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 27-MAR-2024, entry version 128. 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=10.1105/tpc.11.6.1153; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 2. DR STRING; 3702.Q9S7Z3; -. DR MEROPS; C83.002; -. DR iPTMnet; Q9S7Z3; -. DR PaxDb; 3702-AT5G44070-1; -. 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; AT5G44070; CAD1. DR eggNOG; KOG0632; Eukaryota. DR HOGENOM; CLU_046059_0_0_1; -. DR InParanoid; Q9S7Z3; -. DR OMA; CKHESWA; -. DR OrthoDB; 5903at2759; -. DR PhylomeDB; Q9S7Z3; -. DR BioCyc; ARA:AT5G44070-MONOMER; -. DR BioCyc; MetaCyc:AT5G44070-MONOMER; -. 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 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: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: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; Phytochelatin synthase, N-terminal domain; 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; GLUTATHIONE GAMMA-GLUTAMYLCYSTEINYLTRANSFERASE; 1. DR PANTHER; PTHR33447:SF23; GLUTATHIONE GAMMA-GLUTAMYLCYSTEINYLTRANSFERASE 1; 1. DR Pfam; PF05023; Phytochelatin; 1. DR Pfam; PF09328; Phytochelatin_C; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR PROSITE; PS51443; PCS; 1. DR Genevisible; Q9S7Z3; AT. 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 //