GSHB_SOLLC
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 03-AUG-2022, entry version 119.
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}.
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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.Solyc01g098610.2.1; -.
DR PaxDb; O22494; -.
DR PRIDE; O22494; -.
DR GeneID; 543537; -.
DR KEGG; sly:543537; -.
DR eggNOG; KOG0021; Eukaryota.
DR InParanoid; O22494; -.
DR OrthoDB; 1189955at2759; -.
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 GO; GO:0009753; P:response to jasmonic acid; IEA:EnsemblPlants.
DR CDD; cd00228; eu-GS; 1.
DR Gene3D; 1.10.1080.10; -; 1.
DR Gene3D; 3.30.1490.50; -; 1.
DR Gene3D; 3.30.1490.80; -; 1.
DR Gene3D; 3.40.50.1760; -; 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 PANTHER; PTHR11130; PTHR11130; 1.
DR Pfam; PF03917; GSH_synth_ATP; 1.
DR Pfam; PF03199; GSH_synthase; 1.
DR PIRSF; PIRSF001558; GSHase; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01986; glut_syn_euk; 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
