GSHB_BRAJU
ID GSHB_BRAJU Reviewed; 530 AA.
AC O23732;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
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; Synonyms=GSHII;
OS Brassica juncea (Indian mustard) (Sinapis juncea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root;
RX PubMed=9620267; DOI=10.1023/a:1005929022061;
RA Schaefer H.J., Haag-Kerwer A., Rausch T.H.;
RT "cDNA cloning and expression analysis of genes encoding GSH synthesis in
RT roots of the heavy-metal accumulator Brassica juncea L.: evidence for Cd-
RT induction of a putative mitochondrial gamma-glutamylcysteine synthetase
RT isoform.";
RL Plant Mol. Biol. 37:87-97(1998).
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; Y10984; CAA71878.1; -; mRNA.
DR AlphaFoldDB; O23732; -.
DR SMR; O23732; -.
DR UniPathway; UPA00142; UER00210.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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; 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; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..530
FT /note="Glutathione synthetase, chloroplastic"
FT /id="PRO_0000013059"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 204..207
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272..274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 326..329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 419..428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 455..458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 517..518
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 530 AA; 59741 MW; B149C24DB4F5EAFD CRC64;
MVGGCSSLSY SSSSTFIATT TLSSSLKLNP QSFIFHLNLR KRPPLRCLSS LTMESPKPIL
DFEKFDDGFV QKLVYDALVW SSLHGLVVGD KTHQRSGTVP GVGMMHAPIA LLPTPFPESY
WNQACEVAPI FNELVDRISL DGKFIQDSLS RTRKADVFTS RLLEIHSKML ESNKREEIRL
GLHRSDYMLD EETKSLLQIE MNTISCSFPG FGRLVTELHQ SLLRSHGDHL GLDSKRVPRN
GSTSQFADAM AKAWLEYNNP RAVVMVVVQP DERNMYDQHW LSSVLREKHN IVTIRKSLAE
VETEGRVHED GTLTVGGQAV SVVYYRSGYT PRDYPSESEW NARLLIEQSS AVKCPSIAYH
LAGTKKIQQE LAKPGVLERF MDNKDDIAKL RKCFAGLWSL DDPEIIKKAI EKPELFVMKP
QREGGGNNIY GDDVRENLLR LQREGEEENA AYILMQRIFP KVSNVFLLRD GVYHKDQAIS
ELGVYGAYLR NKERVIINEH SGYLMRTKVS SSDEGGVAAG YAVLDSIYLN
