P48239 (GTO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GTO1
Ordered Locus Names:	YGR154C
ORF Names:	G6664

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). Ref.4
Catalytic activity	RX + glutathione = HX + R-S-glutathione. Ref.4 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate. Ref.4
Subcellular location	Peroxisome Ref.5.
Induction	By diamide and 1-chloro-2,4-dinitrobenzene (CDNB) in a transcriptional factors YAP1 and/or MSN2/4-dependent manner. Ref.5
Disruption phenotype	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. Ref.5
Sequence similarities	Belongs to the GST superfamily. Omega family.
Biophysicochemical properties	Kinetic parameters: KM=1.13 mM for reduced glutathione (GSH) Ref.4

Ontologies

Keywords
Cellular component	Peroxisome
Domain	Coiled coil
Molecular function	Oxidoreductase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from sequence or structural similarity Ref.4. Source: SGD
Cellular_component	peroxisome Inferred from direct assay Ref.5. Source: SGD
Molecular_function	glutathione dehydrogenase (ascorbate) activity Inferred from electronic annotation. Source: EC glutathione transferase activity Inferred from direct assay Ref.4. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	Glutathione S-transferase omega-like 1		PRO_0000202833
Regions
	Coiled coil	214 – 257	44	Potential
Sites
	Active site	31	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P48239 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: B4639BD195CDF7F5	FASTA	356	41,301
	10 20 30 40 50 60 MSVSYKGTIS KTHSVFKPEK GRYYIYGALG CPFTHRAILA RSLKKLEPVL GLVLSHWQLD 70 80 90 100 110 120 SKGARFLPAP HRPEKYKERF FTATGGIASA KLDESEELGD VNNDSARLFV DGAFDPVENI 130 140 150 160 170 180 SRLSELYYLN DPKYPGTKFT VPVLWDSKTR KIVNNESGDI IRILNSGVFD EFIQSEETNV 190 200 210 220 230 240 IDLVPHDLID EIDKNIKWVH PKINLGVYKV GLAENGKIYE TEVKTLFENL QKMECVLKEN 250 260 270 280 290 300 YKRLEEQFSG NKQKILAKYF VLGQRLTEAD IRLYPSIIRF DVVYVQHFKC NLKTIRDGFP 310 320 330 340 350 YLHLWLINLY WNYAEFRFTT DFNHIKLFYI RMEVSRNKIN QFGIVPLGPK PDISRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X85807 Genomic DNA. Translation: CAA59811.1. Z72939 Genomic DNA. Translation: CAA97168.1. BK006941 Genomic DNA. Translation: DAA08245.1.
PIR	S60444.
RefSeq	NP_011670.3. NM_001181283.3.
3D structure databases
ProteinModelPortal	P48239.
SMR	P48239. Positions 16-353.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1867N.
IntAct	P48239. 2 interactions.
MINT	MINT-392461.
STRING	4932.YGR154C.
Proteomic databases
PaxDb	P48239.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR154C; YGR154C; YGR154C.
GeneID	853058.
KEGG	sce:YGR154C. sce:YGR161C.
Organism-specific databases
CYGD	YGR154c.
SGD	S000003386. GTO1.
Phylogenomic databases
eggNOG	COG0435.
GeneTree	ENSGT00530000065151.
HOGENOM	HOG000245143.
OMA	THADIKL.
OrthoDB	EOG4617CM.
Enzyme and pathway databases
SABIO-RK	P48239.
Gene expression databases
Genevestigator	P48239.
GermOnline	YGR154C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 2 hits.
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR016639. GST. IPR012336. Thioredoxin-like_fold. [Graphical view]
PANTHER	PTHR32419. PTHR32419. 1 hit.
PIRSF	PIRSF015753. GST. 1 hit.
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
ProtoNet	Search...
Other
NextBio	972989.

Entry information

Entry name

GTO1_YEAST

Accession

Primary (citable) accession number: P48239
Secondary accession number(s): D6VUT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program