ID   PCS_SCHPO               Reviewed;         414 AA.
AC   Q10075;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=Glutathione gamma-glutamylcysteinyltransferase;
DE            EC=2.3.2.15;
DE   AltName: Full=Phytochelatin synthase;
GN   ORFNames=SPAC3H1.10;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, AND INDUCTION.
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   [3]
RP   FUNCTION.
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: Required for detoxification of heavy metals such as cadmium
CC       and arsenate. {ECO:0000269|PubMed:10368185,
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   -!- INDUCTION: By cadmium, copper and zinc. {ECO:0000269|PubMed:10368185}.
CC   -!- SIMILARITY: Belongs to the phytochelatin synthase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00773}.
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DR   EMBL; CU329670; CAA92263.1; -; Genomic_DNA.
DR   PIR; T38742; T38742.
DR   RefSeq; NP_593552.1; NM_001018985.2.
DR   AlphaFoldDB; Q10075; -.
DR   SMR; Q10075; -.
DR   BioGRID; 279789; 8.
DR   STRING; 284812.Q10075; -.
DR   iPTMnet; Q10075; -.
DR   MaxQB; Q10075; -.
DR   PaxDb; 4896-SPAC3H1-10-1; -.
DR   EnsemblFungi; SPAC3H1.10.1; SPAC3H1.10.1:pep; SPAC3H1.10.
DR   GeneID; 2543367; -.
DR   KEGG; spo:SPAC3H1.10; -.
DR   PomBase; SPAC3H1.10; -.
DR   VEuPathDB; FungiDB:SPAC3H1.10; -.
DR   eggNOG; KOG0632; Eukaryota.
DR   HOGENOM; CLU_046059_1_0_1; -.
DR   InParanoid; Q10075; -.
DR   OMA; LCMILNS; -.
DR   PhylomeDB; Q10075; -.
DR   PRO; PR:Q10075; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0046870; F:cadmium ion binding; IDA:PomBase.
DR   GO; GO:0016756; F:glutathione gamma-glutamylcysteinyltransferase activity; IDA:PomBase.
DR   GO; GO:0098849; P:cellular detoxification of cadmium ion; IMP:PomBase.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IMP:PomBase.
DR   GO; GO:0010273; P:detoxification of copper ion; IMP:PomBase.
DR   GO; GO:0046938; P:phytochelatin biosynthetic process; IDA:PomBase.
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   PANTHER; PTHR33447; GLUTATHIONE GAMMA-GLUTAMYLCYSTEINYLTRANSFERASE; 1.
DR   PANTHER; PTHR33447:SF2; GLUTATHIONE GAMMA-GLUTAMYLCYSTEINYLTRANSFERASE; 1.
DR   Pfam; PF05023; Phytochelatin; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS51443; PCS; 1.
PE   2: Evidence at transcript level;
KW   Cadmium; Copper; Metal-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..414
FT                   /note="Glutathione gamma-glutamylcysteinyltransferase"
FT                   /id="PRO_0000116449"
FT   DOMAIN          37..256
FT                   /note="Peptidase C83"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
SQ   SEQUENCE   414 AA;  46741 MW;  4EAB522E9C322EBD CRC64;
     MNIVKRAVPE LLRGMTNATP NIGLIKNKVV SFEAVGQLKK SFYKRQLPKQ CLAFDSSLGK
     DVFLRALQEG RMENYFSLAQ QMVTQNEPAF CGLGTLCMIL NSLKVDPGRL WKGSWRWYDQ
     YMLDCCRSLS DIEKDGVTLE EFSCLANCNG LRTITKCVKD VSFDEFRKDV ISCSTIENKI
     MAISFCRKVL GQTGDGHFSP VGGFSESDNK ILILDVARFK YPCYWVDLKL MYESMFPIDK
     ASGQPRGYVL LEPMHIPLGV LTVGLNKYSW RNVSKHILQQ AATVKNADNL AEILLSINQS
     SIPLIQERSN SSKSGDFEHF KECIRSTKTY HLFLKHTNTN VEYITMAFWA IFSLPMIQKA
     LPKGVLEEIQ SLLKEVEISE INTQLTALKK QLDSLTHCCK TDTGCCSSSC CKNT
//