PCS1_ARATH
ID PCS1_ARATH Reviewed; 485 AA.
AC Q9S7Z3; Q8W122; Q9M6R0; Q9XHP8; Q9ZPM2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glutathione gamma-glutamylcysteinyltransferase 1;
DE EC=2.3.2.15;
DE AltName: Full=Cadmium tolerance protein;
DE AltName: Full=Phytochelatin synthase 1;
DE Short=AtPCS1;
GN Name=PCS1; Synonyms=ARA8, CAD1; OrderedLocusNames=At5g44070;
GN ORFNames=MRH10.11, MRH10_18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY COPPER, LACK
RP OF INDUCTION BY CADMIUM, AND MUTAGENESIS OF ALA-59; CYS-91 AND TRP-190.
RX PubMed=10368185; DOI=10.2307/3870806;
RA Ha S.-B., Smith A.P., Howden R., Dietrich W.M., Bugg S., O'Connell M.J.,
RA Goldsbrough P.B., Cobbett C.S.;
RT "Phytochelatin synthase genes from Arabidopsis and the yeast
RT Schizosaccharomyces pombe.";
RL Plant Cell 11:1153-1164(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10369673; DOI=10.1093/emboj/18.12.3325;
RA Clemens S., Kim E.J., Neumann D., Schroeder J.I.;
RT "Tolerance to toxic metals by a gene family of phytochelatin synthases from
RT plants and yeast.";
RL EMBO J. 18:3325-3333(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ACTIVITY REGULATION.
RX PubMed=10359847; DOI=10.1073/pnas.96.12.7110;
RA Vatamaniuk O.K., Mari S., Lu Y.-P., Rea P.A.;
RT "AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro
RT reconstitution.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7110-7115(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Petrucco S., Bolchi A., Chiapponi C., Ottonello S.;
RT "Isolation of cadmium tolerance gene from Arabidopsis thaliana.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=12514032; DOI=10.1128/aem.69.1.490-494.2003;
RA Sauge-Merle S., Cuine S., Carrier P., Lecomte-Pradines C., Luu D.-T.,
RA Peltier G.;
RT "Enhanced toxic metal accumulation in engineered bacterial cells expressing
RT Arabidopsis thaliana phytochelatin synthase.";
RL Appl. Environ. Microbiol. 69:490-494(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [9]
RP FUNCTION.
RX PubMed=16593801; DOI=10.1073/pnas.84.2.439;
RA Grill E., Winnacker E.-L., Zenk M.H.;
RT "Phytochelatins, a class of heavy-metal-binding peptides from plants, are
RT functionally analogous to metallothioneins.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:439-443(1987).
RN [10]
RP FUNCTION.
RX PubMed=16594069; DOI=10.1073/pnas.86.18.6838;
RA Grill E., Loffler S., Winnacker E.-L., Zenk M.H.;
RT "Phytochelatins, the heavy-metal-binding peptides of plants, are
RT synthesized from glutathione by a specific gamma-glutamylcysteine
RT dipeptidyl transpeptidase (phytochelatin synthase).";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6838-6842(1989).
RN [11]
RP INDUCTION BY CADMIUM, AND DEVELOPMENTAL STAGE.
RX PubMed=12172853; DOI=10.1007/s00425-002-0821-6;
RA Lee S., Korban S.S.;
RT "Transcriptional regulation of Arabidopsis thaliana phytochelatin synthase
RT (AtPCS1) by cadmium during early stages of plant development.";
RL Planta 215:689-693(2002).
RN [12]
RP CHARACTERIZATION.
RX PubMed=14729665; DOI=10.1074/jbc.m314325200;
RA Ruotolo R., Peracchi A., Bolchi A., Infusini G., Amoresano A.,
RA Ottonello S.;
RT "Domain organization of phytochelatin synthase: functional properties of
RT truncated enzyme species identified by limited proteolysis.";
RL J. Biol. Chem. 279:14686-14693(2004).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF SER-21; CYS-56; CYS-90; CYS-91; CYS-109;
RP CYS-113 AND SER-164.
