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Q9S7Z3 (PCS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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 gamma-glutamylcysteinyltransferase 1

EC=2.3.2.15
Alternative name(s):
Cadmium tolerance protein
Phytochelatin synthase 1
Short name=AtPCS1
Gene names
Name:PCS1
Synonyms:ARA8, CAD1
Ordered Locus Names:At5g44070
ORF Names:MRH10.11, MRH10_18
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants. Also involved in glutathione-conjugates degradation. Ref.5 Ref.9 Ref.10 Ref.13 Ref.16

Catalytic activity

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

Enzyme regulation

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. Ref.3 Ref.5 Ref.15

Tissue specificity

Expressed in roots and shoots. Ref.1 Ref.2

Developmental stage

Expressed constitutively. Ref.11

Induction

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. Ref.1 Ref.3 Ref.5 Ref.11 Ref.15

Domain

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.

Disruption phenotype

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. Ref.16

Miscellaneous

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

Sequence similarities

Belongs to the phytochelatin synthase family.

Contains 1 peptidase C83 domain.

Sequence caution

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

Ontologies

Keywords
   LigandCadmium
Copper
Metal-binding
Zinc
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarsenite transport

Inferred from direct assay PubMed 21078981. Source: TAIR

cation transport

Inferred from direct assay PubMed 21078981. Source: GOC

defense response by callose deposition in cell wall

Inferred from mutant phenotype PubMed 19095898. Source: TAIR

defense response to bacterium

Inferred from mutant phenotype PubMed 19095898. Source: TAIR

indole glucosinolate catabolic process

Inferred from mutant phenotype PubMed 19095898. Source: TAIR

phytochelatin biosynthetic process

Inferred from mutant phenotype Ref.16. Source: TAIR

phytochelatin transmembrane transport

Inferred from direct assay PubMed 21078981. Source: GOC

response to arsenic-containing substance

Inferred from direct assay PubMed 17390107. Source: TAIR

response to cadmium ion

Inferred from direct assay PubMed 17390107. Source: TAIR

   Cellular_componentcytosol

Inferred from direct assay PubMed 20304971PubMed 21166475. Source: TAIR

   Molecular_functionarsenite-transmembrane transporting ATPase activity

Inferred from direct assay PubMed 21078981. Source: TAIR

cadmium ion binding

Inferred from direct assay PubMed 7770518. Source: TAIR

copper ion binding

Inferred from direct assay PubMed 7770517. Source: TAIR

glutathione gamma-glutamylcysteinyltransferase activity

Inferred from direct assay Ref.15. Source: TAIR

phytochelatin transmembrane transporter activity

Inferred from direct assay PubMed 21078981. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Glutathione gamma-glutamylcysteinyltransferase 1
PRO_0000287210

Regions

Domain1 – 221221Peptidase C83

Sites

Active site561
Active site1621
Active site1801

Experimental info

Mutagenesis71Y → A: No effect. Ref.14
Mutagenesis211S → A: No effect. Ref.13 Ref.14
Mutagenesis561C → S or A: Loss of function. Ref.13 Ref.14
Mutagenesis591A → V in cad1-4; loss of function. Ref.1
Mutagenesis711D → A: Decreased activity. Ref.14
Mutagenesis841D → A: No effect. Ref.14
Mutagenesis891D → A: Slightly decreased activity. Ref.14
Mutagenesis901C → S or A: Decreased activity. Ref.13 Ref.14
Mutagenesis911C → S or A: No effect. Ref.1 Ref.13 Ref.14
Mutagenesis911C → Y in cad1-1; loss of function. Ref.1 Ref.13 Ref.14
Mutagenesis1091C → S or A: No effect. Ref.13 Ref.14
Mutagenesis1131C → S or A: No effect. Ref.13 Ref.14
Mutagenesis1581T → A: No effect. Ref.14
Mutagenesis1621H → A: Loss of function. Ref.14
Mutagenesis1641S → A: No effect. Ref.13 Ref.14
Mutagenesis1741D → A: Decreased activity. Ref.14
Mutagenesis1801D → A: Loss of function. Ref.14
Mutagenesis1861Y → A: No effect. Ref.14
Mutagenesis1891H → A: Decreased activity. Ref.14
Mutagenesis1901W → C in cad1-3; loss of function. Ref.1
Mutagenesis2041D → A: Decreased activity. Ref.14
Mutagenesis2201H → A: Decreased activity. Ref.14
Sequence conflict1531G → S in AAD16046. Ref.3
Sequence conflict1601T → N in AAD16046. Ref.3
Sequence conflict2981E → A in AAL66747. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9S7Z3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 27204B38310884D6

