GSHB_ARATH
ID GSHB_ARATH Reviewed; 539 AA.
AC P46416; Q8H171; Q9SMW4; Q9SMW5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 165.
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; OrderedLocusNames=At5g27380; ORFNames=F21A20_90;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. RLD;
RX PubMed=8914526; DOI=10.1007/bf00040827;
RA Wang C.L., Oliver D.J.;
RT "Cloning of the cDNA and genomic clones for glutathione synthetase from
RT Arabidopsis thaliana and complementation of a gsh2 mutant in fission
RT yeast.";
RL Plant Mol. Biol. 31:1093-1104(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RA Skipsey M., Andrews C.J., Townson J.K., Jepson I., Edwards R.;
RT "Isolation of cDNA and genomic clones of glutathione synthetase containing
RT plastidic targeting sequences from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-137(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-539.
RC STRAIN=cv. C24;
RX PubMed=8521973; DOI=10.1016/0014-5793(95)01253-1;
RA Rawlins M.R., Leaver C.J., May M.J.;
RT "Characterisation of an Arabidopsis thaliana cDNA encoding glutathione
RT synthetase.";
RL FEBS Lett. 376:81-86(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-539.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8612643; DOI=10.1111/j.1432-1033.1996.00662.x;
RA Ullmann P., Gondet L., Potier S., Bach T.J.;
RT "Cloning of Arabidopsis thaliana glutathione synthetase (GSH2) by
RT functional complementation of a yeast gsh2 mutant.";
RL Eur. J. Biochem. 236:662-669(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-539.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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.
CC -!- SIMILARITY: Belongs to the eukaryotic GSH synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64781.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA99146.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL11580.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA58318.1; Type=Erroneous initiation; Evidence={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; U22359; AAA64781.1; ALT_INIT; mRNA.
DR EMBL; U53856; AAA99146.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AJ243812; CAB51026.1; -; Genomic_DNA.
DR EMBL; AJ243813; CAB51027.1; -; mRNA.
DR EMBL; AC007123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93678.1; -; Genomic_DNA.
DR EMBL; Z50153; CAA90515.1; -; mRNA.
DR EMBL; X83411; CAA58318.1; ALT_INIT; mRNA.
DR EMBL; AF424586; AAL11580.1; ALT_INIT; mRNA.
DR EMBL; BT000624; AAN18190.1; -; mRNA.
DR PIR; S62654; S62654.
DR PIR; S68223; S68223.
DR PIR; T52565; T52565.
DR RefSeq; NP_568495.2; NM_122620.4.
DR AlphaFoldDB; P46416; -.
DR SMR; P46416; -.
DR BioGRID; 18071; 3.
DR STRING; 3702.AT5G27380.1; -.
DR iPTMnet; P46416; -.
DR PaxDb; P46416; -.
DR PRIDE; P46416; -.
DR ProteomicsDB; 222360; -.
DR EnsemblPlants; AT5G27380.1; AT5G27380.1; AT5G27380.
DR GeneID; 832797; -.
DR Gramene; AT5G27380.1; AT5G27380.1; AT5G27380.
DR KEGG; ath:AT5G27380; -.
DR Araport; AT5G27380; -.
DR TAIR; locus:2146395; AT5G27380.
DR eggNOG; KOG0021; Eukaryota.
DR HOGENOM; CLU_025152_3_0_1; -.
DR InParanoid; P46416; -.
DR OMA; NGLVMYP; -.
DR OrthoDB; 1189955at2759; -.
DR PhylomeDB; P46416; -.
DR BioCyc; ARA:AT5G27380-MON; -.
DR BRENDA; 6.3.2.3; 399.
DR UniPathway; UPA00142; UER00210.
DR PRO; PR:P46416; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P46416; baseline and differential.
DR Genevisible; P46416; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006750; P:glutathione biosynthetic process; IDA:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
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..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..539
FT /note="Glutathione synthetase, chloroplastic"
FT /id="PRO_0000013058"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 213..216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281..283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 335..338
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 428..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 464..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 526..527
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 17
FT /note="N -> S (in Ref. 2; CAB51026/CAB51027)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="S -> P (in Ref. 2; CAB51026/CAB51027)"
FT /evidence="ECO:0000305"
FT CONFLICT 30..34
FT /note="SSSLK -> ELRQG (in Ref. 5; CAA90515)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="S -> P (in Ref. 2 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="V -> G (in Ref. 6; CAA58318)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="S -> T (in Ref. 2 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="A -> G (in Ref. 2 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="N -> D (in Ref. 2 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="G -> S (in Ref. 2; CAB51027)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="D -> G (in Ref. 2; CAB51027)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="G -> A (in Ref. 6; CAA58318)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="I -> T (in Ref. 2; CAB51027)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="I -> M (in Ref. 2; CAB51027)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="E -> K (in Ref. 2 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="I -> N (in Ref. 2 and 6)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 60271 MW; 2BFBF9A1D53E4A96 CRC64;
MGSGCSSLSY SSSSTCNATV FSISSSPSSS SSLKLNPSSF LFQNPKTLRN QSPLRCGRSF
KMESQKPIFD LEKLDDEFVQ KLVYDALVWS SLHGLVVGDK SYQKSGNVPG VGLMHAPIAL
LPTAFPEAYW KQACNVTPLF NELIDRVSLD GKFLQDSLSR TKKVDVFTSR LLDIHSKMLE
RNKKEDIRLG LHRFDYMLDE ETNSLLQIEM NTISCSFPGL SRLVSQLHQS LLRSYGDQIG
IDSERVPINT STIQFADALA KAWLEYSNPR AVVMVIVQPE ERNMYDQHLL SSILREKHNI
VVIRKTLAEV EKEGSVQEDE TLIVGGQAVA VVYFRSGYTP NDHPSESEWN ARLLIEESSA
VKCPSIAYHL TGSKKIQQEL AKPGVLERFL DNKEDIAKLR KCFAGLWSLD DSEIVKQAIE
KPGLFVMKPQ REGGGNNIYG DDVRENLLRL QKEGEEGNAA YILMQRIFPK VSNMFLVREG
VYHKHQAISE LGVYGAYLRS KDEVIVNEQS GYLMRTKIAS SDEGGVAAGF GVLDSIYLI
