ID GSHB_SOLLC Reviewed; 546 AA. AC O22494; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 24-JAN-2024, entry version 125. DE RecName: Full=Glutathione synthetase, chloroplastic; DE Short=GSH synthetase; DE Short=GSH-S; DE Short=Glutathione synthase; DE EC=6.3.2.3; DE Flags: Precursor; GN Name=GSH2; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum; OC Solanum subgen. Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Ohio state 4; RA Kovari I.A., Goldsbrough P.B.; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. 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; AF017984; AAB71231.1; -; mRNA. DR PIR; T04336; T04336. DR RefSeq; NP_001234014.2; NM_001247085.3. DR AlphaFoldDB; O22494; -. DR SMR; O22494; -. DR STRING; 4081.O22494; -. DR PaxDb; 4081-Solyc01g098610-2-1; -. DR GeneID; 543537; -. DR KEGG; sly:543537; -. DR eggNOG; KOG0021; Eukaryota. DR InParanoid; O22494; -. DR OrthoDB; 1448at2759; -. DR UniPathway; UPA00142; UER00210. DR Proteomes; UP000004994; Unplaced. DR ExpressionAtlas; O22494; baseline and differential. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR CDD; cd00228; eu-GS; 1. 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 2: Evidence at transcript level; KW ATP-binding; Chloroplast; Glutathione biosynthesis; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Plastid; Reference proteome; KW Transit peptide. FT TRANSIT 1..63 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 64..546 FT /note="Glutathione synthetase, chloroplastic" FT /id="PRO_0000013060" FT BINDING 200 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 216 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 216 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 218 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 220..223 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 288..290 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 294 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 342..345 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 381 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 435..444 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 439 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 446 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 471..474 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 497 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 522 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 524 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 530 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 533..534 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 546 AA; 61174 MW; BD1CD811647C43D4 CRC64; MGSGCSSPSI SLTTIATSHF QSQESLSNSL NFYSPTRFLE PHLLKSSKIF IPKSPLKCAK VPEMQTQLED SAKPIVDPHD IDSKLVQKLA NDALVWCPLR GLLVGDRNSE RSGTIPGVDM VHAPVALIPM SFPESHWKQA CEVAPIFNEL VDRVSQDGEF LQQSLSRTRK ADPFTSRLLE IHSKMLEINK LEEIRLGLHR SDYMLDEQTK LLLQIELNTI SSSFPGLSCL VSELHRSLLQ QYREDIASDP NRIPANNAVN QFAEALAKAW NEYGDPRAVI IFVVQAEERN MYDQHWLSAS LRERHQVTTI RKTLAEIDAL GELQQDGTLV VDGQAVAVIY FRAGYAPSDY HSESEWKARL LMEQSRAVKC PSISYHLAGS KKIQQELAKP NVLERFLENK DDIAKLRKCF AGLWSLDESD IVKDAIERPE LYVMKPQREG GGNNIYGEDV RGALLKLQKE GTGSDAAYIL MQRIFPKISH SILMREGISH KEETISELGI YGTYLRNKTE VLINQQAGYL MRTKVSSSDE GGVAAGFAVL DSIYLV //