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Protein

Glutathione S-transferase 2

Gene

GTT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291Glutathione; via amide nitrogen1 Publication
Binding sitei58 – 581Glutathione1 Publication
Binding sitei72 – 721Glutathione; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei133 – 1331Glutathione1 Publication

GO - Molecular functioni

  1. glutathione transferase activity Source: SGD

GO - Biological processi

  1. glutathione metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciYEAST:YLL060C-MONOMER.
SABIO-RKQ12390.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 2 (EC:2.5.1.18)
Alternative name(s):
GST-II
Gene namesi
Name:GTT2
Ordered Locus Names:YLL060C
ORF Names:L0560
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLL060c.
EuPathDBiFungiDB:YLL060C.
SGDiS000003983. GTT2.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271G → A: Reduced enzyme activity. 1 Publication
Mutagenesisi27 – 271G → C, F or S: Loss of enzyme activity. 1 Publication
Mutagenesisi129 – 1291S → A: Reduced enzyme activity. 1 Publication
Mutagenesisi133 – 1331H → A: Loss of enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 233233Glutathione S-transferase 2PRO_0000185988Add
BLAST

Proteomic databases

PaxDbiQ12390.
PeptideAtlasiQ12390.

Expressioni

Gene expression databases

GenevestigatoriQ12390.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi31256. 19 interactions.
DIPiDIP-2981N.
IntActiQ12390. 1 interaction.
MINTiMINT-2785201.
STRINGi4932.YLL060C.

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 234Combined sources
Helixi28 – 3912Combined sources
Helixi43 – 453Combined sources
Beta strandi47 – 504Combined sources
Helixi53 – 553Combined sources
Helixi57 – 593Combined sources
Helixi61 – 666Combined sources
Beta strandi74 – 763Combined sources
Beta strandi82 – 854Combined sources
Helixi86 – 9611Combined sources
Beta strandi101 – 1033Combined sources
Helixi107 – 12317Combined sources
Helixi125 – 13511Combined sources
Turni141 – 1433Combined sources
Helixi149 – 17022Combined sources
Beta strandi178 – 1803Combined sources
Helixi183 – 19715Combined sources
Helixi207 – 21812Combined sources
Helixi220 – 2256Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ERFX-ray2.23A1-233[»]
3ERGX-ray2.20A/B1-233[»]
3IBHX-ray2.10A1-233[»]
ProteinModelPortaliQ12390.
SMRiQ12390. Positions 19-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12390.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 10185GST N-terminalAdd
BLAST
Domaini106 – 233128GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni85 – 862Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125751.
InParanoidiQ12390.
OMAiPYPARVR.
OrthoDBiEOG7QNVXT.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12390-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGRGFLIYN GGEKMKQKMI IYDTPAGPYP ARVRIALAEK NMLSSVQFVR
60 70 80 90 100
INLWKGEHKK PEFLAKNYSG TVPVLELDDG TLIAECTAIT EYIDALDGTP
110 120 130 140 150
TLTGKTPLEK GVIHMMNKRA ELELLDPVSV YFHHATPGLG PEVELYQNKE
160 170 180 190 200
WGLRQRDKAL HGMHYFDTVL RERPYVAGDS FSMADITVIA GLIFAAIVKL
210 220 230
QVPEECEALR AWYKRMQQRP SVKKLLEIRS KSS
Length:233
Mass (Da):26,340
Last modified:November 1, 1996 - v1
Checksum:iB5EE0E47D5A37175
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47973 Genomic DNA. Translation: CAA87997.1.
Z73165 Genomic DNA. Translation: CAA97513.1.
AY557940 Genomic DNA. Translation: AAS56266.1.
BK006945 Genomic DNA. Translation: DAA09265.1.
PIRiS50960.
RefSeqiNP_013040.1. NM_001181880.1.

Genome annotation databases

EnsemblFungiiYLL060C; YLL060C; YLL060C.
GeneIDi850666.
KEGGisce:YLL060C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47973 Genomic DNA. Translation: CAA87997.1.
Z73165 Genomic DNA. Translation: CAA97513.1.
AY557940 Genomic DNA. Translation: AAS56266.1.
BK006945 Genomic DNA. Translation: DAA09265.1.
PIRiS50960.
RefSeqiNP_013040.1. NM_001181880.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ERFX-ray2.23A1-233[»]
3ERGX-ray2.20A/B1-233[»]
3IBHX-ray2.10A1-233[»]
ProteinModelPortaliQ12390.
SMRiQ12390. Positions 19-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31256. 19 interactions.
DIPiDIP-2981N.
IntActiQ12390. 1 interaction.
MINTiMINT-2785201.
STRINGi4932.YLL060C.

Proteomic databases

PaxDbiQ12390.
PeptideAtlasiQ12390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLL060C; YLL060C; YLL060C.
GeneIDi850666.
KEGGisce:YLL060C.

Organism-specific databases

CYGDiYLL060c.
EuPathDBiFungiDB:YLL060C.
SGDiS000003983. GTT2.

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125751.
InParanoidiQ12390.
OMAiPYPARVR.
OrthoDBiEOG7QNVXT.

Enzyme and pathway databases

BioCyciYEAST:YLL060C-MONOMER.
SABIO-RKQ12390.

Miscellaneous databases

EvolutionaryTraceiQ12390.
NextBioi966644.
PROiQ12390.

Gene expression databases

GenevestigatoriQ12390.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces cerevisiae including the subtelomeric region of the left arm."
    Wedler H., Wambutt R.
    Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "A novel membrane-bound glutathione S-transferase functions in the stationary phase of the yeast Saccharomyces cerevisiae."
    Choi J.H., Lou W., Vancura A.
    J. Biol. Chem. 273:29915-29922(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family."
    Ma X.X., Jiang Y.L., He Y.X., Bao R., Chen Y., Zhou C.Z.
    EMBO Rep. 10:1320-1326(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-27; SER-129 AND HIS-133, SUBUNIT.

Entry informationi

Entry nameiGST2_YEAST
AccessioniPrimary (citable) accession number: Q12390
Secondary accession number(s): D6VXU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: April 29, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.