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Protein

Glutathione synthetase, chloroplastic

Gene

GSH2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathway: glutathione biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes glutathione from L-cysteine and L-glutamate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate--cysteine ligase, chloroplastic (GSH1)
  2. Glutathione synthetase, chloroplastic (GSH2)
This subpathway is part of the pathway glutathione biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutathione from L-cysteine and L-glutamate, the pathway glutathione biosynthesis and in Sulfur metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei193 – 1931SubstrateBy similarity
Metal bindingi209 – 2091MagnesiumBy similarity
Binding sitei209 – 2091ATPBy similarity
Metal bindingi211 – 2111MagnesiumBy similarity
Binding sitei287 – 2871SubstrateBy similarity
Binding sitei374 – 3741ATPBy similarity
Metal bindingi432 – 4321MagnesiumBy similarity
Binding sitei439 – 4391ATPBy similarity
Binding sitei490 – 4901ATPBy similarity
Binding sitei515 – 5151SubstrateBy similarity
Binding sitei517 – 5171ATPBy similarity
Binding sitei523 – 5231ATP; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi428 – 43710ATPBy similarity
Nucleotide bindingi464 – 4674ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • glutathione biosynthetic process Source: TAIR
  • response to jasmonic acid Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G27380-MONOMER.
BRENDAi6.3.2.3. 399.
ReactomeiREACT_290784. Glutathione synthesis and recycling.
UniPathwayiUPA00142; UER00210.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione synthetase, chloroplastic (EC:6.3.2.3)
Short name:
GSH synthetase
Short name:
GSH-S
Short name:
Glutathione synthase
Gene namesi
Name:GSH2
Synonyms:GSHII
Ordered Locus Names:At5g27380
ORF Names:F21A20_90
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G27380.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6161ChloroplastSequence AnalysisAdd
BLAST
Chaini62 – 539478Glutathione synthetase, chloroplasticPRO_0000013058Add
BLAST

Proteomic databases

PaxDbiP46416.
PRIDEiP46416.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi18071. 1 interaction.
STRINGi3702.AT5G27380.1.

Structurei

3D structure databases

ProteinModelPortaliP46416.
SMRiP46416. Positions 67-538.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni213 – 2164Substrate bindingBy similarity
Regioni281 – 2833Substrate bindingBy similarity
Regioni335 – 3384Substrate bindingBy similarity
Regioni526 – 5272Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the eukaryotic GSH synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG329040.
HOGENOMiHOG000172641.
InParanoidiP46416.
KOiK01920.
OMAiRIPANNA.
PhylomeDBiP46416.

Family and domain databases

Gene3Di1.10.1080.10. 1 hit.
3.30.1490.50. 1 hit.
3.30.1490.80. 1 hit.
3.40.50.1760. 1 hit.
InterProiIPR004887. Glutathione_synth_subst-bd_euk.
IPR014042. Glutathione_synthase_a-hlx_euk.
IPR014709. Glutathione_synthase_dom.
IPR005615. Glutathione_synthase_euk.
IPR014049. Glutathione_synthase_N_euk.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PANTHERiPTHR11130. PTHR11130. 1 hit.
PfamiPF03917. GSH_synth_ATP. 1 hit.
PF03199. GSH_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001558. GSHase. 1 hit.
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01986. glut_syn_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46416-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSGCSSLSY SSSSTCNATV FSISSSPSSS SSLKLNPSSF LFQNPKTLRN
60 70 80 90 100
QSPLRCGRSF KMESQKPIFD LEKLDDEFVQ KLVYDALVWS SLHGLVVGDK
110 120 130 140 150
SYQKSGNVPG VGLMHAPIAL LPTAFPEAYW KQACNVTPLF NELIDRVSLD
160 170 180 190 200
GKFLQDSLSR TKKVDVFTSR LLDIHSKMLE RNKKEDIRLG LHRFDYMLDE
210 220 230 240 250
ETNSLLQIEM NTISCSFPGL SRLVSQLHQS LLRSYGDQIG IDSERVPINT
260 270 280 290 300
STIQFADALA KAWLEYSNPR AVVMVIVQPE ERNMYDQHLL SSILREKHNI
310 320 330 340 350
VVIRKTLAEV EKEGSVQEDE TLIVGGQAVA VVYFRSGYTP NDHPSESEWN
360 370 380 390 400
ARLLIEESSA VKCPSIAYHL TGSKKIQQEL AKPGVLERFL DNKEDIAKLR
410 420 430 440 450
KCFAGLWSLD DSEIVKQAIE KPGLFVMKPQ REGGGNNIYG DDVRENLLRL
460 470 480 490 500
QKEGEEGNAA YILMQRIFPK VSNMFLVREG VYHKHQAISE LGVYGAYLRS
510 520 530
KDEVIVNEQS GYLMRTKIAS SDEGGVAAGF GVLDSIYLI
Length:539
Mass (Da):60,271
Last modified:April 30, 2003 - v3
Checksum:i2BFBF9A1D53E4A96
GO

