ID   PCS1_WHEAT              Reviewed;         500 AA.
AC   Q9SWW5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 82.
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   AltName: Full=TaPCS1;
GN   Name=PCS1;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY CADMIUM, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Root;
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).
CC   -!- FUNCTION: Involved in the synthesis of phytochelatins (PC) and
CC       homophytochelatins (hPC), the heavy-metal-binding peptides of plants.
CC       {ECO:0000269|PubMed:10369673}.
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. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC       {ECO:0000269|PubMed:10369673}.
CC   -!- INDUCTION: 5- to 10-fold by 100 uM cadmium.
CC       {ECO:0000269|PubMed:10369673}.
CC   -!- SIMILARITY: Belongs to the phytochelatin synthase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00773}.
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DR   EMBL; AF093752; AAD50592.1; -; mRNA.
DR   AlphaFoldDB; Q9SWW5; -.
DR   SMR; Q9SWW5; -.
DR   STRING; 4565.Q9SWW5; -.
DR   PaxDb; 4565-Traes_7DS_E848BACC2-1; -.
DR   eggNOG; KOG0632; Eukaryota.
DR   BioCyc; MetaCyc:MONOMER-16321; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q9SWW5; baseline and differential.
DR   GO; GO:0016756; F:glutathione gamma-glutamylcysteinyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0098849; P:cellular detoxification of cadmium ion; IBA:GO_Central.
DR   GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central.
DR   GO; GO:0046938; P:phytochelatin biosynthetic process; IBA:GO_Central.
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:SF2; GLUTATHIONE GAMMA-GLUTAMYLCYSTEINYLTRANSFERASE; 1.
DR   Pfam; PF05023; Phytochelatin; 1.
DR   Pfam; PF09328; Phytochelatin_C; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS51443; PCS; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Cadmium; Metal-binding; Reference proteome; Transferase.
FT   CHAIN           1..500
FT                   /note="Glutathione gamma-glutamylcysteinyltransferase 1"
FT                   /id="PRO_0000287212"
FT   DOMAIN          1..221
FT                   /note="Peptidase C83"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
SQ   SEQUENCE   500 AA;  55045 MW;  530B8B55FC46B008 CRC64;
     MEVASLYRRV LPSPPAVEFA SAEGKRLFAE ALQGGTMEGF FNLISYFQTQ SEPAFCGLAS
     LSVVLNALAI DPGRPWKGPW RWFDESMLDC CEPLHKVKAE GITFGKVVCL AHCAGARVQS
     FRADQTTIHD FRAHLTRCAS SQDCHLISSY HRSPFKQTGT GHFSPIGGYH AEKDMALILD
     VARFKYPPHW VPLTLLWDAM NTTDEATGLL RGFMLVSRRS SAPSLLYTVS CGHGSWKSMA
     KYCVEDVPNL LKDESLDNVT TLLSRLVESL PANAGDLIKC VIEVRRKEEG ESSLSKEEKE
     RLFLKEKVLQ QIRDTDLFRV VHELQYPKGL CGSCSSSSDE DSLAEIAATV CCQGAAFLSG
     NLVSRDGFCC RETCIKCIEA NGDGLKTVIS GTVVSKGNEQ AVDLLLPTSS SKTSLCNSNL
     KSKIVKYPSS TDVLTVLLLV LQPNTWLGIK DENVKAEFQS LVSTDNLPDL LKQEILHLRR
     QLHYLAGCKG QEACQEPPSP
//