ID   PCS2_LOTJA              Reviewed;         482 AA.
AC   Q2TE74;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Glutathione gamma-glutamylcysteinyltransferase 2;
DE            EC=2.3.2.15;
DE   AltName: Full=LjPCS2-7R;
DE   AltName: Full=Phytochelatin synthase 2;
GN   Name=PCS2;
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] (ISOFORM LJAP2R).
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], ALTERNATIVE SPLICING, FUNCTION, TISSUE
RP   SPECIFICITY, AND 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Ljap2N;
CC         IsoId=Q2TE74-1; Sequence=Displayed;
CC       Name=Ljap2R;
CC         IsoId=Q2TE74-2; Sequence=VSP_025376;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, nodules and leaves.
CC       {ECO:0000269|PubMed:17208961}.
CC   -!- INDUCTION: By cadmium. {ECO:0000269|PubMed:17208961}.
CC   -!- MISCELLANEOUS: [Isoform Ljap2N]: Found in nodules.
CC   -!- MISCELLANEOUS: [Isoform Ljap2R]: Found in roots. Not functional in
CC       yeast heterologous system. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phytochelatin synthase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00773}.
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DR   EMBL; AY633846; AAT80341.1; -; mRNA.
DR   EMBL; AY928091; AAX99139.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2TE74; -.
DR   SMR; Q2TE74; -.
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; Alternative splicing; Cadmium; Metal-binding; Transferase.
FT   CHAIN           1..482
FT                   /note="Glutathione gamma-glutamylcysteinyltransferase 2"
FT                   /id="PRO_0000287214"
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"
FT   VAR_SEQ         73..77
FT                   /note="Missing (in isoform Ljap2R)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_025376"
SQ   SEQUENCE   482 AA;  53692 MW;  BE6368B067F9DAE0 CRC64;
     MASVSLYRRV LPSPPAIDFA SQEGKKIFVE ALGQGTMEGF FKLISFYQTQ SEPAYCGLAT
     LSVVLNALAI DPGRKWKGPW RWFDDSMLDC CEPLEKVKVQ GITFGKVACL ARCNGAKVEA
     FRSNESTVSD FRNRVISCCS SEDRHAIVSY HRSGLKQTGE GHFSPLGGYH AERDMVLILD
     VTRYKYPPHW VPVTLLWNAM NTIDRATGLQ RGYMIISKLN RAPSILYTLS CRHEGWSSVA
     KFLTENVPLL LKSEDLKDIQ EVLSVVFKSP PSELREFITW IAEVRRQEDG NLTLSEEEKG
     RLVIKAEILE KIRTAGLFKH VTSWLDSQRS RCSTIANLQD KDMLPELAAR VCCQGACLLT
     GCCLSGGKCC CQIDVKHLNV DSKNLATTFV SGTFTTGSSS EQGVDVLVPL CQRGPEGHYI
     AMHPSTADVL TVLLLALPLH TWSGIKEEKL RAEVTSLVTT EDLPSLLQEE VILYMEPVLQ
     FF