ID GSHB_SALTI Reviewed; 315 AA. AC P58581; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 1. DT 27-MAR-2024, entry version 137. 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=STY3248, t3007; OS Salmonella typhi. OC Bacteria; Pseudomonadota; 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 + gamma-L-glutamyl-L-cysteine + glycine = ADP + CC glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173, CC ChEBI:CHEBI:456216; EC=6.3.2.3; Evidence={ECO:0000255|HAMAP- CC 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}. 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; CAD02919.1; -; Genomic_DNA. DR EMBL; AE014613; AAO70559.1; -; Genomic_DNA. DR RefSeq; NP_457487.1; NC_003198.1. DR RefSeq; WP_000593242.1; NZ_WSUR01000049.1. DR AlphaFoldDB; P58581; -. DR SMR; P58581; -. DR STRING; 220341.gene:17587121; -. DR KEGG; stt:t3007; -. DR KEGG; sty:STY3248; -. DR PATRIC; fig|220341.7.peg.3312; -. DR eggNOG; COG0189; Bacteria. DR HOGENOM; CLU_068239_0_0_6; -. DR OMA; IWMRKDP; -. DR OrthoDB; 9785415at2; -. DR UniPathway; UPA00142; UER00210. DR Proteomes; UP000000541; Chromosome. DR Proteomes; UP000002670; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 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. FT CHAIN 1..315 FT /note="Glutathione synthetase" FT /id="PRO_0000197483" 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; 35380 MW; D9AC53F9B23070C3 CRC64; MIKLGIVMDP IAHINIKKDT SFAMLLEAQR RGYELHYMEM ADLYLINGEA RACTRTLSVE 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 //