ID GSHB_NOSS1 Reviewed; 324 AA. AC P45480; Q43879; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 27-MAR-2024, entry version 127. 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}; Synonyms=gsh-II; GN OrderedLocusNames=all3859; OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576). OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7557485; DOI=10.1016/0378-1119(95)00416-4; RA Doherty H.M., Adams D.G.; RT "Cloning and sequence of ftsZ and flanking regions from the cyanobacterium RT Anabaena PCC 7120."; RL Gene 163:93-96(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576; RX PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., RA Takazawa M., Yamada M., Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-324. RX PubMed=8525061; DOI=10.1016/0923-2508(96)80290-7; RA Zhang C.C., Huguenin S., Friry A.; RT "Analysis of genes encoding the cell division protein FtsZ and a RT glutathione synthetase homologue in the cyanobacterium Anabaena sp. PCC RT 7120."; RL Res. Microbiol. 146:445-455(1995). 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; U14408; AAA85527.1; -; Genomic_DNA. DR EMBL; BA000019; BAB75558.1; -; Genomic_DNA. DR EMBL; Z31371; CAA83242.1; -; Genomic_DNA. DR PIR; AD2288; AD2288. DR PIR; JC4291; JC4291. DR RefSeq; WP_010998000.1; NZ_RSCN01000011.1. DR AlphaFoldDB; P45480; -. DR SMR; P45480; -. DR STRING; 103690.gene:10495901; -. DR KEGG; ana:all3859; -. DR eggNOG; COG0189; Bacteria. DR OrthoDB; 9785415at2; -. DR UniPathway; UPA00142; UER00210. DR Proteomes; UP000002483; 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..324 FT /note="Glutathione synthetase" FT /id="PRO_0000197452" FT DOMAIN 133..317 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162" FT BINDING 159..215 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162" FT BINDING 288 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162" FT BINDING 290 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162" FT CONFLICT 50 FT /note="W -> C (in Ref. 1; AAA85527)" FT /evidence="ECO:0000305" FT CONFLICT 243 FT /note="M -> V (in Ref. 3; CAA83242)" FT /evidence="ECO:0000305" SQ SEQUENCE 324 AA; 35953 MW; 03C6E7E8481DD8D1 CRC64; MKLAFIIDPI HQLDPCHDTS VALMEAAQIL GHEVWVTQAN WLSVVDSKAW AILQQVELVP VQLIDGRWVA ASPWYTLNTR SFSSLETMDA VFMRTDPPVN DAYLYATYVL DYVDQRKTLV INNPNGIRGA NEKMYALQFT KAIPETIVSA DKDFIRQFVE AKGATVLKPL GNKAGEGILF LQAGDRNFNS IVELSTQQGR LPVMVQTYLP EAKEGDKRII LLNGEPIGAL NRLASGSDFR NNMATGGTVA KTEITPREEE ICSQIAANLR QDGLIFVGID VIGGYLTEVN VTSPTGIREI DRLDGTRLAH QVIQWVEKNL QIQN //