P36014 · GPX1_YEAST
- ProteinGlutathione peroxidase-like peroxiredoxin 1
- GeneGPX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids167 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
Has peroxidase activity using thioredoxin or glutathione as a reducing power (PubMed:20572871, PubMed:22659048).
Involved in peroxisome formation (PubMed:22659048).
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.
Catalytic activity
- 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
141 μM | H2O2 | using glutathione as electron donor | ||||
75 μM | tert-butyl hydroperoxide | using glutathione as electron donor | ||||
120 μM | H2O2 | using thioredoxin as electron donor | ||||
223 μM | tert-butyl hydroperoxide | using glutathione as electron donor |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
2.98 μmol/min/mg | for H2O2 (using glutathione as electron donor) | ||||
0.579 μmol/min/mg | for tert-butyl hydroperoxide (using glutathione as electron donor) | ||||
0.739 μmol/min/mg | for H2O2 (using thioredoxin as electron donor) | ||||
1.25 μmol/min/mg | for tert-butyl hydroperoxide (using thioredoxin as electron donor) |
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 36 | Cysteine sulfenic acid (-SOH) intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | peroxisomal matrix | |
Molecular Function | glutathione peroxidase activity | |
Molecular Function | phospholipid-hydroperoxide glutathione peroxidase activity | |
Molecular Function | thioredoxin-dependent peroxiredoxin activity | |
Biological Process | cellular response to oxidative stress | |
Biological Process | peroxisome organization |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione peroxidase-like peroxiredoxin 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP36014
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion outer membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Impairs growth and peroxisome formation in oleic acid medium.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 36 | Prevents oxidation of the protein. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 7 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000066641 | 1-167 | Glutathione peroxidase-like peroxiredoxin 1 | |||
Sequence: MQEFYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQDKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGIKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPIIEELLNQPPEEQI | ||||||
Disulfide bond | 36↔82 | Redox-active | ||||
Sequence: CAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFC |
Keywords
- PTM
Proteomic databases
Expression
Induction
By glucose starvation.
Structure
Sequence
- Sequence statusComplete
- Length167
- Mass (Da)19,485
- Last updated1994-06-01 v1
- Checksum8C421FFF813391DD
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z28026 EMBL· GenBank· DDBJ | CAA81861.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY557895 EMBL· GenBank· DDBJ | AAS56221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006944 EMBL· GenBank· DDBJ | DAA09128.1 EMBL· GenBank· DDBJ | Genomic DNA |