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Protein

Glutathione S-transferase omega-like 2

Gene

ECM4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 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). May be involved in cell wall organization and biogenesis.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=1.42 mM for reduced glutathione (GSH)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei46 – 461Nucleophile1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. glutathione metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciYEAST:G3O-32040-MONOMER.
SABIO-RKP36156.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase omega-like 2 (EC:2.5.1.18)
Alternative name(s):
Extracellular mutant protein 4
Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
Gene namesi
Name:ECM4
Synonyms:GTO2
Ordered Locus Names:YKR076W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKR076w.
SGDiS000001784. ECM4.

Subcellular locationi

Cytoplasm 2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461C → S or Y: Completely inactive as thiol transferase. No activity recovered against 1-chloro-2,4-dinitrobenzene (CDNB). 1 Publication
Mutagenesisi51 – 511R → A: No effect on thiol transferase activity. No effect on thiol transferase activity; when associated with D-173. 1 Publication
Mutagenesisi173 – 1731E → A or D: No effect on thiol transferase activity. 1 Publication
Mutagenesisi174 – 1741S → A: No effect on thiol transferase activity. 1 Publication
Mutagenesisi246 – 2461L → A: No effect on thiol transferase activity. 1 Publication
Mutagenesisi280 – 2801G → L: No effect on thiol transferase activity. 1 Publication
Mutagenesisi287 – 2871D → G: Abolishes thiol transferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Glutathione S-transferase omega-like 2PRO_0000086922Add
BLAST

Proteomic databases

MaxQBiP36156.
PaxDbiP36156.
PeptideAtlasiP36156.

Expressioni

Inductioni

Under oxidative stress conditions. By agents such as diamide, 1-chloro-2,4-dinitrobenzene, tert-butyl hydroperoxide (t-BOOH) and cadmium in a transcriptional factors YAP1 and/or MSN2/4-dependent manner.2 Publications

Gene expression databases

GenevestigatoriP36156.

Interactioni

Protein-protein interaction databases

BioGridi34207. 9 interactions.
MINTiMINT-4493799.
STRINGi4932.YKR076W.

Structurei

3D structure databases

ProteinModelPortaliP36156.
SMRiP36156. Positions 10-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini201 – 353153GST C-terminalAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0435.
GeneTreeiENSGT00530000065151.
HOGENOMiHOG000245143.
InParanoidiP36156.
KOiK07393.
OMAiNSWVYDS.
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.
PROSITEiPS50405. GST_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36156-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKQWASGTN GAFKRQVSSF RETISKQHPI YKPAKGRYWL YVSLACPWAH
60 70 80 90 100
RTLITRALKG LTSVIGCSVV HWHLDEKGWR FLDMEKQLED SEDFLEHWHD
110 120 130 140 150
VAGGIRTAKE DSSKSFAEIK NDSQRFMVDA TNEPHYGYKR ISDLYYKSDP
160 170 180 190 200
QYSARFTVPV LWDLETQTIV NNESSEIIRI LNSSAFDEFV DDDHKKTDLV
210 220 230 240 250
PAQLKTQIDD FNSWVYDSIN NGVYKTGFAE KAEVYESEVN NVFEHLDKVE
260 270 280 290 300
KILSDKYSKL KAKYGEEDRQ KILGEFFTVG DQLTEADIRL YTTVIRFDPV
310 320 330 340 350
YVQHFKCNFT SIRAGYPFIH LWVRNLYWNY DAFRYTTDFD HIKLHYTRSH
360 370
TRINPLGITP LGPKPDIRPL
Length:370
Mass (Da):43,274
Last modified:June 1, 1994 - v1
Checksum:i2ED6659ADD4CA6ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28301 Genomic DNA. Translation: CAA82155.1.
BK006944 Genomic DNA. Translation: DAA09226.1.
PIRiS38153.
RefSeqiNP_013002.3. NM_001179866.3.

Genome annotation databases

EnsemblFungiiYKR076W; YKR076W; YKR076W.
GeneIDi853951.
KEGGisce:YKR076W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28301 Genomic DNA. Translation: CAA82155.1.
BK006944 Genomic DNA. Translation: DAA09226.1.
PIRiS38153.
RefSeqiNP_013002.3. NM_001179866.3.

3D structure databases

ProteinModelPortaliP36156.
SMRiP36156. Positions 10-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34207. 9 interactions.
MINTiMINT-4493799.
STRINGi4932.YKR076W.

Proteomic databases

MaxQBiP36156.
PaxDbiP36156.
PeptideAtlasiP36156.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR076W; YKR076W; YKR076W.
GeneIDi853951.
KEGGisce:YKR076W.

Organism-specific databases

CYGDiYKR076w.
SGDiS000001784. ECM4.

Phylogenomic databases

eggNOGiCOG0435.
GeneTreeiENSGT00530000065151.
HOGENOMiHOG000245143.
InParanoidiP36156.
KOiK07393.
OMAiNSWVYDS.
OrthoDBiEOG722JK6.

Enzyme and pathway databases

BioCyciYEAST:G3O-32040-MONOMER.
SABIO-RKP36156.

Miscellaneous databases

NextBioi975356.

Gene expression databases

GenevestigatoriP36156.

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.
PROSITEiPS50405. GST_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae."
    Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J., Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C., Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M., Davies J., Klis F.M., Robbins P.W., Bussey H.
    Genetics 147:435-450(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, MUTAGENESIS OF CYS-46; ARG-51; GLU-173; SER-174; LEU-246; GLY-280 AND ASP-287.
  7. "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: SUBCELLULAR LOCATION, INDUCTION.

Entry informationi

Entry nameiGTO2_YEAST
AccessioniPrimary (citable) accession number: P36156
Secondary accession number(s): D6VXD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 7, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1670 molecules/cell in log phase SD medium.1 Publication
A version of this protein truncated after amino acid 200 is not active in the beta-hydroxyethyl disulfide (HED) assay.

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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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.