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Protein

Glutathione S-transferase omega-like 1

Gene

GTO1

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

Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB).1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.1 Publication

Kineticsi

  1. KM=1.13 mM for reduced glutathione (GSH)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei31 – 311NucleophileBy similarity

GO - Molecular functioni

  1. glutathione dehydrogenase (ascorbate) activity Source: UniProtKB-EC
  2. glutathione transferase activity Source: SGD

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase, Transferase

Enzyme and pathway databases

BioCyciYEAST:G3O-30856-MONOMER.
SABIO-RKP48239.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase omega-like 1 (EC:2.5.1.18)
Alternative name(s):
Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
Gene namesi
Name:GTO1
Ordered Locus Names:YGR154C
ORF Names:G6664
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGR154c.
EuPathDBiFungiDB:YGR154C.
SGDiS000003386. GTO1.

Subcellular locationi

  1. Peroxisome 1 Publication

GO - Cellular componenti

  1. peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Disruption phenotypei

Null mutants display increased sensitivity to cadmium in the absence of GTT1 and GTT2. Null mutants also show growth defects on oleic acid-based medium, indicative of abnormal peroxisomal functions and altered expression of genes related to sulfur amino acid metabolism, and have low levels of reduced glutathione.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Glutathione S-transferase omega-like 1PRO_0000202833Add
BLAST

Proteomic databases

PaxDbiP48239.

Expressioni

Inductioni

By diamide and 1-chloro-2,4-dinitrobenzene (CDNB) in a transcriptional factors YAP1 and/or MSN2/4-dependent manner.1 Publication

Gene expression databases

GenevestigatoriP48239.

Interactioni

Protein-protein interaction databases

BioGridi33402. 8 interactions.
DIPiDIP-1867N.
IntActiP48239. 1 interaction.
MINTiMINT-392461.
STRINGi4932.YGR154C.

Structurei

3D structure databases

SMRiP48239. Positions 16-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili214 – 25744Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the GST superfamily. Omega family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0435.
GeneTreeiENSGT00530000065151.
HOGENOMiHOG000245143.
InParanoidiP48239.
OrthoDBiEOG722JK6.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 2 hits.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR016639. GST.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR32419. PTHR32419. 1 hit.
PfamiPF13409. GST_N_2. 1 hit.
[Graphical view]
PIRSFiPIRSF015753. GST. 1 hit.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 2 hits.

Sequencei

Sequence statusi: Complete.

P48239-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVSYKGTIS KTHSVFKPEK GRYYIYGALG CPFTHRAILA RSLKKLEPVL
60 70 80 90 100
GLVLSHWQLD SKGARFLPAP HRPEKYKERF FTATGGIASA KLDESEELGD
110 120 130 140 150
VNNDSARLFV DGAFDPVENI SRLSELYYLN DPKYPGTKFT VPVLWDSKTR
160 170 180 190 200
KIVNNESGDI IRILNSGVFD EFIQSEETNV IDLVPHDLID EIDKNIKWVH
210 220 230 240 250
PKINLGVYKV GLAENGKIYE TEVKTLFENL QKMECVLKEN YKRLEEQFSG
260 270 280 290 300
NKQKILAKYF VLGQRLTEAD IRLYPSIIRF DVVYVQHFKC NLKTIRDGFP
310 320 330 340 350
YLHLWLINLY WNYAEFRFTT DFNHIKLFYI RMEVSRNKIN QFGIVPLGPK

PDISRL
Length:356
Mass (Da):41,301
Last modified:February 1, 1996 - v1
Checksum:iB4639BD195CDF7F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85807 Genomic DNA. Translation: CAA59811.1.
Z72939 Genomic DNA. Translation: CAA97168.1.
BK006941 Genomic DNA. Translation: DAA08245.1.
PIRiS60444.
RefSeqiNP_011670.3. NM_001181283.3.

Genome annotation databases

EnsemblFungiiYGR154C; YGR154C; YGR154C.
GeneIDi853058.
KEGGisce:YGR154C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85807 Genomic DNA. Translation: CAA59811.1.
Z72939 Genomic DNA. Translation: CAA97168.1.
BK006941 Genomic DNA. Translation: DAA08245.1.
PIRiS60444.
RefSeqiNP_011670.3. NM_001181283.3.

3D structure databases

SMRiP48239. Positions 16-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33402. 8 interactions.
DIPiDIP-1867N.
IntActiP48239. 1 interaction.
MINTiMINT-392461.
STRINGi4932.YGR154C.

Proteomic databases

PaxDbiP48239.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR154C; YGR154C; YGR154C.
GeneIDi853058.
KEGGisce:YGR154C.

Organism-specific databases

CYGDiYGR154c.
EuPathDBiFungiDB:YGR154C.
SGDiS000003386. GTO1.

Phylogenomic databases

eggNOGiCOG0435.
GeneTreeiENSGT00530000065151.
HOGENOMiHOG000245143.
InParanoidiP48239.
OrthoDBiEOG722JK6.

Enzyme and pathway databases

BioCyciYEAST:G3O-30856-MONOMER.
SABIO-RKP48239.

Miscellaneous databases

NextBioi972989.
PROiP48239.

Gene expression databases

GenevestigatoriP48239.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 2 hits.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR016639. GST.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR32419. PTHR32419. 1 hit.
PfamiPF13409. GST_N_2. 1 hit.
[Graphical view]
PIRSFiPIRSF015753. GST. 1 hit.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of a 27 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new open reading frames."
    Skala J., Nawrocki A., Goffeau A.
    Yeast 11:1421-1427(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(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. "Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases."
    Garcera A., Barreto L., Piedrafita L., Tamarit J., Herrero E.
    Biochem. J. 398:187-196(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  5. "A peroxisomal glutathione transferase of Saccharomyces cerevisiae is functionally related to sulfur amino acid metabolism."
    Barreto L., Garcera A., Jansson K., Sunnerhagen P., Herrero E.
    Eukaryot. Cell 5:1748-1759(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION.

Entry informationi

Entry nameiGTO1_YEAST
AccessioniPrimary (citable) accession number: P48239
Secondary accession number(s): D6VUT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 29, 2015
This is version 103 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

Complete proteome, Reference proteome

Documents

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