UniProtKB - P36014 (GPX1_YEAST)
Protein
Glutathione peroxidase-like peroxiredoxin 1
Gene
GPX1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588). Has peroxidase activity using thioredoxin or glutathione as a reducing power (PubMed:20572871, PubMed:22659048). Involved in peroxisome formation (PubMed:22659048).4 Publications
Miscellaneous
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
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 both glutathione and thioredoxin almost equally as reducing power instead (PubMed:20572871).3 Publications
Catalytic activityi
Kineticsi
- KM=141 µM for H2O2 (using glutathione as electron donor)1 Publication
- KM=75 µM for tert-butyl hydroperoxide (using glutathione as electron donor)1 Publication
- KM=120 µM for H2O2 (using thioredoxin as electron donor)1 Publication
- KM=223 µM for tert-butyl hydroperoxide (using glutathione as electron donor)1 Publication
- Vmax=2.98 µmol/min/mg enzyme for H2O2 (using glutathione as electron donor)1 Publication
- Vmax=0.579 µmol/min/mg enzyme for tert-butyl hydroperoxide (using glutathione as electron donor)1 Publication
- Vmax=0.739 µmol/min/mg enzyme for H2O2 (using thioredoxin as electron donor)1 Publication
- Vmax=1.25 µmol/min/mg enzyme for tert-butyl hydroperoxide (using thioredoxin as electron donor)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 36 | Cysteine sulfenic acid (-SOH) intermediate2 Publications | 1 |
GO - Molecular functioni
- glutathione peroxidase activity Source: SGD
- peroxidase activity Source: GO_Central
- phospholipid-hydroperoxide glutathione peroxidase activity Source: SGD
GO - Biological processi
- cellular response to oxidative stress Source: SGD
- peroxisome organization Source: SGD
Keywordsi
Molecular function | Antioxidant, Oxidoreductase, Peroxidase |
Protein family/group databases
PeroxiBasei | 3740, SceGPx01 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:GPX11 Publication Ordered Locus Names:YKL026CImported |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000001509, GPX1 |
VEuPathDBi | FungiDB:YKL026C |
Subcellular locationi
Mitochondrion
- Mitochondrion outer membrane ; Peripheral membrane protein 1 Publication
Peroxisome
- Peroxisome matrix 1 Publication
Cytosol
- cytosol Source: SGD
Mitochondrion
Peroxisome
- peroxisomal matrix Source: SGD
Keywords - Cellular componenti
Membrane, Mitochondrion, Mitochondrion outer membrane, PeroxisomePathology & Biotechi
Disruption phenotypei
Impairs growth and peroxisome formation in oleic acid medium.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 36 | C → S: Prevents oxidation of the protein. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000066641 | 1 – 167 | Glutathione peroxidase-like peroxiredoxin 1Add BLAST | 167 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 36 ↔ 82 | Redox-active1 Publication |
Keywords - PTMi
Disulfide bondProteomic databases
MaxQBi | P36014 |
PaxDbi | P36014 |
PRIDEi | P36014 |
Expressioni
Inductioni
By glucose starvation.1 Publication
Interactioni
Subunit structurei
Monomer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 34105, 31 interactors |
DIPi | DIP-5437N |
IntActi | P36014, 1 interactor |
MINTi | P36014 |
STRINGi | 4932.YKL026C |
Miscellaneous databases
RNActi | P36014, protein |
Family & Domainsi
Sequence similaritiesi
Belongs to the glutathione peroxidase family.Curated
Keywords - Domaini
Redox-active centerPhylogenomic databases
eggNOGi | KOG1651, Eukaryota |
GeneTreei | ENSGT00940000165680 |
HOGENOMi | CLU_029507_3_2_1 |
InParanoidi | P36014 |
OMAi | GKVVKFW |
Family and domain databases
CDDi | cd00340, GSH_Peroxidase, 1 hit |
Gene3Di | 3.40.30.10, 1 hit |
InterProi | View protein in InterPro IPR000889, Glutathione_peroxidase IPR029759, GPX_AS IPR029760, GPX_CS IPR036249, Thioredoxin-like_sf |
PANTHERi | PTHR11592, PTHR11592, 1 hit |
Pfami | View protein in Pfam PF00255, GSHPx, 1 hit |
PIRSFi | PIRSF000303, Glutathion_perox, 1 hit |
PRINTSi | PR01011, GLUTPROXDASE |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS00460, GLUTATHIONE_PEROXID_1, 1 hit PS00763, GLUTATHIONE_PEROXID_2, 1 hit PS51355, GLUTATHIONE_PEROXID_3, 1 hit |
i Sequence
Sequence statusi: Complete.
