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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)DescriptionActionsGraphical viewLength
Binding sitei29Glutathione; via amide nitrogen1 Publication1
Binding sitei58Glutathione1 Publication1
Binding sitei72Glutathione; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei133Glutathione1 Publication1

GO - Molecular functioni

  • glutathione transferase activity Source: SGD

GO - Biological processi

  • 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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLL060C.
SGDiS000003983. GTT2.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27G → A: Reduced enzyme activity. 1 Publication1
Mutagenesisi27G → C, F or S: Loss of enzyme activity. 1 Publication1
Mutagenesisi129S → A: Reduced enzyme activity. 1 Publication1
Mutagenesisi133H → A: Loss of enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001859881 – 233Glutathione S-transferase 2Add BLAST233

Proteomic databases

PRIDEiQ12390.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi31256. 19 interactors.
DIPiDIP-2981N.
IntActiQ12390. 1 interactor.
MINTiMINT-2785201.

Structurei

Secondary structure

1233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 23Combined sources4
Helixi28 – 39Combined sources12
Helixi43 – 45Combined sources3
Beta strandi47 – 50Combined sources4
Helixi53 – 55Combined sources3
Helixi57 – 59Combined sources3
Helixi61 – 66Combined sources6
Beta strandi74 – 76Combined sources3
Beta strandi82 – 85Combined sources4
Helixi86 – 96Combined sources11
Beta strandi101 – 103Combined sources3
Helixi107 – 123Combined sources17
Helixi125 – 135Combined sources11
Turni141 – 143Combined sources3
Helixi149 – 170Combined sources22
Beta strandi178 – 180Combined sources3
Helixi183 – 197Combined sources15
Helixi207 – 218Combined sources12
Helixi220 – 225Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ12390.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 101GST N-terminalAdd BLAST85
Domaini106 – 233GST C-terminalAdd BLAST128

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni85 – 86Glutathione binding2

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000125751.
InParanoidiQ12390.
OMAiPEVELYQ.
OrthoDBiEOG092C4EF1.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ERFX-ray2.23A1-233[»]
3ERGX-ray2.20A/B1-233[»]
3IBHX-ray2.10A1-233[»]
ProteinModelPortaliQ12390.
SMRiQ12390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31256. 19 interactors.
DIPiDIP-2981N.
IntActiQ12390. 1 interactor.
MINTiMINT-2785201.

Proteomic databases

PRIDEiQ12390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YLL060C.
SGDiS000003983. GTT2.

Phylogenomic databases

HOGENOMiHOG000125751.
InParanoidiQ12390.
OMAiPEVELYQ.
OrthoDBiEOG092C4EF1.

Enzyme and pathway databases

BioCyciYEAST:YLL060C-MONOMER.
SABIO-RKQ12390.

Miscellaneous databases

EvolutionaryTraceiQ12390.
PROiQ12390.

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...

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: November 2, 2016
This is version 129 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

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 one 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.