ID   PCS1_LOTJA              Reviewed;         501 AA.
AC   Q2TSC7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Glutathione gamma-glutamylcysteinyltransferase 1;
DE            EC=2.3.2.15;
DE   AltName: Full=LjPCS1-8R;
DE   AltName: Full=Phytochelatin synthase 1;
GN   Name=PCS1;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND 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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RC   STRAIN=cv. Miyakojima MG-20;
RX   PubMed=17208961; DOI=10.1104/pp.106.090894;
RA   Ramos J., Clemente M.R., Naya L., Loscos J., Perez-Rontome C., Sato S.,
RA   Tabata S., Becana M.;
RT   "Phytochelatin synthases of the model legume Lotus japonicus. A small
RT   multigene family with differential response to cadmium and alternatively
RT   spliced variants.";
RL   Plant Physiol. 143:1110-1118(2007).
CC   -!- FUNCTION: Involved in the synthesis of phytochelatins (PC) and
CC       homophytochelatins (hPC), the heavy-metal-binding peptides of plants.
CC       {ECO:0000269|PubMed:17208961}.
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 by Zn(2+), Cu(2+), Fe(2+) or Fe(3+) ions, but not by Co(2+) or
CC       Ni(2+) ions. {ECO:0000269|PubMed:16489135}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, nodules and leaves.
CC       {ECO:0000269|PubMed:17208961}.
CC   -!- INDUCTION: By cadmium. {ECO:0000269|PubMed:17208961}.
CC   -!- MISCELLANEOUS: In roots, Cd(2+) and Zn(2+) induce preferentially
CC       homophytochelatin (hPC) synthesis whereas Cu(2+) has a major effect on
CC       phytochelatin (PC) synthesis.
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}.
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DR   EMBL; AY633847; AAT80342.1; -; mRNA.
DR   EMBL; AY270030; AAQ01752.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2TSC7; -.
DR   SMR; Q2TSC7; -.
DR   PRIDE; Q2TSC7; -.
DR   BioCyc; MetaCyc:MON-16320; -.
DR   BRENDA; 2.3.2.15; 3076.
DR   GO; GO:0016756; F:glutathione gamma-glutamylcysteinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046938; P:phytochelatin biosynthetic process; IEA:InterPro.
DR   GO; GO:0010038; P:response to metal ion; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acyltransferase; Cadmium; Copper; Iron; Metal-binding; Transferase; Zinc.
FT   CHAIN           1..501
FT                   /note="Glutathione gamma-glutamylcysteinyltransferase 1"
FT                   /id="PRO_0000287213"
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   501 AA;  55520 MW;  EC92820F194A0482 CRC64;
     MAMAGLYRRL LPSPPAVDFA SSQGKQLFLE AVQNGTMESF YRLVSYFQTQ SEPAFCGLAS
     LSMVLNALAI DPGRKWKGPW RWFDESMLDC CEPLDKIKAR GISFGKLVCL AHCAGAKVEA
     FHASHSSIDH FRKYVMKCST SDDCHVISSY HREALKQTGT GHFSPIGGYH AGKDMALILD
     VARFKYPPHW IPLTHLWEGM NYVDESTGKT RGFMLISRPH REPGMLYTLS CKHESWNSIA
     KFLIDDIPFL LTSEDVKDIC KVLSVIVTSL PSNFEEFIKW VAEIRRGEDG SPSLSVEEKA
     RLSVKEEILK QVQRTGLFKH VASFLSHSCS GHTPTSGDRD TFPVIAASVC CQGAEILGGK
     ISSSAEYCCR ETCMKCWKAE DDKPIRMVCG TVVNGNTEQG VDVLIPSSCG KLSCTCSSTT
     KSIRKHPAST DVLTVLLLSL PTSTWAGIAD EKLLSEIHDL VSIENLPALL QEEVLHLRRQ
     LHILKRCQEG KVDEDLGVPL S