P36014-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MQEFYSFSPI DENGNPFPFN SLRNKVVLIV NVASHCAFTP QYKELEYLYE
60 70 80 90 100
KYKSHGLVIV AFPCGQFGNQ EFEKDKEINK FCQDKYGVTF PILHKIRCNG
110 120 130 140 150
QKQDPVYKFL KNSVSGKSGI KMIKWNFEKF VVDRNGKVVK RFSCMTRPLE
160
LCPIIEELLN QPPEEQI
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z28026 Genomic DNA Translation: CAA81861.1 AY557895 Genomic DNA Translation: AAS56221.1 BK006944 Genomic DNA Translation: DAA09128.1 |
PIRi | S37843 |
RefSeqi | NP_012899.3, NM_001179592.3 |
Genome annotation databases
EnsemblFungii | YKL026C_mRNA; YKL026C; YKL026C |
GeneIDi | 853842 |
KEGGi | sce:YKL026C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z28026 Genomic DNA Translation: CAA81861.1 AY557895 Genomic DNA Translation: AAS56221.1 BK006944 Genomic DNA Translation: DAA09128.1 |
PIRi | S37843 |
RefSeqi | NP_012899.3, NM_001179592.3 |
3D structure databases
SMRi | P36014 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 34105, 31 interactors |
DIPi | DIP-5437N |
IntActi | P36014, 1 interactor |
MINTi | P36014 |
STRINGi | 4932.YKL026C |
Protein family/group databases
PeroxiBasei | 3740, SceGPx01 |
Proteomic databases
MaxQBi | P36014 |
PaxDbi | P36014 |
PRIDEi | P36014 |
Genome annotation databases
EnsemblFungii | YKL026C_mRNA; YKL026C; YKL026C |
GeneIDi | 853842 |
KEGGi | sce:YKL026C |
Organism-specific databases
SGDi | S000001509, GPX1 |
VEuPathDBi | FungiDB:YKL026C |
Phylogenomic databases
eggNOGi | KOG1651, Eukaryota |
GeneTreei | ENSGT00940000165680 |
HOGENOMi | CLU_029507_3_2_1 |
InParanoidi | P36014 |
OMAi | GKVVKFW |
Miscellaneous databases
PROi | PR:P36014 |
RNActi | P36014, protein |
Family and domain databases
CDDi | cd00340, GSH_Peroxidase, 1 hit |
Gene3Di | 3.40.30.10, 1 hit |
InterProi | View protein in InterPro IPR000889, Glutathione_peroxidase IPR029759, GPX_AS IPR029760, GPX_CS IPR036249, Thioredoxin-like_sf |
PANTHERi | PTHR11592, PTHR11592, 1 hit |
Pfami | View protein in Pfam PF00255, GSHPx, 1 hit |
PIRSFi | PIRSF000303, Glutathion_perox, 1 hit |
PRINTSi | PR01011, GLUTPROXDASE |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS00460, GLUTATHIONE_PEROXID_1, 1 hit PS00763, GLUTATHIONE_PEROXID_2, 1 hit PS51355, GLUTATHIONE_PEROXID_3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GPX1_YEAST | |
Accessioni | P36014Primary (citable) accession number: P36014 Secondary accession number(s): D6VXQ8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
Last sequence update: | June 1, 1994 | |
Last modified: | February 10, 2021 | |
This is version 166 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XI
Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names - SIMILARITY comments
Index of protein domains and families