SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9S7Z3

- PCS1_ARATH

UniProt

Q9S7Z3 - PCS1_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutathione gamma-glutamylcysteinyltransferase 1

Gene
PCS1, ARA8, CAD1, At5g44070, MRH10.11, MRH10_18
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

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
Complete GO annotation...

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
Complete GO annotation...

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.5 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 221221Peptidase C83Add
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

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531G → S in AAD16046. 1 Publication
Sequence conflicti160 – 1601T → N in AAD16046. 1 Publication
Sequence conflicti298 – 2981E → A in AAL66747. 1 Publication

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 79 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

Similar proteinsi