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Protein

Glutathione peroxidase-like peroxiredoxin 2

Gene

GPX2

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

Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588). Plays an important role in the oxidative stress-induced response in the presence of Ca2+. Has peroxidase activity using preferentially thioredoxin as a reducing power. The redox state of the mitochondrial GPX2 is regulated by TRX1 and TRX2 (cytoplasmic thioredoxin), and by TRX3 (mitochondrial matrix thioredoxin) (PubMed:16251189). Involved in sporulation (PubMed:21763276).4 Publications

Miscellaneous

Present with 2010 molecules/cell in log phase SD medium.1 Publication
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide.1 Publication

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.1 Publication

Kineticsi

  1. KM=170 µM for H2O2 (using glutathione as electron donor)1 Publication
  2. KM=313 µM for tert-butyl hydroperoxide (using glutathione as electron donor)1 Publication
  3. KM=20 µM for H2O2 (using thioredoxin as electron donor)1 Publication
  4. KM=62.5 µM for tert-butyl hydroperoxide (using glutathione as electron donor)1 Publication
  1. Vmax=0.27 µmol/min/mg enzyme for H2O2 (using glutathione as electron donor)1 Publication
  2. Vmax=0.295 µmol/min/mg enzyme for tert-butyl hydroperoxide (using glutathione as electron donor)1 Publication
  3. Vmax=2.6 µmol/min/mg enzyme for H2O2 (using thioredoxin as electron donor)1 Publication
  4. Vmax=1 µmol/min/mg enzyme for tert-butyl hydroperoxide (using thioredoxin as electron donor)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei37Cysteine sulfenic acid (-SOH) intermediate1 Publication1

GO - Molecular functioni

  • glutathione peroxidase activity Source: SGD
  • peroxiredoxin activity Source: UniProtKB-EC
  • phospholipid-hydroperoxide glutathione peroxidase activity Source: SGD

GO - Biological processi

  • cellular response to oxidative stress Source: SGD

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciYEAST:YBR244W-MONOMER.

Protein family/group databases

PeroxiBasei3741. SceGPx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase-like peroxiredoxin 21 Publication (EC:1.11.1.151 Publication)
Alternative name(s):
Glutathione peroxidase homolog 21 Publication
Short name:
GPx 2
Gene namesi
Name:GPX21 Publication
Ordered Locus Names:YBR244WImported
ORF Names:YBR1632
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR244W.
SGDiS000000448. GPX2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi37C → A: Prevents oxidation of the protein. 1 Publication1
Mutagenesisi83C → A: Prevents oxidation of the protein. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000666421 – 162Glutathione peroxidase-like peroxiredoxin 2Add BLAST162

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi37 ↔ 83Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP38143.
PRIDEiP38143.

PTM databases

iPTMnetiP38143.

Expressioni

Inductioni

By oxidative stress, dependent on transcription factor YAP1 (PubMed:10480913). By oleic acid (PubMed:21763276).2 Publications

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi32939. 68 interactors.
DIPiDIP-8180N.
IntActiP38143. 13 interactors.
MINTiMINT-385855.
STRINGi4932.YBR244W.

Structurei

3D structure databases

ProteinModelPortaliP38143.
SMRiP38143.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00840000130500.
HOGENOMiHOG000277054.
InParanoidiP38143.
KOiK00432.
OMAiVTFPIFH.
OrthoDBiEOG092C4H0P.

Family and domain databases

CDDicd00340. GSH_Peroxidase. 1 hit.
InterProiView protein in InterPro
IPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiView protein in Pfam
PF00255. GSHPx. 1 hit.
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.

Sequencei

Sequence statusi: Complete.

P38143-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSFYDLEC KDKKGESFKF DQLKGKVVLI VNVASKCGFT PQYKELEELY
60 70 80 90 100
KKYQDKGFVI LGFPCNQFGK QEPGSDEQIT EFCQLNYGVT FPIMKKIDVN
110 120 130 140 150
GSNADSVYNY LKSQKAGLLG FKGIKWNFEK FLVDSNGKVV QRFSSLTKPS
160
SLDQEIQSLL SK
Length:162
Mass (Da):18,406
Last modified:October 1, 1994 - v1
Checksum:iBD02E7E6D38527A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36113 Genomic DNA. Translation: CAA85207.1.
AY557641 Genomic DNA. Translation: AAS55967.1.
BK006936 Genomic DNA. Translation: DAA07360.1.
PIRiS46121.
RefSeqiNP_009803.3. NM_001178592.3.

Genome annotation databases

EnsemblFungiiYBR244W; YBR244W; YBR244W.
GeneIDi852546.
KEGGisce:YBR244W.

Similar proteinsi

Entry informationi

Entry nameiGPX2_YEAST
AccessioniPrimary (citable) accession number: P38143
Secondary accession number(s): D6VQP0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: September 27, 2017
This is version 152 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be a glutathione peroxidase (PubMed:10480913) or a phospholipid hydroperoxide glutathione peroxidase (PubMed:11445588), but functions as an atypical 2-Cys peroxiredoxin using thioredoxin as reducing power instead (PubMed:16251189).3 Publications

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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names