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P46416 (GSHB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione synthetase, chloroplastic

Short name=GSH synthetase
Short name=GSH-S
Short name=Glutathione synthase
EC=6.3.2.3
Gene names
Name:GSH2
Synonyms:GSHII
Ordered Locus Names:At5g27380
ORF Names:F21A20_90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.

Subunit structure

Homodimer By similarity.

Subcellular location

Plastidchloroplast.

Sequence similarities

Belongs to the eukaryotic GSH synthase family.

Sequence caution

The sequence AAA64781.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAA99146.1 differs from that shown. Reason: Frameshift at positions 40 and 44.

The sequence AAL11580.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA58318.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6161Chloroplast Potential
Chain62 – 539478Glutathione synthetase, chloroplastic
PRO_0000013058

Regions

Nucleotide binding428 – 43710ATP By similarity
Nucleotide binding464 – 4674ATP By similarity
Region213 – 2164Substrate binding By similarity
Region281 – 2833Substrate binding By similarity
Region335 – 3384Substrate binding By similarity
Region526 – 5272Substrate binding By similarity

Sites

Metal binding2091Magnesium By similarity
Metal binding2111Magnesium By similarity
Metal binding4321Magnesium By similarity
Binding site1931Substrate By similarity
Binding site2091ATP By similarity
Binding site2871Substrate By similarity
Binding site3741ATP By similarity
Binding site4391ATP By similarity
Binding site4901ATP By similarity
Binding site5151Substrate By similarity
Binding site5171ATP By similarity
Binding site5231ATP; via carbonyl oxygen By similarity

Experimental info

Sequence conflict171N → S in CAB51026. Ref.2
Sequence conflict171N → S in CAB51027. Ref.2
Sequence conflict261S → P in CAB51026. Ref.2
Sequence conflict261S → P in CAB51027. Ref.2
Sequence conflict30 – 345SSSLK → ELRQG in CAA90515. Ref.5
Sequence conflict521S → P Ref.2
Sequence conflict521S → P Ref.6
Sequence conflict961V → G in CAA58318. Ref.6
Sequence conflict1011S → T Ref.2
Sequence conflict1011S → T Ref.6
Sequence conflict1241A → G Ref.2
Sequence conflict1241A → G Ref.6
Sequence conflict1351N → D Ref.2
Sequence conflict1351N → D Ref.6
Sequence conflict1511G → S in CAB51027. Ref.2
Sequence conflict1991D → G in CAB51027. Ref.2
Sequence conflict2191G → A in CAA58318. Ref.6
Sequence conflict4381I → T in CAB51027. Ref.2
Sequence conflict4881I → M in CAB51027. Ref.2
Sequence conflict5031E → K Ref.2
Sequence conflict5031E → K Ref.6
Sequence conflict5391I → N Ref.2
Sequence conflict5391I → N Ref.6

Sequences

Sequence LengthMass (Da)Tools
P46416 [UniParc].

Last modified April 30, 2003. Version 3.
Checksum: 2BFBF9A1D53E4A96

FASTA53960,271
        10         20         30         40         50         60 
MGSGCSSLSY SSSSTCNATV FSISSSPSSS SSLKLNPSSF LFQNPKTLRN QSPLRCGRSF 

        70         80         90        100        110        120 
KMESQKPIFD LEKLDDEFVQ KLVYDALVWS SLHGLVVGDK SYQKSGNVPG VGLMHAPIAL 

       130        140        150        160        170        180 
LPTAFPEAYW KQACNVTPLF NELIDRVSLD GKFLQDSLSR TKKVDVFTSR LLDIHSKMLE 

       190        200        210        220        230        240 
RNKKEDIRLG LHRFDYMLDE ETNSLLQIEM NTISCSFPGL SRLVSQLHQS LLRSYGDQIG 

       250        260        270        280        290        300 
IDSERVPINT STIQFADALA KAWLEYSNPR AVVMVIVQPE ERNMYDQHLL SSILREKHNI 

       310        320        330        340        350        360 
VVIRKTLAEV EKEGSVQEDE TLIVGGQAVA VVYFRSGYTP NDHPSESEWN ARLLIEESSA 

       370        380        390        400        410        420 
VKCPSIAYHL TGSKKIQQEL AKPGVLERFL DNKEDIAKLR KCFAGLWSLD DSEIVKQAIE 

       430        440        450        460        470        480 
KPGLFVMKPQ REGGGNNIYG DDVRENLLRL QKEGEEGNAA YILMQRIFPK VSNMFLVREG 

       490        500        510        520        530 
VYHKHQAISE LGVYGAYLRS KDEVIVNEQS GYLMRTKIAS SDEGGVAAGF GVLDSIYLI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS62654.
S68223.
T52565.
RefSeqNP_568495.2. NM_122620.3.
UniGeneAt.21515.
At.55036.

3D structure databases

ProteinModelPortalP46416.
SMRP46416. Positions 67-538.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid18071. 1 interaction.

Proteomic databases

PaxDbP46416.
PRIDEP46416.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G27380.1; AT5G27380.1; AT5G27380.
GeneID832797.
KEGGath:AT5G27380.

Organism-specific databases

TAIRAT5G27380.

Phylogenomic databases

eggNOGNOG329040.
HOGENOMHOG000172641.
InParanoidP46416.
KOK01920.
OMARIPANNA.
PhylomeDBP46416.

Enzyme and pathway databases

BioCycARA:AT5G27380-MONOMER.
UniPathwayUPA00142; UER00210.

Gene expression databases

GenevestigatorP46416.

Family and domain databases

Gene3D1.10.1080.10. 1 hit.
3.30.1490.50. 1 hit.
3.30.1490.80. 1 hit.
3.40.50.1760. 1 hit.
InterProIPR004887. 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]
PANTHERPTHR11130. PTHR11130. 1 hit.
PfamPF03917. GSH_synth_ATP. 1 hit.
PF03199. GSH_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF001558. GSHase. 1 hit.
SUPFAMSSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01986. glut_syn_euk. 1 hit.
ProtoNetSearch...

Other

PROP46416.

Entry information

Entry nameGSHB_ARATH
AccessionPrimary (citable) accession number: P46416
Secondary accession number(s): Q8H171, Q9SMW4, Q9SMW5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 30, 2003
Last modified: May 14, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names