ID   PCS3_LOTJA              Reviewed;         479 AA.
AC   Q2QKL5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Glutathione gamma-glutamylcysteinyltransferase 3;
DE            EC=2.3.2.15;
DE   AltName: Full=LjPCS3-7N;
DE   AltName: Full=Phytochelatin synthase 3;
GN   Name=PCS3;
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].
RC   TISSUE=Root;
RA   Naya L., Ramos J., Becana M.;
RT   "Lotus japonicus phytochelatin synthase mRNA (pcs2).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, nodules and leaves.
CC       {ECO:0000269|PubMed:17208961}.
CC   -!- INDUCTION: By cadmium. {ECO:0000269|PubMed:17208961}.
CC   -!- SIMILARITY: Belongs to the phytochelatin synthase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00773}.
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; DQ013041; AAY81941.1; -; mRNA.
DR   EMBL; DQ013040; AAY81940.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2QKL5; -.
DR   SMR; Q2QKL5; -.
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; Metal-binding; Transferase.
FT   CHAIN           1..479
FT                   /note="Glutathione gamma-glutamylcysteinyltransferase 3"
FT                   /id="PRO_0000287215"
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   479 AA;  53187 MW;  D9D1E442D74E27C2 CRC64;
     MASAGLYRRV LPSPPAIDFA SPEGKKIFVE ALGQGTMEGF FKLVSYYQTQ SEPAYCGLAT
     LTVVLNALSI DPGRKWKGPW RWFDDSMLDC CEPLEKIKVQ GITFGKVACL ARCNGAHVEA
     FRSNESTVSD FRDRVISCCS SEDRHLIVSY HRSGLKQTGE GHFSPIGGYH AERDMVLILD
     VTRYKYPPHW VPLTLLWDAM NTIDRATGLQ RGYMIISKLK RAPSILYTVS CRHEGWSSVA
     KFLTENVPLL LKSEDLKDIQ EVLSVVFKSP PSELREFITW IAEVRRQEDG NLTLSEEEKG
     RLAIKADILE QIRTTTLFKH VTSWLDSQRS RCRTIAKLQD RDMLPELAAG VCCQGACLLT
     GCCLPGGKCC SQIDVKHLNV DHKNIVTLVS GTVASGSSSE QGVDVLVPLC QMGPEGHCIG
     MHPSTADVLT VLLLALPLHT WSGIKEEKLC AEVTSLLTTE NLPPLLQEEV RFSLETVLF