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P46416

- GSHB_ARATH

UniProt

P46416 - GSHB_ARATH

Protein

Glutathione synthetase, chloroplastic

Gene

GSH2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (30 Apr 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Pathwayi

    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

    1. ATP binding Source: UniProtKB
    2. glutathione binding Source: UniProtKB
    3. glutathione synthase activity Source: TAIR
    4. magnesium ion binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. glutathione biosynthetic process Source: TAIR
    2. response to jasmonic acid Source: TAIR

    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.
    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: Chromosome 5

    Organism-specific databases

    TAIRiAT5G27380.

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. cytosol Source: TAIR

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP46416.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi18071. 1 interaction.

    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

    MGSGCSSLSY SSSSTCNATV FSISSSPSSS SSLKLNPSSF LFQNPKTLRN    50
    QSPLRCGRSF KMESQKPIFD LEKLDDEFVQ KLVYDALVWS SLHGLVVGDK 100
    SYQKSGNVPG VGLMHAPIAL LPTAFPEAYW KQACNVTPLF NELIDRVSLD 150
    GKFLQDSLSR TKKVDVFTSR LLDIHSKMLE RNKKEDIRLG LHRFDYMLDE 200
    ETNSLLQIEM NTISCSFPGL SRLVSQLHQS LLRSYGDQIG IDSERVPINT 250
    STIQFADALA KAWLEYSNPR AVVMVIVQPE ERNMYDQHLL SSILREKHNI 300
    VVIRKTLAEV EKEGSVQEDE TLIVGGQAVA VVYFRSGYTP NDHPSESEWN 350
    ARLLIEESSA VKCPSIAYHL TGSKKIQQEL AKPGVLERFL DNKEDIAKLR 400
    KCFAGLWSLD DSEIVKQAIE KPGLFVMKPQ REGGGNNIYG DDVRENLLRL 450
    QKEGEEGNAA YILMQRIFPK VSNMFLVREG VYHKHQAISE LGVYGAYLRS 500
    KDEVIVNEQS GYLMRTKIAS SDEGGVAAGF GVLDSIYLI 539
    Length:539
    Mass (Da):60,271
    Last modified:April 30, 2003 - v3
    Checksum:i2BFBF9A1D53E4A96
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171N → S in CAB51026. 1 PublicationCurated
    Sequence conflicti17 – 171N → S in CAB51027. 1 PublicationCurated
    Sequence conflicti26 – 261S → P in CAB51026. 1 PublicationCurated
    Sequence conflicti26 – 261S → P in CAB51027. 1 PublicationCurated
    Sequence conflicti30 – 345SSSLK → ELRQG in CAA90515. (PubMed:8521973)Curated
    Sequence conflicti52 – 521S → P1 PublicationCurated
    Sequence conflicti52 – 521S → P(PubMed:8612643)Curated
    Sequence conflicti96 – 961V → G in CAA58318. (PubMed:8612643)Curated
    Sequence conflicti101 – 1011S → T1 PublicationCurated
    Sequence conflicti101 – 1011S → T(PubMed:8612643)Curated
    Sequence conflicti124 – 1241A → G1 PublicationCurated
    Sequence conflicti124 – 1241A → G(PubMed:8612643)Curated
    Sequence conflicti135 – 1351N → D1 PublicationCurated
    Sequence conflicti135 – 1351N → D(PubMed:8612643)Curated
    Sequence conflicti151 – 1511G → S in CAB51027. 1 PublicationCurated
    Sequence conflicti199 – 1991D → G in CAB51027. 1 PublicationCurated
    Sequence conflicti219 – 2191G → A in CAA58318. (PubMed:8612643)Curated
    Sequence conflicti438 – 4381I → T in CAB51027. 1 PublicationCurated
    Sequence conflicti488 – 4881I → M in CAB51027. 1 PublicationCurated
    Sequence conflicti503 – 5031E → K1 PublicationCurated
    Sequence conflicti503 – 5031E → K(PubMed:8612643)Curated
    Sequence conflicti539 – 5391I → N1 PublicationCurated
    Sequence conflicti539 – 5391I → N(PubMed:8612643)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S62654.
    S68223.
    T52565.
    RefSeqi NP_568495.2. NM_122620.3.
    UniGenei At.21515.
    At.55036.

    3D structure databases

    ProteinModelPortali P46416.
    SMRi P46416. Positions 67-538.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 18071. 1 interaction.

    Proteomic databases

    PaxDbi P46416.
    PRIDEi P46416.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G27380.1 ; AT5G27380.1 ; AT5G27380 .
    GeneIDi 832797.
    KEGGi ath:AT5G27380.

    Organism-specific databases

    TAIRi AT5G27380.

    Phylogenomic databases

    eggNOGi NOG329040.
    HOGENOMi HOG000172641.
    InParanoidi P46416.
    KOi K01920.
    OMAi RIPANNA.
    PhylomeDBi P46416.

    Enzyme and pathway databases

    UniPathwayi UPA00142 ; UER00210 .
    BioCyci ARA:AT5G27380-MONOMER.

    Miscellaneous databases

    PROi P46416.

    Gene expression databases

    Genevestigatori P46416.

    Family and domain databases

    Gene3Di 1.10.1080.10. 1 hit.
    3.30.1490.50. 1 hit.
    3.30.1490.80. 1 hit.
    3.40.50.1760. 1 hit.
    InterProi IPR004887. 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 ]
    PANTHERi PTHR11130. PTHR11130. 1 hit.
    Pfami PF03917. GSH_synth_ATP. 1 hit.
    PF03199. GSH_synthase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001558. GSHase. 1 hit.
    SUPFAMi SSF52440. SSF52440. 1 hit.
    TIGRFAMsi TIGR01986. glut_syn_euk. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 122 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