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Q9S7Z3

- PCS1_ARATH

UniProt

Q9S7Z3 - PCS1_ARATH

Protein

Glutathione gamma-glutamylcysteinyltransferase 1

Gene

PCS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants. Also involved in glutathione-conjugates degradation.5 Publications

    Catalytic activityi

    Glutathione + (Glu(-Cys))(n)-Gly = Gly + (Glu(-Cys))(n+1)-Gly.PROSITE-ProRule annotation

    Enzyme regulationi

    Requires cadmium for activity. Also activated in vitro or in heterologous system by Ag+, Hg+, Zn2+, Cu2+, Fe2+ or Fe3+ ions, but not by Co2+ or Ni2+ ions.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei56 – 561
    Active sitei162 – 1621
    Active sitei180 – 1801

    GO - Molecular functioni

    1. arsenite-transmembrane transporting ATPase activity Source: TAIR
    2. cadmium ion binding Source: TAIR
    3. copper ion binding Source: TAIR
    4. glutathione gamma-glutamylcysteinyltransferase activity Source: TAIR
    5. phytochelatin transmembrane transporter activity Source: TAIR

    GO - Biological processi

    1. arsenite transport Source: TAIR
    2. cation transport Source: GOC
    3. defense response by callose deposition in cell wall Source: TAIR
    4. defense response to bacterium Source: TAIR
    5. indole glucosinolate catabolic process Source: TAIR
    6. phytochelatin biosynthetic process Source: TAIR
    7. phytochelatin transmembrane transport Source: GOC
    8. response to arsenic-containing substance Source: TAIR
    9. response to cadmium ion Source: TAIR

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Cadmium, Copper, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciARA:AT5G44070-MONOMER.
    MetaCyc:AT5G44070-MONOMER.

    Protein family/group databases

    MEROPSiC83.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione gamma-glutamylcysteinyltransferase 1 (EC:2.3.2.15)
    Alternative name(s):
    Cadmium tolerance protein
    Phytochelatin synthase 1
    Short name:
    AtPCS1
    Gene namesi
    Name:PCS1
    Synonyms:ARA8, CAD1
    Ordered Locus Names:At5g44070
    ORF Names:MRH10.11, MRH10_18
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G44070.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR

    Pathology & Biotechi

    Disruption phenotypei

    Plants are highly sensitive to Cd (20- to 40-fold) and AsO43- ions, sensitive (eightfold) to Ag ions, slightly sensitive (twofold) to Cu and Hg ions, and insensitive to Zn, SeO32- and Ni ions.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71Y → A: No effect. 1 Publication
    Mutagenesisi21 – 211S → A: No effect. 2 Publications
    Mutagenesisi56 – 561C → S or A: Loss of function. 2 Publications
    Mutagenesisi59 – 591A → V in cad1-4; loss of function. 1 Publication
    Mutagenesisi71 – 711D → A: Decreased activity. 1 Publication
    Mutagenesisi84 – 841D → A: No effect. 1 Publication
    Mutagenesisi89 – 891D → A: Slightly decreased activity. 1 Publication
    Mutagenesisi90 – 901C → S or A: Decreased activity. 2 Publications
    Mutagenesisi91 – 911C → S or A: No effect. 3 Publications
    Mutagenesisi91 – 911C → Y in cad1-1; loss of function. 3 Publications
    Mutagenesisi109 – 1091C → S or A: No effect. 2 Publications
    Mutagenesisi113 – 1131C → S or A: No effect. 2 Publications
    Mutagenesisi158 – 1581T → A: No effect. 1 Publication
    Mutagenesisi162 – 1621H → A: Loss of function. 1 Publication
    Mutagenesisi164 – 1641S → A: No effect. 2 Publications
    Mutagenesisi174 – 1741D → A: Decreased activity. 1 Publication
    Mutagenesisi180 – 1801D → A: Loss of function. 1 Publication
    Mutagenesisi186 – 1861Y → A: No effect. 1 Publication
    Mutagenesisi189 – 1891H → A: Decreased activity. 1 Publication
    Mutagenesisi190 – 1901W → C in cad1-3; loss of function. 1 Publication
    Mutagenesisi204 – 2041D → A: Decreased activity. 1 Publication
    Mutagenesisi220 – 2201H → A: Decreased activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 485485Glutathione gamma-glutamylcysteinyltransferase 1PRO_0000287210Add
    BLAST

