GSHB_YEAST
ID GSHB_YEAST Reviewed; 491 AA.
AC Q08220; D6W218;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Glutathione synthetase GSH2 {ECO:0000303|PubMed:9512666};
DE Short=GSH synthetase;
DE Short=GSH-S;
DE EC=6.3.2.3;
DE AltName: Full=Glutathione synthase;
GN Name=GSH2; OrderedLocusNames=YOL049W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9512666; DOI=10.1016/s0167-4781(97)00199-1;
RA Inoue Y., Sugiyama K.I., Izawa S., Kimura A.;
RT "Molecular identification of glutathione synthetase (GSH2) gene from
RT Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1395:315-320(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP AMP-PNP, COFACTOR, AND SUBUNIT.
RX PubMed=12467574; DOI=10.1016/s0969-2126(02)00906-1;
RA Gogos A., Shapiro L.;
RT "Large conformational changes in the catalytic cycle of glutathione
RT synthase.";
RL Structure 10:1669-1676(2002).
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 Evidence={ECO:0000269|PubMed:9512666};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13558;
CC Evidence={ECO:0000305|PubMed:9512666};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12467574};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:12467574};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12467574}.
CC -!- MISCELLANEOUS: Present with 3430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic GSH synthase family.
CC {ECO:0000305}.
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DR EMBL; Y13804; CAA74136.1; -; Genomic_DNA.
DR EMBL; Z74791; CAA99054.1; -; Genomic_DNA.
DR EMBL; AY723864; AAU09781.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10734.1; -; Genomic_DNA.
DR PIR; S66734; S66734.
DR RefSeq; NP_014593.1; NM_001183303.1.
DR PDB; 1M0T; X-ray; 2.30 A; A/B=1-491.
DR PDB; 1M0W; X-ray; 1.80 A; A/B=1-491.
DR PDBsum; 1M0T; -.
DR PDBsum; 1M0W; -.
DR AlphaFoldDB; Q08220; -.
DR SMR; Q08220; -.
DR BioGRID; 34354; 136.
DR IntAct; Q08220; 1.
DR STRING; 4932.YOL049W; -.
DR iPTMnet; Q08220; -.
DR MaxQB; Q08220; -.
DR PaxDb; Q08220; -.
DR PRIDE; Q08220; -.
DR EnsemblFungi; YOL049W_mRNA; YOL049W; YOL049W.
DR GeneID; 854108; -.
DR KEGG; sce:YOL049W; -.
DR SGD; S000005409; GSH2.
DR VEuPathDB; FungiDB:YOL049W; -.
DR eggNOG; KOG0021; Eukaryota.
DR GeneTree; ENSGT00390000013764; -.
DR HOGENOM; CLU_025152_2_1_1; -.
DR InParanoid; Q08220; -.
DR OMA; NGLVMYP; -.
DR BioCyc; YEAST:YOL049W-MON; -.
DR BRENDA; 6.3.2.3; 984.
DR Reactome; R-SCE-174403; Glutathione synthesis and recycling.
DR UniPathway; UPA00142; UER00210.
DR EvolutionaryTrace; Q08220; -.
DR PRO; PR:Q08220; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08220; protein.
DR GO; GO:0005737; C:cytoplasm; TAS:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0043295; F:glutathione binding; IDA:UniProtKB.
DR GO; GO:0004363; F:glutathione synthase activity; IDA:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006750; P:glutathione biosynthetic process; IMP:SGD.
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 3D-structure; ATP-binding; Glutathione biosynthesis; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..491
FT /note="Glutathione synthetase GSH2"
FT /id="PRO_0000211266"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12467574"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 BINDING 228..230
FT /ligand="substrate"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12467574"
FT BINDING 285..288
FT /ligand="substrate"
FT BINDING 324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 382..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 415..418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 478..479
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 8..25
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 55..79
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1M0W"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 123..136
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 191..208
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1M0W"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1M0W"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 316..321
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:1M0W"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 343..350
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 397..402
FT /evidence="ECO:0007829|PDB:1M0W"
FT HELIX 406..411
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 439..451
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 456..469
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:1M0W"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:1M0W"
SQ SEQUENCE 491 AA; 55815 MW; D2AE50A487E0791C CRC64;
MAHYPPSKDQ LNELIQEVNQ WAITNGLSMY PPKFEENPSN ASVSPVTIYP TPIPRKCFDE
AVQIQPVFNE LYARITQDMA QPDSYLHKTT EALALSDSEF TGKLWSLYLA TLKSAQYKKQ
NFRLGIFRSD YLIDKKKGTE QIKQVEFNTV SVSFAGLSEK VDRLHSYLNR ANKYDPKGPI
YNDQNMVISD SGYLLSKALA KAVESYKSQQ SSSTTSDPIV AFIVQRNERN VFDQKVLELN
LLEKFGTKSV RLTFDDVNDK LFIDDKTGKL FIRDTEQEIA VVYYRTGYTT TDYTSEKDWE
ARLFLEKSFA IKAPDLLTQL SGSKKIQQLL TDEGVLGKYI SDAEKKSSLL KTFVKIYPLD
DTKLGREGKR LALSEPSKYV LKPQREGGGN NVYKENIPNF LKGIEERHWD AYILMELIEP
ELNENNIILR DNKSYNEPII SELGIYGCVL FNDEQVLSNE FSGSLLRSKF NTSNEGGVAA
GFGCLDSIIL Y
