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Protein

Glutathione gamma-glutamylcysteinyltransferase 1

Gene

PCS1

Organism
Lotus japonicus (Lotus corniculatus var. japonicus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants.1 Publication

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 by Zn2+, Cu2+, Fe2+ or Fe3+ ions, but not by Co2+ or Ni2+ ions.1 Publication

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Cadmium, Copper, Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16320.
BRENDAi2.3.2.15. 3076.

Protein family/group databases

MEROPSiC83.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione gamma-glutamylcysteinyltransferase 1 (EC:2.3.2.15)
Alternative name(s):
LjPCS1-8R
Phytochelatin synthase 1
Gene namesi
Name:PCS1
OrganismiLotus japonicus (Lotus corniculatus var. japonicus)
Taxonomic identifieri34305 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeLoteaeLotus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Glutathione gamma-glutamylcysteinyltransferase 1PRO_0000287213Add
BLAST

Expressioni

Tissue specificityi

Expressed in roots, nodules and leaves.1 Publication

Inductioni

By cadmium.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ2TSC7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

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.

Q2TSC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMAGLYRRL LPSPPAVDFA SSQGKQLFLE AVQNGTMESF YRLVSYFQTQ
60 70 80 90 100
SEPAFCGLAS LSMVLNALAI DPGRKWKGPW RWFDESMLDC CEPLDKIKAR
110 120 130 140 150
GISFGKLVCL AHCAGAKVEA FHASHSSIDH FRKYVMKCST SDDCHVISSY
160 170 180 190 200
HREALKQTGT GHFSPIGGYH AGKDMALILD VARFKYPPHW IPLTHLWEGM
210 220 230 240 250
NYVDESTGKT RGFMLISRPH REPGMLYTLS CKHESWNSIA KFLIDDIPFL
260 270 280 290 300
LTSEDVKDIC KVLSVIVTSL PSNFEEFIKW VAEIRRGEDG SPSLSVEEKA
310 320 330 340 350
RLSVKEEILK QVQRTGLFKH VASFLSHSCS GHTPTSGDRD TFPVIAASVC
360 370 380 390 400
CQGAEILGGK ISSSAEYCCR ETCMKCWKAE DDKPIRMVCG TVVNGNTEQG
410 420 430 440 450
VDVLIPSSCG KLSCTCSSTT KSIRKHPAST DVLTVLLLSL PTSTWAGIAD
460 470 480 490 500
EKLLSEIHDL VSIENLPALL QEEVLHLRRQ LHILKRCQEG KVDEDLGVPL

S
Length:501
Mass (Da):55,520
Last modified:January 24, 2006 - v1
Checksum:iEC92820F194A0482
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY633847 mRNA. Translation: AAT80342.1.
AY270030 Genomic DNA. Translation: AAQ01752.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY633847 mRNA. Translation: AAT80342.1.
AY270030 Genomic DNA. Translation: AAQ01752.1.

3D structure databases

ProteinModelPortaliQ2TSC7.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC83.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16320.
BRENDAi2.3.2.15. 3076.

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]
ProtoNetiSearch...

Publicationsi

  1. "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: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION.
    Tissue: Root.
  2. "Phytochelatin synthases of the model legume Lotus japonicus. A small multigene family with differential response to cadmium and alternatively spliced variants."
    Ramos J., Clemente M.R., Naya L., Loscos J., Perez-Rontome C., Sato S., Tabata S., Becana M.
    Plant Physiol. 143:1110-1118(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Miyakojima MG-20.

Entry informationi

Entry nameiPCS1_LOTJA
AccessioniPrimary (citable) accession number: Q2TSC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: January 24, 2006
Last modified: April 1, 2015
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

In roots, Cd2+ and Zn2+ induce preferentially homophytochelatin (hPC) synthesis whereas Cu2+ has a major effect on phytochelatin (PC) synthesis.
Homoglutathione (hGSH) is a good acceptor, but a poor donor, of gamma-glutamylcysteine units.

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.