    Proteomic databases

    PaxDbiQ9S7Z3.
    PRIDEiQ9S7Z3.

    Expressioni

    Tissue specificityi

    Expressed in roots and shoots.2 Publications

    Developmental stagei

    Expressed constitutively.1 Publication

    Inductioni

    Induced by copper, and by cadmium during the early stages of plant development. Gradual decrease of cadmium induction as plants continue to grow, and by 15 day after germination, total loss of induction.2 Publications

    Gene expression databases

    GenevestigatoriQ9S7Z3.

    Interactioni

    Protein-protein interaction databases

    BioGridi19680. 2 interactions.
    IntActiQ9S7Z3. 1 interaction.
    STRINGi3702.AT5G44070.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9S7Z3.
    SMRiQ9S7Z3. Positions 11-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 221221Peptidase C83PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The intermediate part (284-372) is important for enzyme stabilization.
    The C-terminal part (373-485) is required to determine enzyme responsiveness to a broad range of heavy metals.

    Sequence similaritiesi

    Belongs to the phytochelatin synthase family.PROSITE-ProRule annotation
    Contains 1 peptidase C83 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG76926.
    HOGENOMiHOG000241441.
    InParanoidiQ9S7Z3.
    KOiK05941.
    OMAiCEPLEKV.
    PhylomeDBiQ9S7Z3.

    Family and domain databases

    InterProiIPR007719. Phytochelatin_synthase.
    IPR015407. Phytochelatin_synthase_C.
    [Graphical view]
    PfamiPF05023. Phytochelatin. 1 hit.
    PF09328. Phytochelatin_C. 1 hit.
    [Graphical view]
    PROSITEiPS51443. PCS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9S7Z3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMASLYRRS LPSPPAIDFS SAEGKLIFNE ALQKGTMEGF FRLISYFQTQ    50
    SEPAYCGLAS LSVVLNALSI DPGRKWKGPW RWFDESMLDC CEPLEVVKEK 100
    GISFGKVVCL AHCSGAKVEA FRTSQSTIDD FRKFVVKCTS SENCHMISTY 150
    HRGVFKQTGT GHFSPIGGYN AERDMALILD VARFKYPPHW VPLKLLWEAM 200
    DSIDQSTGKR RGFMLISRPH REPGLLYTLS CKDESWIEIA KYLKEDVPRL 250
    VSSQHVDSVE KIISVVFKSL PSNFNQFIRW VAEIRITEDS NQNLSAEEKS 300
    RLKLKQLVLK EVHETELFKH INKFLSTVGY EDSLTYAAAK ACCQGAEILS 350
    GSPSKEFCCR ETCVKCIKGP DDSEGTVVTG VVVRDGNEQK VDLLVPSTQT 400
    ECECGPEATY PAGNDVFTAL LLALPPQTWS GIKDQALMHE MKQLISMASL 450
    PTLLQEEVLH LRRQLQLLKR CQENKEEDDL AAPAY 485
    Length:485
    Mass (Da):54,475
    Last modified:May 1, 2000 - v1
    Checksum:i27204B38310884D6
    GO

