GSHB_SCHPO
ID GSHB_SCHPO Reviewed; 498 AA.
AC P35669; Q8X1A1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Glutathione synthetase large chain;
DE Short=GSH synthetase large chain;
DE Short=GSH-S;
DE EC=6.3.2.3;
DE AltName: Full=Glutathione synthase large chain;
DE AltName: Full=Phytochelatin synthetase;
GN Name=gsa1; Synonyms=gsh2; ORFNames=SPAC3F10.04;
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 [GENOMIC DNA].
RC STRAIN=SP011;
RX PubMed=10219997;
RX DOI=10.1002/(sici)1097-0061(19990330)15:5<385::aid-yea382>3.0.co;2-6;
RA Al-Lahham A., Rohde V., Heim P., Leuchter R., Veeck J., Wunderlich C.,
RA Wolf K., Zimmermann M.;
RT "Biosynthesis of phytochelatins in the fission yeast. Phytochelatin
RT synthesis: a second role for the glutathione synthetase gene of
RT Schizosaccharomyces pombe.";
RL Yeast 15:385-396(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shin Y.H., Lim C.-J.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-498, AND PROTEIN SEQUENCE OF
RP 218-229 AND 392-403.
RC STRAIN=972 / ATCC 24843;
RX PubMed=1958212; DOI=10.1016/s0006-291x(05)81437-8;
RA Mutoh N., Nakagawa C.W., Ando S., Tanabe K., Hayashi Y.;
RT "Cloning and sequencing of the gene encoding the large subunit of
RT glutathione synthetase of Schizosaccharomyces pombe.";
RL Biochem. Biophys. Res. Commun. 181:430-436(1991).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP +
CC glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
CC ChEBI:CHEBI:456216; EC=6.3.2.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 2/2.
CC -!- SUBUNIT: Heterodimer composed of a large and a small chain.
CC -!- SIMILARITY: Belongs to the eukaryotic GSH synthase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA93302.1; -; Genomic_DNA.
DR EMBL; AF448236; AAL41009.1; -; Genomic_DNA.
DR EMBL; Y08414; CAA69691.1; -; Genomic_DNA.
DR EMBL; M85179; AAA35307.1; -; Genomic_DNA.
DR PIR; JT0961; JT0961.
DR PIR; T38705; T38705.
DR RefSeq; NP_593936.1; NM_001019364.2.
DR AlphaFoldDB; P35669; -.
DR SMR; P35669; -.
DR BioGRID; 279340; 11.
DR STRING; 4896.SPAC3F10.04.1; -.
DR iPTMnet; P35669; -.
DR MaxQB; P35669; -.
DR PaxDb; P35669; -.
DR PRIDE; P35669; -.
DR EnsemblFungi; SPAC3F10.04.1; SPAC3F10.04.1:pep; SPAC3F10.04.
DR PomBase; SPAC3F10.04; gsa1.
DR VEuPathDB; FungiDB:SPAC3F10.04; -.
DR eggNOG; KOG0021; Eukaryota.
DR HOGENOM; CLU_025152_2_1_1; -.
DR InParanoid; P35669; -.
DR OMA; NGLVMYP; -.
DR PhylomeDB; P35669; -.
DR BioCyc; MetaCyc:MON-10022; -.
DR BRENDA; 6.3.2.3; 5613.
DR Reactome; R-SPO-174403; Glutathione synthesis and recycling.
DR UniPathway; UPA00142; UER00210.
DR PRO; PR:P35669; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0036087; C:glutathione synthase complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR GO; GO:0004363; F:glutathione synthase activity; IDA:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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:0006750; P:glutathione biosynthetic process; IDA:PomBase.
DR GO; GO:0046938; P:phytochelatin biosynthetic process; IMP:PomBase.
DR GO; GO:0090423; P:phytochelatin-metal complex formation; IMP:PomBase.
DR CDD; cd00228; eu-GS; 1.
DR Gene3D; 1.10.1080.10; -; 1.
DR Gene3D; 3.30.1490.50; -; 1.
DR Gene3D; 3.30.1490.80; -; 1.
DR Gene3D; 3.40.50.1760; -; 1.
DR InterPro; IPR005615; Glutathione_synthase.
DR InterPro; IPR014042; Glutathione_synthase_a-hlx.
DR InterPro; IPR014709; Glutathione_synthase_C_euk.
DR InterPro; IPR014049; Glutathione_synthase_N_euk.
DR InterPro; IPR037013; GSH-S_sub-bd_sf.
DR InterPro; IPR004887; GSH_synth_subst-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11130; PTHR11130; 1.
DR Pfam; PF03917; GSH_synth_ATP; 1.
DR Pfam; PF03199; GSH_synthase; 1.
DR PIRSF; PIRSF001558; GSHase; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01986; glut_syn_euk; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Glutathione biosynthesis; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..498
FT /note="Glutathione synthetase large chain"
FT /id="PRO_0000211265"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 150..153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233..235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 291..294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 387..396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 420..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 484..485
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 132
FT /note="M -> T (in Ref. 2; AAL41009)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="N -> T (in Ref. 4; AAA35307)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="A -> R (in Ref. 4; AAA35307)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="K -> E (in Ref. 4; AAA35307)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="K -> N (in Ref. 4; AAA35307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 56153 MW; AD2921C5AD667ABF CRC64;
MEIEKYTPEQ IEELGKGARD FAFAHGVVFT ELSVSKEGRN IATQIPITLF PSVIPHGAFV
EAVSVQKAYN KLYAKIANDY EFLRLHLQSI TKYDEFMNKL WNLYQKHREA VAHLKENQFQ
PLSLGVFRSD YMVHQDDSFI GCKQVEFNTI SVSFGGVSKA VSNLHAYCSQ SGLYRKPLTT
NYLTVNTSVS GICTGISNAV DAYRDYVKNI TSKMNIASDN TKPIVLFVVK GGERNITDQR
TLEYELLNRF HVISKRIDIA ELNSLIHDKS SNKLYMKTSF TTYEVAVVYY RVGYALDDYP
SQEAWDMRLT IENTLAIKCP SISTHLAGSK KIQQVLAESN ALERFLEGDE LQAVRSTFAD
MYPLDDTPRG KEGIKLAFEK PEDFVLKPQR EGGGNNTYGK DIPGLLSKMP QEEWDSYILM
RYINAVPSQN YILKGERPEK FDVVDEIGIL GTIVWNIKTD EVVQNGQSGF ICRTKPKKTN
EGGVATGYAS LSSIELSE