Sequence cautioni

The sequence AAA64781.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAA99146.1 differs from that shown. Reason: Frameshift at positions 40 and 44. Curated
The sequence AAL11580.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA58318.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171N → S in CAB51026 (Ref. 2) Curated
Sequence conflicti17 – 171N → S in CAB51027 (Ref. 2) Curated
Sequence conflicti26 – 261S → P in CAB51026 (Ref. 2) Curated
Sequence conflicti26 – 261S → P in CAB51027 (Ref. 2) Curated
Sequence conflicti30 – 345SSSLK → ELRQG in CAA90515 (PubMed:8521973).Curated
Sequence conflicti52 – 521S → P (Ref. 2) Curated
Sequence conflicti52 – 521S → P (PubMed:8612643).Curated
Sequence conflicti96 – 961V → G in CAA58318 (PubMed:8612643).Curated
Sequence conflicti101 – 1011S → T (Ref. 2) Curated
Sequence conflicti101 – 1011S → T (PubMed:8612643).Curated
Sequence conflicti124 – 1241A → G (Ref. 2) Curated
Sequence conflicti124 – 1241A → G (PubMed:8612643).Curated
Sequence conflicti135 – 1351N → D (Ref. 2) Curated
Sequence conflicti135 – 1351N → D (PubMed:8612643).Curated
Sequence conflicti151 – 1511G → S in CAB51027 (Ref. 2) Curated
Sequence conflicti199 – 1991D → G in CAB51027 (Ref. 2) Curated
Sequence conflicti219 – 2191G → A in CAA58318 (PubMed:8612643).Curated
Sequence conflicti438 – 4381I → T in CAB51027 (Ref. 2) Curated
Sequence conflicti488 – 4881I → M in CAB51027 (Ref. 2) Curated
Sequence conflicti503 – 5031E → K (Ref. 2) Curated
Sequence conflicti503 – 5031E → K (PubMed:8612643).Curated
Sequence conflicti539 – 5391I → N (Ref. 2) Curated
Sequence conflicti539 – 5391I → N (PubMed:8612643).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22359 mRNA. Translation: AAA64781.1. Different initiation.
U53856 Genomic DNA. Translation: AAA99146.1. Frameshift.
AJ243812 Genomic DNA. Translation: CAB51026.1.
AJ243813 mRNA. Translation: CAB51027.1.
AC007123 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93678.1.
Z50153 mRNA. Translation: CAA90515.1.
X83411 mRNA. Translation: CAA58318.1. Different initiation.
AF424586 mRNA. Translation: AAL11580.1. Different initiation.
BT000624 mRNA. Translation: AAN18190.1.
PIRiS62654.
S68223.
T52565.
RefSeqiNP_568495.2. NM_122620.3.
UniGeneiAt.21515.
At.55036.

