ID GSHB_ECO57 Reviewed; 315 AA. AC P58578; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 1. DT 27-MAR-2024, entry version 130. 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=Z4292, ECs3823; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). 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; AE005174; AAG58078.1; -; Genomic_DNA. DR EMBL; BA000007; BAB37246.1; -; Genomic_DNA. DR PIR; B85952; B85952. DR PIR; G91106; G91106. DR RefSeq; NP_311850.1; NC_002695.1. DR RefSeq; WP_000593272.1; NZ_VOAI01000003.1. DR AlphaFoldDB; P58578; -. DR SMR; P58578; -. DR STRING; 155864.Z4292; -. DR GeneID; 916355; -. DR KEGG; ece:Z4292; -. DR KEGG; ecs:ECs_3823; -. DR PATRIC; fig|386585.9.peg.3989; -. DR eggNOG; COG0189; Bacteria. DR HOGENOM; CLU_068239_0_0_6; -. DR OMA; IWMRKDP; -. DR UniPathway; UPA00142; UER00210. DR Proteomes; UP000000558; Chromosome. DR Proteomes; UP000002519; 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; Reference proteome. FT CHAIN 1..315 FT /note="Glutathione synthetase" FT /id="PRO_0000197467" 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; 967AB29DE113DDE4 CRC64; MIKLGIVMDP IANINIKKDS SFAMLLEAQR RGYELHYMEM GDLYLINGEA RAHTRTLNVK QNYEEWFSFV GEQDLPLADL DVILMRKDPP FDTEFIYATY ILERAEEKGT LIVNKPQSLR DCNEKLFTAW FSDLTPETLV TRNKAQLKAF WEKHSDIILK PLDGMGGASI FRVKEGDPNL GVIAETLTEH GTRYCMAQNY LPAIKDGDKR VLVVDGEPVP YCLARIPQGG ETRGNLAAGG RGEPRPLTES DWKIARQIGP TLKEKGLIFV GLDIIGDRLT EINVTSPTCI REIEAEFPVS ITGMLMDAIE ARLQQ //