GST2_YEAST
ID GST2_YEAST Reviewed; 233 AA.
AC Q12390; D6VXU9;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Glutathione S-transferase 2;
DE EC=2.5.1.18;
DE AltName: Full=GST-II;
GN Name=GTT2; OrderedLocusNames=YLL060C; ORFNames=L0560;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Wedler H., Wambutt R.;
RT "Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces
RT cerevisiae including the subtelomeric region of the left arm.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 CHARACTERIZATION.
RX PubMed=9792709; DOI=10.1074/jbc.273.45.29915;
RA Choi J.H., Lou W., Vancura A.;
RT "A novel membrane-bound glutathione S-transferase functions in the
RT stationary phase of the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:29915-29922(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-27; SER-129 AND HIS-133, AND
RP SUBUNIT.
RX PubMed=19851333; DOI=10.1038/embor.2009.216;
RA Ma X.X., Jiang Y.L., He Y.X., Bao R., Chen Y., Zhou C.Z.;
RT "Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic
RT type of GST family.";
RL EMBO Rep. 10:1320-1326(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:19851333};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19851333}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; Z47973; CAA87997.1; -; Genomic_DNA.
DR EMBL; Z73165; CAA97513.1; -; Genomic_DNA.
DR EMBL; AY557940; AAS56266.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09265.1; -; Genomic_DNA.
DR PIR; S50960; S50960.
DR RefSeq; NP_013040.1; NM_001181880.1.
DR PDB; 3ERF; X-ray; 2.23 A; A=1-233.
DR PDB; 3ERG; X-ray; 2.20 A; A/B=1-233.
DR PDB; 3IBH; X-ray; 2.10 A; A=1-233.
DR PDBsum; 3ERF; -.
DR PDBsum; 3ERG; -.
DR PDBsum; 3IBH; -.
DR AlphaFoldDB; Q12390; -.
DR SMR; Q12390; -.
DR BioGRID; 31256; 42.
DR DIP; DIP-2981N; -.
DR IntAct; Q12390; 1.
DR MINT; Q12390; -.
DR STRING; 4932.YLL060C; -.
DR PaxDb; Q12390; -.
DR PRIDE; Q12390; -.
DR EnsemblFungi; YLL060C_mRNA; YLL060C; YLL060C.
DR GeneID; 850666; -.
DR KEGG; sce:YLL060C; -.
DR SGD; S000003983; GTT2.
DR VEuPathDB; FungiDB:YLL060C; -.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT01000000220041; -.
DR HOGENOM; CLU_011226_6_3_1; -.
DR InParanoid; Q12390; -.
DR OMA; AICRYFE; -.
DR BioCyc; MetaCyc:YLL060C-MON; -.
DR BioCyc; YEAST:YLL060C-MON; -.
DR SABIO-RK; Q12390; -.
DR EvolutionaryTrace; Q12390; -.
DR PRO; PR:Q12390; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12390; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0043295; F:glutathione binding; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:SGD.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:SGD.
DR CDD; cd03182; GST_C_GTT2_like; 1.
DR CDD; cd03051; GST_N_GTT2_like; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR034346; Gtt2-like_C.
DR InterPro; IPR034345; Gtt2-like_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..233
FT /note="Glutathione S-transferase 2"
FT /id="PRO_0000185988"
FT DOMAIN 17..101
FT /note="GST N-terminal"
FT DOMAIN 106..233
FT /note="GST C-terminal"
FT BINDING 29
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:19851333"
FT BINDING 58
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:19851333"
FT BINDING 72
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:19851333"
FT BINDING 85..86
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT BINDING 133
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:19851333"
FT MUTAGEN 27
FT /note="G->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:19851333"
FT MUTAGEN 27
FT /note="G->C,F,S: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:19851333"
FT MUTAGEN 129
FT /note="S->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:19851333"
FT MUTAGEN 133
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:19851333"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3IBH"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:3IBH"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3IBH"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:3IBH"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:3IBH"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 149..170
FT /evidence="ECO:0007829|PDB:3IBH"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:3IBH"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:3IBH"
SQ SEQUENCE 233 AA; 26340 MW; B5EE0E47D5A37175 CRC64;
MNGRGFLIYN GGEKMKQKMI IYDTPAGPYP ARVRIALAEK NMLSSVQFVR INLWKGEHKK
PEFLAKNYSG TVPVLELDDG TLIAECTAIT EYIDALDGTP TLTGKTPLEK GVIHMMNKRA
ELELLDPVSV YFHHATPGLG PEVELYQNKE WGLRQRDKAL HGMHYFDTVL RERPYVAGDS
FSMADITVIA GLIFAAIVKL QVPEECEALR AWYKRMQQRP SVKKLLEIRS KSS
