; MF_00162; GSH_S; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006284; Glut_synth_pro.
DR   InterPro; IPR004218; GSHS_ATP-bd.
DR   InterPro; IPR004215; GSHS_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR01380; glut_syn; 1.
DR   NCBIfam; NF003573; PRK05246.1; 1.
DR   PANTHER; PTHR21621:SF4; GLUTATHIONE SYNTHETASE; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF02955; GSH-S_ATP; 1.
DR   Pfam; PF02951; GSH-S_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutathione biosynthesis; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..315
FT                   /note="Glutathione synthetase"
FT                   /id="PRO_0000197484"
FT   DOMAIN          125..310
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT   BINDING         151..207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT   BINDING         281
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT   BINDING         283
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
SQ   SEQUENCE   315 AA;  35433 MW;  98AC5A80C230761F CRC64;
     MIKLGIVMDP IAHINIKKDT SFAMLLEAQR RGYELHYMEM ADLYLINGEA RARTRTLSVE
     QNYDKWYEFG SEQEIKLADL DVILMRKDPP FDTEFIYATY ILERAEEEGT LIVNKPQSLR
     DCNEKLYTAW FADLTPETLV TRNKAQLKAF WEKHGDIIMK PLDGMGGASI FRVKEGDPNI
     GVIAETLTEL GNRYCMAQNY LPAIKDGDKR VLVVDGEPVP YCLARIPQGG ETRGNLAAGG
     RGEPRPLSES DWEIARRVGP TLKAKGLIFV GLDIIGDRLT EINVTSPTCV REIEAEYPIS
     ITGMLMDAIE ARLAK
//