RX PubMed=15004013; DOI=10.1074/jbc.m313142200;
RA Vatamaniuk O.K., Mari S., Lang A., Chalasani S., Demkiv L.O., Rea P.A.;
RT "Phytochelatin synthase, a dipeptidyltransferase that undergoes multisite
RT acylation with gamma-glutamylcysteine during catalysis: stoichiometric and
RT site-directed mutagenic analysis of arabidopsis thaliana PCS1-catalyzed
RT phytochelatin synthesis.";
RL J. Biol. Chem. 279:22449-22460(2004).
RN [14]
RP CHARACTERIZATION, AND MUTAGENESIS OF TYR-7; SER-21; CYS-56; ASP-71; ASP-84;
RP ASP-89; CYS-90; CYS-91; CYS-109; CYS-113; THR-158; HIS-162; SER-164;
RP ASP-174; ASP-180; TYR-186; HIS-189; ASP-204 AND HIS-220.
RX PubMed=16714405; DOI=10.1104/pp.106.082131;
RA Romanyuk N.D., Rigden D.J., Vatamaniuk O.K., Lang A., Cahoon R.E.,
RA Jez J.M., Rea P.A.;
RT "Mutagenic definition of a papain-like catalytic triad, sufficiency of the
RT N-terminal domain for single-site core catalytic enzyme acylation, and C-
RT terminal domain for augmentative metal activation of a eukaryotic
RT phytochelatin synthase.";
RL Plant Physiol. 141:858-869(2006).
RN [15]
RP ACTIVITY REGULATION.
RC TISSUE=Root;
RX PubMed=16489135; DOI=10.1104/pp.105.073635;
RA Loscos J., Naya L., Ramos J., Clemente M.R., Matamoros M.A., Becana M.;
RT "A reassessment of substrate specificity and activation of phytochelatin
RT synthases from model plants by physiologically relevant metals.";
RL Plant Physiol. 140:1213-1221(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17253989; DOI=10.1111/j.1365-313x.2006.02993.x;
RA Blum R., Beck A., Korte A., Stengel A., Letzel T., Lendzian K., Grill E.;
RT "Function of phytochelatin synthase in catabolism of glutathione-
RT conjugates.";
RL Plant J. 49:740-749(2007).
CC -!- FUNCTION: Involved in the synthesis of phytochelatins (PC) and
CC homophytochelatins (hPC), the heavy-metal-binding peptides of plants.
CC Also involved in glutathione-conjugates degradation.
CC {ECO:0000269|PubMed:12514032, ECO:0000269|PubMed:15004013,
CC ECO:0000269|PubMed:16593801, ECO:0000269|PubMed:16594069,
CC ECO:0000269|PubMed:17253989}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly
CC + glycine; Xref=Rhea:RHEA:17917, Rhea:RHEA-COMP:12438, Rhea:RHEA-
CC COMP:12439, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:131728; EC=2.3.2.15; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00773};
CC -!- ACTIVITY REGULATION: Requires cadmium for activity. Also activated in
CC vitro or in heterologous system by Ag(+), Hg(+), Zn(2+), Cu(2+), Fe(2+)
CC or Fe(3+) ions, but not by Co(2+) or Ni(2+) ions.
CC {ECO:0000269|PubMed:10359847, ECO:0000269|PubMed:12514032,
CC ECO:0000269|PubMed:16489135}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC {ECO:0000269|PubMed:10368185, ECO:0000269|PubMed:10369673}.
CC -!- DEVELOPMENTAL STAGE: Expressed constitutively.
CC {ECO:0000269|PubMed:12172853}.
CC -!- INDUCTION: Induced by copper, and by cadmium during the early stages of
CC plant development. Gradual decrease of cadmium induction as plants
CC continue to grow, and by 15 day after germination, total loss of
CC induction. {ECO:0000269|PubMed:10368185, ECO:0000269|PubMed:12172853}.
CC -!- DOMAIN: The intermediate part (284-372) is important for enzyme
CC stabilization.
CC -!- DOMAIN: The C-terminal part (373-485) is required to determine enzyme
CC responsiveness to a broad range of heavy metals.
