ID GSHB_XANC3 Reviewed; 316 AA. AC Q8PHZ5; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 02-SEP-2026, 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=XAC3103; OS Xanthomonas citri pv. citri (strain 306). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Lysobacterales; Lysobacteraceae; Xanthomonas. OX NCBI_TaxID=1203463; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(2002). 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}. 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; AE008923; AAM37948.1; -; Genomic_DNA. DR RefSeq; WP_011052038.1; NC_003919.1. DR AlphaFoldDB; Q8PHZ5; -. DR SMR; Q8PHZ5; -. DR GeneID; 66912172; -. DR KEGG; xac:XAC3103; -. DR eggNOG; COG0189; Bacteria. DR HOGENOM; CLU_068239_0_0_6; -. DR UniPathway; UPA00142; UER00210. DR Proteomes; UP000000576; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. 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: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..316 FT /note="Glutathione synthetase" FT /id="PRO_0000197496" FT DOMAIN 124..311 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162" FT BINDING 151..208 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 316 AA; 34321 MW; BAEABE5F8A0FF268 CRC64; MSLDVVVVMD PIASIKIAKD TTFAMLLEAQ RRGHRLHYVR PGGLSLREGR AVAQVAPLSV REDKTSWFTL GEFAELAFGP GQVVLMRKDP PVDAEFVYDT QVLSVAQRAG AQIVNDPQGL RDYNEKLAAL LFPQCCPPTL VSRDAAALKA FVLEHGQAVL KPLDGMGGRS IFRSGSGDPN LNVILETLTD GNRKLTLAQR FIPDITAGDK RILLVDGLPV DYCLARIPQG DEFRGNLAAG GRGEGRPLSE RDRWIAAQVG PEMRRRGMRF VGLDVIGDYL TEVNVTSPTC VRELDAQFGL NIAGLLFDAI EAGAAQ //