ID GSHB_RHIME Reviewed; 315 AA. AC Q92SN3; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 111. 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}; OrderedLocusNames=R00338; GN ORFNames=SMc00419; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11481430; DOI=10.1073/pnas.161294398; RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T., RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., RA Thebault P., Vandenbol M., Weidner S., Galibert F.; RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium RT meliloti strain 1021."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., RA Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(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; AL591688; CAC41775.1; -; Genomic_DNA. DR RefSeq; NP_384444.1; NC_003047.1. DR RefSeq; WP_003529770.1; NC_003047.1. DR AlphaFoldDB; Q92SN3; -. DR SMR; Q92SN3; -. DR EnsemblBacteria; CAC41775; CAC41775; SMc00419. DR GeneID; 61601817; -. DR KEGG; sme:SMc00419; -. DR PATRIC; fig|266834.11.peg.1709; -. DR eggNOG; COG0189; Bacteria. DR HOGENOM; CLU_068239_0_0_5; -. DR OrthoDB; 9785415at2; -. DR UniPathway; UPA00142; UER00210. DR Proteomes; UP000001976; 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_0000197481" FT DOMAIN 127..311 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162" FT BINDING 153..209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162" FT BINDING 282 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162" FT BINDING 284 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162" SQ SEQUENCE 315 AA; 35317 MW; 32666BD118EB4087 CRC64; MAGIVNVGVQ MDHVSGITIA GDSTFAMSLE AQARGYRLFH YTPDKLSLRD GRVYATAQQM QLRDVRGDHF TLGEDERIDL STMDVILLRQ DPPFDMAYIT STHLLERLHP KTLVVNDPAW VRNSPEKIFV TEFPDLMPKT LITRDPDEIA RFRQEMGDII LKPLYGNGGA GVFHSARDDR NFSSLLEMFA QMFREPYIAQ EYLPAVRKGD KRILLVDGEP VGAINRVPAE HDSRSNMHVG GRAEATDLTA REREICTRIG PALKERGFLF VGIDVIGDYL TEINVTSPTG IREVKKFGGA DVASLLWDAI EKKRA //