CC -!- DISRUPTION PHENOTYPE: Plants are highly sensitive to Cd (20- to 40-
CC fold) and AsO(4)(3-) ions, sensitive (eightfold) to Ag ions, slightly
CC sensitive (twofold) to Cu and Hg ions, and insensitive to Zn,
CC SeO(3)(2-) and Ni ions. {ECO:0000269|PubMed:17253989}.
CC -!- MISCELLANEOUS: Homoglutathione (hGSH) is a good acceptor, but a poor
CC donor, of gamma-glutamylcysteine units.
CC -!- SIMILARITY: Belongs to the phytochelatin synthase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00773}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD29446.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF135155; AAD41794.1; -; mRNA.
DR EMBL; AF093753; AAD50593.1; -; mRNA.
DR EMBL; AF085230; AAD16046.1; -; mRNA.
DR EMBL; AF085231; AAD29446.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF162689; AAF42805.1; -; mRNA.
DR EMBL; AF461180; AAL66747.1; -; mRNA.
DR EMBL; AB006703; BAB09067.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95055.1; -; Genomic_DNA.
DR EMBL; AY079384; AAL85115.1; -; mRNA.
DR EMBL; AY048257; AAK82519.1; -; mRNA.
DR EMBL; AY039951; AAK64055.1; -; mRNA.
DR RefSeq; NP_199220.1; NM_123774.4.
DR AlphaFoldDB; Q9S7Z3; -.
DR SMR; Q9S7Z3; -.
DR BioGRID; 19680; 3.
DR IntAct; Q9S7Z3; 1.
DR STRING; 3702.AT5G44070.1; -.
DR MEROPS; C83.002; -.
DR iPTMnet; Q9S7Z3; -.
DR PaxDb; Q9S7Z3; -.
DR PRIDE; Q9S7Z3; -.
DR ProteomicsDB; 236374; -.
DR EnsemblPlants; AT5G44070.1; AT5G44070.1; AT5G44070.
DR GeneID; 834430; -.
DR Gramene; AT5G44070.1; AT5G44070.1; AT5G44070.
DR KEGG; ath:AT5G44070; -.
DR Araport; AT5G44070; -.
DR TAIR; locus:2172497; AT5G44070.
DR eggNOG; KOG0632; Eukaryota.
DR HOGENOM; CLU_046059_0_0_1; -.
DR InParanoid; Q9S7Z3; -.
DR OMA; CKHESWA; -.
DR OrthoDB; 1279063at2759; -.
DR PhylomeDB; Q9S7Z3; -.
DR BioCyc; ARA:AT5G44070-MON; -.
DR BioCyc; MetaCyc:AT5G44070-MON; -.
DR BRENDA; 2.3.2.15; 399.
DR SABIO-RK; Q9S7Z3; -.
DR PRO; PR:Q9S7Z3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9S7Z3; baseline and differential.
DR Genevisible; Q9S7Z3; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0044604; F:ABC-type phytochelatin transporter activity; IDA:TAIR.
DR GO; GO:0015446; F:ATPase-coupled arsenite transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0046870; F:cadmium ion binding; IDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; IDA:TAIR.
DR GO; GO:0016756; F:glutathione gamma-glutamylcysteinyltransferase activity; IDA:TAIR.
DR GO; GO:0015700; P:arsenite transport; IDA:TAIR.
DR GO; GO:0098849; P:cellular detoxification of cadmium ion; IBA:GO_Central.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central.
DR GO; GO:0042344; P:indole glucosinolate catabolic process; IMP:TAIR.
DR GO; GO:0046938; P:phytochelatin biosynthetic process; IMP:TAIR.
DR GO; GO:0046685; P:response to arsenic-containing substance; IDA:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IDA:TAIR.
DR Gene3D; 3.90.70.30; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR040409; PCS-like.
DR InterPro; IPR007719; PCS_N.
DR InterPro; IPR038156; PCS_N_sf.
DR InterPro; IPR015407; Phytochelatin_synthase_C.
DR PANTHER; PTHR33447; PTHR33447; 1.
DR Pfam; PF05023; Phytochelatin; 1.
DR Pfam; PF09328; Phytochelatin_C; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51443; PCS; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cadmium; Copper; Metal-binding; Reference proteome;
KW Transferase; Zinc.