    Sequence cautioni

    The sequence AAD29446.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531G → S in AAD16046. (PubMed:10359847)Curated
    Sequence conflicti160 – 1601T → N in AAD16046. (PubMed:10359847)Curated
    Sequence conflicti298 – 2981E → A in AAL66747. (PubMed:12514032)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF135155 mRNA. Translation: AAD41794.1.
    AF093753 mRNA. Translation: AAD50593.1.
    AF085230 mRNA. Translation: AAD16046.1.
    AF085231 Genomic DNA. Translation: AAD29446.1. Sequence problems.
    AF162689 mRNA. Translation: AAF42805.1.
    AF461180 mRNA. Translation: AAL66747.1.
    AB006703 Genomic DNA. Translation: BAB09067.1.
    CP002688 Genomic DNA. Translation: AED95055.1.
    AY079384 mRNA. Translation: AAL85115.1.
    AY048257 mRNA. Translation: AAK82519.1.
    AY039951 mRNA. Translation: AAK64055.1.
    RefSeqiNP_199220.1. NM_123774.3.
    UniGeneiAt.7305.

    Genome annotation databases

    EnsemblPlantsiAT5G44070.1; AT5G44070.1; AT5G44070.
    GeneIDi834430.
    KEGGiath:AT5G44070.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF135155 mRNA. Translation: AAD41794.1 .
    AF093753 mRNA. Translation: AAD50593.1 .
    AF085230 mRNA. Translation: AAD16046.1 .
    AF085231 Genomic DNA. Translation: AAD29446.1 . Sequence problems.
    AF162689 mRNA. Translation: AAF42805.1 .
    AF461180 mRNA. Translation: AAL66747.1 .
    AB006703 Genomic DNA. Translation: BAB09067.1 .
    CP002688 Genomic DNA. Translation: AED95055.1 .
    AY079384 mRNA. Translation: AAL85115.1 .
    AY048257 mRNA. Translation: AAK82519.1 .
    AY039951 mRNA. Translation: AAK64055.1 .
    RefSeqi NP_199220.1. NM_123774.3.
    UniGenei At.7305.

    3D structure databases

    ProteinModelPortali Q9S7Z3.
    SMRi Q9S7Z3. Positions 11-217.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 19680. 2 interactions.
    IntActi Q9S7Z3. 1 interaction.
    STRINGi 3702.AT5G44070.1-P.

    Protein family/group databases

    MEROPSi C83.002.

    Proteomic databases

    PaxDbi Q9S7Z3.
    PRIDEi Q9S7Z3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G44070.1 ; AT5G44070.1 ; AT5G44070 .
    GeneIDi 834430.
    KEGGi ath:AT5G44070.

    Organism-specific databases

    TAIRi AT5G44070.

    Phylogenomic databases

    eggNOGi NOG76926.
    HOGENOMi HOG000241441.
    InParanoidi Q9S7Z3.
    KOi K05941.
    OMAi CEPLEKV.
    PhylomeDBi Q9S7Z3.

    Enzyme and pathway databases

    BioCyci ARA:AT5G44070-MONOMER.
    MetaCyc:AT5G44070-MONOMER.

    Gene expression databases

    Genevestigatori Q9S7Z3.