Genome annotation databases

EnsemblPlantsiAT5G27380.1; AT5G27380.1; AT5G27380.
GeneIDi832797.
KEGGiath:AT5G27380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22359 mRNA. Translation: AAA64781.1. Different initiation.
U53856 Genomic DNA. Translation: AAA99146.1. Frameshift.
AJ243812 Genomic DNA. Translation: CAB51026.1.
AJ243813 mRNA. Translation: CAB51027.1.
AC007123 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93678.1.
Z50153 mRNA. Translation: CAA90515.1.
X83411 mRNA. Translation: CAA58318.1. Different initiation.
AF424586 mRNA. Translation: AAL11580.1. Different initiation.
BT000624 mRNA. Translation: AAN18190.1.
PIRiS62654.
S68223.
T52565.
RefSeqiNP_568495.2. NM_122620.3.
UniGeneiAt.21515.
At.55036.

3D structure databases

ProteinModelPortaliP46416.
SMRiP46416. Positions 67-538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi18071. 1 interaction.
STRINGi3702.AT5G27380.1.

Proteomic databases

PaxDbiP46416.
PRIDEiP46416.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G27380.1; AT5G27380.1; AT5G27380.
GeneIDi832797.
KEGGiath:AT5G27380.

Organism-specific databases

TAIRiAT5G27380.

Phylogenomic databases

eggNOGiNOG329040.
HOGENOMiHOG000172641.
InParanoidiP46416.
KOiK01920.
OMAiRIPANNA.
PhylomeDBiP46416.

Enzyme and pathway databases

UniPathwayiUPA00142; UER00210.
BioCyciARA:AT5G27380-MONOMER.
BRENDAi6.3.2.3. 399.
ReactomeiREACT_290784. Glutathione synthesis and recycling.

Miscellaneous databases

PROiP46416.

Family and domain databases

Gene3Di1.10.1080.10. 1 hit.
3.30.1490.50. 1 hit.
3.30.1490.80. 1 hit.
3.40.50.1760. 1 hit.
InterProiIPR004887. Glutathione_synth_subst-bd_euk.
IPR014042. Glutathione_synthase_a-hlx_euk.
IPR014709. Glutathione_synthase_dom.
IPR005615. Glutathione_synthase_euk.
IPR014049. Glutathione_synthase_N_euk.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PANTHERiPTHR11130. PTHR11130. 1 hit.
PfamiPF03917. GSH_synth_ATP. 1 hit.
PF03199. GSH_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001558. GSHase. 1 hit.
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01986. glut_syn_euk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNA and genomic clones for glutathione synthetase from Arabidopsis thaliana and complementation of a gsh2 mutant in fission yeast."
    Wang C.L., Oliver D.J.
    Plant Mol. Biol. 31:1093-1104(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: cv. RLD.
  2. "Isolation of cDNA and genomic clones of glutathione synthetase containing plastidic targeting sequences from Arabidopsis thaliana."
    Skipsey M., Andrews C.J., Townson J.K., Jepson I., Edwards R.
    Plant Gene Register PGR99-137
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Characterisation of an Arabidopsis thaliana cDNA encoding glutathione synthetase."
    Rawlins M.R., Leaver C.J., May M.J.
    FEBS Lett. 376:81-86(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-539.
    Strain: cv. C24.
  6. "Cloning of Arabidopsis thaliana glutathione synthetase (GSH2) by functional complementation of a yeast gsh2 mutant."
    Ullmann P., Gondet L., Potier S., Bach T.J.
    Eur. J. Biochem. 236:662-669(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-539.
    Strain: cv. Landsberg erecta.
  7. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-539.
    Strain: cv. Columbia.

Entry informationi

Entry nameiGSHB_ARATH
AccessioniPrimary (citable) accession number: P46416
Secondary accession number(s): Q8H171, Q9SMW4, Q9SMW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 30, 2003
Last modified: June 24, 2015
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.