FT CHAIN 1..485
FT /note="Glutathione gamma-glutamylcysteinyltransferase 1"
FT /id="PRO_0000287210"
FT DOMAIN 1..221
FT /note="Peptidase C83"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
FT ACT_SITE 56
FT ACT_SITE 162
FT ACT_SITE 180
FT MUTAGEN 7
FT /note="Y->A: No effect."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 21
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:15004013,
FT ECO:0000269|PubMed:16714405"
FT MUTAGEN 56
FT /note="C->S,A: Loss of function."
FT /evidence="ECO:0000269|PubMed:15004013,
FT ECO:0000269|PubMed:16714405"
FT MUTAGEN 59
FT /note="A->V: In cad1-4; loss of function."
FT /evidence="ECO:0000269|PubMed:10368185"
FT MUTAGEN 71
FT /note="D->A: Decreased activity."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 84
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 89
FT /note="D->A: Slightly decreased activity."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 90
FT /note="C->S,A: Decreased activity."
FT /evidence="ECO:0000269|PubMed:15004013,
FT ECO:0000269|PubMed:16714405"
FT MUTAGEN 91
FT /note="C->S,A: No effect."
FT /evidence="ECO:0000269|PubMed:10368185,
FT ECO:0000269|PubMed:15004013, ECO:0000269|PubMed:16714405"
FT MUTAGEN 91
FT /note="C->Y: In cad1-1; loss of function."
FT /evidence="ECO:0000269|PubMed:10368185,
FT ECO:0000269|PubMed:15004013, ECO:0000269|PubMed:16714405"
FT MUTAGEN 109
FT /note="C->S,A: No effect."
FT /evidence="ECO:0000269|PubMed:15004013,
FT ECO:0000269|PubMed:16714405"
FT MUTAGEN 113
FT /note="C->S,A: No effect."
FT /evidence="ECO:0000269|PubMed:15004013,
FT ECO:0000269|PubMed:16714405"
FT MUTAGEN 158
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 162
FT /note="H->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 164
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:15004013,
FT ECO:0000269|PubMed:16714405"
FT MUTAGEN 174
FT /note="D->A: Decreased activity."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 180
FT /note="D->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 186
FT /note="Y->A: No effect."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 189
FT /note="H->A: Decreased activity."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 190
FT /note="W->C: In cad1-3; loss of function."
FT /evidence="ECO:0000269|PubMed:10368185"
FT MUTAGEN 204
FT /note="D->A: Decreased activity."
FT /evidence="ECO:0000269|PubMed:16714405"
FT MUTAGEN 220
FT /note="H->A: Decreased activity."
FT /evidence="ECO:0000269|PubMed:16714405"
FT CONFLICT 153
FT /note="G -> S (in Ref. 3; AAD16046)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="T -> N (in Ref. 3; AAD16046)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="E -> A (in Ref. 5; AAL66747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 54475 MW; 27204B38310884D6 CRC64;
MAMASLYRRS LPSPPAIDFS SAEGKLIFNE ALQKGTMEGF FRLISYFQTQ SEPAYCGLAS
LSVVLNALSI DPGRKWKGPW RWFDESMLDC CEPLEVVKEK GISFGKVVCL AHCSGAKVEA
FRTSQSTIDD FRKFVVKCTS SENCHMISTY HRGVFKQTGT GHFSPIGGYN AERDMALILD
VARFKYPPHW VPLKLLWEAM DSIDQSTGKR RGFMLISRPH REPGLLYTLS CKDESWIEIA
KYLKEDVPRL VSSQHVDSVE KIISVVFKSL PSNFNQFIRW VAEIRITEDS NQNLSAEEKS
RLKLKQLVLK EVHETELFKH INKFLSTVGY EDSLTYAAAK ACCQGAEILS GSPSKEFCCR
ETCVKCIKGP DDSEGTVVTG VVVRDGNEQK VDLLVPSTQT ECECGPEATY PAGNDVFTAL
LLALPPQTWS GIKDQALMHE MKQLISMASL PTLLQEEVLH LRRQLQLLKR CQENKEEDDL
AAPAY