    Family and domain databases

    InterProi IPR007719. Phytochelatin_synthase.
    IPR015407. Phytochelatin_synthase_C.
    [Graphical view ]
    Pfami PF05023. Phytochelatin. 1 hit.
    PF09328. Phytochelatin_C. 1 hit.
    [Graphical view ]
    PROSITEi PS51443. PCS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Phytochelatin synthase genes from Arabidopsis and the yeast Schizosaccharomyces pombe."
      Ha S.-B., Smith A.P., Howden R., Dietrich W.M., Bugg S., O'Connell M.J., Goldsbrough P.B., Cobbett C.S.
      Plant Cell 11:1153-1164(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY COPPER, LACK OF INDUCTION BY CADMIUM, MUTAGENESIS OF ALA-59; CYS-91 AND TRP-190.
    2. "Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast."
      Clemens S., Kim E.J., Neumann D., Schroeder J.I.
      EMBO J. 18:3325-3333(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    3. "AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution."
      Vatamaniuk O.K., Mari S., Lu Y.-P., Rea P.A.
      Proc. Natl. Acad. Sci. U.S.A. 96:7110-7115(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ENZYME REGULATION.
    4. "Isolation of cadmium tolerance gene from Arabidopsis thaliana."
      Petrucco S., Bolchi A., Chiapponi C., Ottonello S.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Enhanced toxic metal accumulation in engineered bacterial cells expressing Arabidopsis thaliana phytochelatin synthase."
      Sauge-Merle S., Cuine S., Carrier P., Lecomte-Pradines C., Luu D.-T., Peltier G.
      Appl. Environ. Microbiol. 69:490-494(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION.
    6. "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones."
      Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S.
      DNA Res. 4:291-300(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    7. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    8. "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].
      Strain: cv. Columbia.
    9. "Phytochelatins, a class of heavy-metal-binding peptides from plants, are functionally analogous to metallothioneins."
      Grill E., Winnacker E.-L., Zenk M.H.
      Proc. Natl. Acad. Sci. U.S.A. 84:439-443(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)."
      Grill E., Loffler S., Winnacker E.-L., Zenk M.H.
      Proc. Natl. Acad. Sci. U.S.A. 86:6838-6842(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Transcriptional regulation of Arabidopsis thaliana phytochelatin synthase (AtPCS1) by cadmium during early stages of plant development."
      Lee S., Korban S.S.
      Planta 215:689-693(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY CADMIUM, DEVELOPMENTAL STAGE.
    12. "Domain organization of phytochelatin synthase: functional properties of truncated enzyme species identified by limited proteolysis."
      Ruotolo R., Peracchi A., Bolchi A., Infusini G., Amoresano A., Ottonello S.
      J. Biol. Chem. 279:14686-14693(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    13. "Phytochelatin synthase, a dipeptidyltransferase that undergoes multisite acylation with gamma-glutamylcysteine during catalysis: stoichiometric and site-directed mutagenic analysis of arabidopsis thaliana PCS1-catalyzed phytochelatin synthesis."
      Vatamaniuk O.K., Mari S., Lang A., Chalasani S., Demkiv L.O., Rea P.A.
      J. Biol. Chem. 279:22449-22460(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-21; CYS-56; CYS-90; CYS-91; CYS-109; CYS-113 AND SER-164.
    14. "Mutagenic definition of a papain-like catalytic triad, sufficiency of the N-terminal domain for single-site core catalytic enzyme acylation, and C-terminal domain for augmentative metal activation of a eukaryotic phytochelatin synthase."
      Romanyuk N.D., Rigden D.J., Vatamaniuk O.K., Lang A., Cahoon R.E., Jez J.M., Rea P.A.
      Plant Physiol. 141:858-869(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF TRY-7; SER-21; CYS-56; ASP-71; ASP-84; ASP-89; CYS-90; CYS-91; CYS-109; CYS-113; THR-158; HIS-162; SER-164; ASP-174; ASP-180; TYR-186; HIS-189; ASP-204 AND HIS-220.
    15. "A reassessment of substrate specificity and activation of phytochelatin synthases from model plants by physiologically relevant metals."
      Loscos J., Naya L., Ramos J., Clemente M.R., Matamoros M.A., Becana M.
      Plant Physiol. 140:1213-1221(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
      Tissue: Root.
    16. "Function of phytochelatin synthase in catabolism of glutathione-conjugates."
      Blum R., Beck A., Korte A., Stengel A., Letzel T., Lendzian K., Grill E.
      Plant J. 49:740-749(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiPCS1_ARATH
    AccessioniPrimary (citable) accession number: Q9S7Z3
    Secondary accession number(s): Q8W122
    , Q9M6R0, Q9XHP8, Q9ZPM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 80 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Homoglutathione (hGSH) is a good acceptor, but a poor donor, of gamma-glutamylcysteine units.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3