FASTA48554,475
        10         20         30         40         50         60 
MAMASLYRRS LPSPPAIDFS SAEGKLIFNE ALQKGTMEGF FRLISYFQTQ SEPAYCGLAS 

        70         80         90        100        110        120 
LSVVLNALSI DPGRKWKGPW RWFDESMLDC CEPLEVVKEK GISFGKVVCL AHCSGAKVEA 

       130        140        150        160        170        180 
FRTSQSTIDD FRKFVVKCTS SENCHMISTY HRGVFKQTGT GHFSPIGGYN AERDMALILD 

       190        200        210        220        230        240 
VARFKYPPHW VPLKLLWEAM DSIDQSTGKR RGFMLISRPH REPGLLYTLS CKDESWIEIA 

       250        260        270        280        290        300 
KYLKEDVPRL VSSQHVDSVE KIISVVFKSL PSNFNQFIRW VAEIRITEDS NQNLSAEEKS 

       310        320        330        340        350        360 
RLKLKQLVLK EVHETELFKH INKFLSTVGY EDSLTYAAAK ACCQGAEILS GSPSKEFCCR 

       370        380        390        400        410        420 
ETCVKCIKGP DDSEGTVVTG VVVRDGNEQK VDLLVPSTQT ECECGPEATY PAGNDVFTAL 

       430        440        450        460        470        480 
LLALPPQTWS GIKDQALMHE MKQLISMASL PTLLQEEVLH LRRQLQLLKR CQENKEEDDL 


AAPAY 

« Hide

References

« Hide 'large scale' references
[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. 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].
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_199220.1. NM_123774.3.
UniGeneAt.7305.

3D structure databases

ProteinModelPortalQ9S7Z3.
SMRQ9S7Z3. Positions 11-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid19680. 2 interactions.
IntActQ9S7Z3. 1 interaction.
STRING3702.AT5G44070.1-P.

Protein family/group databases

MEROPSC83.002.

Proteomic databases

PaxDbQ9S7Z3.
PRIDEQ9S7Z3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G44070.1; AT5G44070.1; AT5G44070.
GeneID834430.
KEGGath:AT5G44070.

Organism-specific databases

TAIRAT5G44070.

Phylogenomic databases

eggNOGNOG76926.
HOGENOMHOG000241441.
InParanoidQ9S7Z3.
KOK05941.
OMALLWEAMD.
PhylomeDBQ9S7Z3.
ProtClustDBCLSN2679907.

Enzyme and pathway databases

BioCycARA:AT5G44070-MONOMER.
MetaCyc:AT5G44070-MONOMER.

Gene expression databases

GenevestigatorQ9S7Z3.

Family and domain databases

InterProIPR007719. Phytochelatin_synthase.
IPR015407. Phytochelatin_synthase_C.
[Graphical view]
PfamPF05023. Phytochelatin. 1 hit.
PF09328. Phytochelatin_C. 1 hit.
[Graphical view]
PROSITEPS51443. PCS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePCS1_ARATH
AccessionPrimary (citable) accession number: Q9S7Z3
Secondary accession number(s): Q8W122 expand/collapse secondary AC list , Q9M6R0, Q9XHP8, Q9ZPM2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 78 of the entry and version 1 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

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names