ID GSHB_DICDI Reviewed; 476 AA. AC Q54E83; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 24-JAN-2024, entry version 105. DE RecName: Full=Glutathione synthetase; DE Short=GSH synthetase; DE Short=GSH-S; DE EC=6.3.2.3; DE AltName: Full=Glutathione synthase; GN Name=gshB; ORFNames=DDB_G0291756; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from CC L-cysteine and L-glutamate: step 2/2. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the eukaryotic GSH synthase family. CC {ECO:0000305}. 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; AAFI02000182; EAL61574.1; -; Genomic_DNA. DR RefSeq; XP_629979.1; XM_629977.1. DR AlphaFoldDB; Q54E83; -. DR SMR; Q54E83; -. DR STRING; 44689.Q54E83; -. DR PaxDb; 44689-DDB0231404; -. DR EnsemblProtists; EAL61574; EAL61574; DDB_G0291756. DR GeneID; 8628309; -. DR KEGG; ddi:DDB_G0291756; -. DR dictyBase; DDB_G0291756; gshB. DR eggNOG; KOG0021; Eukaryota. DR HOGENOM; CLU_025152_2_1_1; -. DR InParanoid; Q54E83; -. DR OMA; NGLVMYP; -. DR PhylomeDB; Q54E83; -. DR Reactome; R-DDI-174403; Glutathione synthesis and recycling. DR UniPathway; UPA00142; UER00210. DR PRO; PR:Q54E83; -. DR Proteomes; UP000002195; Chromosome 6. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB. DR GO; GO:0004363; F:glutathione synthase activity; ISS:dictyBase. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0006750; P:glutathione biosynthetic process; ISS:dictyBase. DR Gene3D; 3.30.1490.50; -; 1. DR Gene3D; 3.30.1490.80; -; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR Gene3D; 3.40.50.1760; Glutathione synthase, substrate-binding domain superfamily, eukaryotic; 1. DR InterPro; IPR005615; Glutathione_synthase. DR InterPro; IPR014042; Glutathione_synthase_a-hlx. DR InterPro; IPR014709; Glutathione_synthase_C_euk. DR InterPro; IPR014049; Glutathione_synthase_N_euk. DR InterPro; IPR037013; GSH-S_sub-bd_sf. DR InterPro; IPR004887; GSH_synth_subst-bd. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR NCBIfam; TIGR01986; glut_syn_euk; 1. DR PANTHER; PTHR11130; GLUTATHIONE SYNTHETASE; 1. DR PANTHER; PTHR11130:SF0; GLUTATHIONE SYNTHETASE; 1. DR Pfam; PF03917; GSH_synth_ATP; 1. DR Pfam; PF03199; GSH_synthase; 1. DR PIRSF; PIRSF001558; GSHase; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. PE 3: Inferred from homology; KW ATP-binding; Glutathione biosynthesis; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..476 FT /note="Glutathione synthetase" FT /id="PRO_0000312710" FT BINDING 117 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 137 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 137 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 139 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 141..144 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 211..213 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 217 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 267..270 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 308 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 367..376 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 371 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 378 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 400..403 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 426 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 452 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 454 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 460 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 463..464 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 476 AA; 54140 MW; 539645AD00EA4904 CRC64; MEEKLNDLKE QGIDWAFANG LIMIKKPTEE EAKNNVVNVT HVPFSLYPSK MNKKLFNEAC KLAEDYNLLV HNISKDYDFL QNTLKDVFDD FTQMLLNIQR KVVKEGIKQK ISLGIFRSDY MFHNKIEGEE ERIYQVELNT ISSSLAVVSN RVFNLHKYLI GRNDLNDNGY DLLNHPTNQS DKEISDSIAL AHKLYNKEKS SVVLMIIQEG ERNIYDQKGL EFQLWSNHSI KLIRRTMKEI NQCAKLDEEN GSVLIVDGME ISVAYYRAGY TPNDYTSSGG DEWKARLLIE RSLAIKCPTI AHHLVGVKKI QQVLAQPGVL EKFINNDKES LQRVKRSFTG LYSLSKEDID MSVVKEAIES PQNYVMKPQR EGGGNNIYND QVAIALKSMS SEELSSYILM DKIMSKSFKT HVVRDRQLLE IEGLYELGIY SVFISNGDDD IVLNKQAGIL LRTKTANSDE VGVAAGFGLL DSPILE //