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UniProtKB - P34227 (PRX1_YEAST)
Protein
Peroxiredoxin PRX1, mitochondrial
Gene
PRX1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Involved in mitochondrial protection of cadmium-induced oxidative stress.
3 PublicationsMiscellaneous
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 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule. C(P) is reactivated by glutathionylation and subsequent reduction by either glutaredoxin GRX2 or thioredoxin reductase TRR2, coupled with reduced glutathione (GSH).2 Publications
Present with 4510 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
Kineticsi
- KM=6.2 µM for H2O21 Publication
- KM=10.9 µM for tert-butyl hydroperoxide1 Publication
- KM=8.1 µM for TRX31 Publication
- Vmax=8.5 µmol/min/mg enzyme for H2O21 Publication
- Vmax=7.4 µmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication
- Vmax=9.5 µmol/min/mg enzyme for TRX31 Publication
pH dependencei
Optimum pH is 7.0 (PubMed:10821871). Optimum pH is 8.5 (using glutaredoxin as electron donor) (PubMed:20059400).2 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 91 | Cysteine sulfenic acid (-SOH) intermediate1 Publication | 1 |
GO - Molecular functioni
- peroxidase activity Source: GO_Central
- thioredoxin peroxidase activity Source: SGD
GO - Biological processi
- cell redox homeostasis Source: SGD
- cellular response to oxidative stress Source: SGD
- regulation of hydrogen peroxide-induced cell death Source: SGD
- response to cadmium ion Source: SGD
Keywordsi
Molecular function | Antioxidant, Oxidoreductase, Peroxidase |
Enzyme and pathway databases
BRENDAi | 1.11.1.25, 984 |
Reactomei | R-SCE-6798695, Neutrophil degranulation |
Names & Taxonomyi
Protein namesi | Recommended name: Peroxiredoxin PRX1, mitochondrialCurated (EC:1.11.1.251 Publication, EC:1.11.1.271 Publication)Short name: Prx Alternative name(s): 1-Cys PRX Glutaredoxin-dependent peroxiredoxinCurated Glutathione-dependent peroxiredoxinCurated Mitochondrial thiol peroxidase1 Publication Short name: mTPx1 Publication Thioredoxin peroxidase |
Gene namesi | Name:PRX11 Publication Ordered Locus Names:YBL064C ORF Names:YBL0503, YBL0524 |
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 | S000000160, PRX1 |
VEuPathDBi | FungiDB:YBL064C |
Subcellular locationi
Mitochondrion
- Mitochondrion 2 Publications
Cytosol
- cytosol Source: GO_Central
Mitochondrion
- mitochondrion Source: SGD
Keywords - Cellular componenti
MitochondrionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 38 | C → S: Impairs dimer formation. 1 Publication | 1 | |
Mutagenesisi | 91 | C → S: No activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 13 | MitochondrionSequence analysisAdd BLAST | 13 | |
ChainiPRO_0000135151 | 14 – 261 | Peroxiredoxin PRX1, mitochondrialAdd BLAST | 248 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 38 | Interchain1 Publication | ||
Modified residuei | 53 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
Disulfide bond, PhosphoproteinProteomic databases
MaxQBi | P34227 |
PaxDbi | P34227 |
PRIDEi | P34227 |
TopDownProteomicsi | P34227 |
2D gel databases
UCD-2DPAGEi | P34227 |
PTM databases
iPTMneti | P34227 |
Interactioni
Subunit structurei
Homodimer; disulfide-linked.
1 Publication1 PublicationProtein-protein interaction databases
BioGRIDi | 32635, 82 interactors |
DIPi | DIP-6412N |
IntActi | P34227, 12 interactors |
MINTi | P34227 |
STRINGi | 4932.YBL064C |
Miscellaneous databases
RNActi | P34227, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P34227 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 49 – 212 | ThioredoxinPROSITE-ProRule annotationAdd BLAST | 164 |
Sequence similaritiesi
Keywords - Domaini
Redox-active center, Transit peptidePhylogenomic databases
eggNOGi | KOG0854, Eukaryota |
GeneTreei | ENSGT00940000171910 |
HOGENOMi | CLU_042529_4_2_1 |
InParanoidi | P34227 |
OMAi | KVMVIPS |
Family and domain databases
CDDi | cd03016, PRX_1cys, 1 hit |
InterProi | View protein in InterPro IPR000866, AhpC/TSA IPR024706, Peroxiredoxin_AhpC-typ IPR019479, Peroxiredoxin_C IPR045020, PRX_1cys IPR036249, Thioredoxin-like_sf IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF10417, 1-cysPrx_C, 1 hit PF00578, AhpC-TSA, 1 hit |
PIRSFi | PIRSF000239, AHPC, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS51352, THIOREDOXIN_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P34227-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFSRICSAQL KRTAWTLPKQ AHLQSQTIKT FATAPILCKQ FKQSDQPRLR
60 70 80 90 100
INSDAPNFDA DTTVGKINFY DYLGDSWGVL FSHPADFTPV CTTEVSAFAK
110 120 130 140 150
LKPEFDKRNV KLIGLSVEDV ESHEKWIQDI KEIAKVKNVG FPIIGDTFRN
160 170 180 190 200
VAFLYDMVDA EGFKNINDGS LKTVRSVFVI DPKKKIRLIF TYPSTVGRNT
210 220 230 240 250
SEVLRVIDAL QLTDKEGVVT PINWQPADDV IIPPSVSNDE AKAKFGQFNE
260
IKPYLRFTKS K
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z23261 Genomic DNA Translation: CAA80784.1 Z35825 Genomic DNA Translation: CAA84884.1 BK006936 Genomic DNA Translation: DAA07056.1 |
PIRi | S39825 |
RefSeqi | NP_009489.1, NM_001178304.1 |
Genome annotation databases
EnsemblFungii | YBL064C_mRNA; YBL064C; YBL064C |
GeneIDi | 852215 |
KEGGi | sce:YBL064C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z23261 Genomic DNA Translation: CAA80784.1 Z35825 Genomic DNA Translation: CAA84884.1 BK006936 Genomic DNA Translation: DAA07056.1 |
PIRi | S39825 |
RefSeqi | NP_009489.1, NM_001178304.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5YKJ | X-ray | 1.53 | A | 49-261 | [»] | |
5YKW | X-ray | 2.08 | B | 88-95 | [»] | |
SMRi | P34227 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 32635, 82 interactors |
DIPi | DIP-6412N |
IntActi | P34227, 12 interactors |
MINTi | P34227 |
STRINGi | 4932.YBL064C |
PTM databases
iPTMneti | P34227 |
2D gel databases
UCD-2DPAGEi | P34227 |
Proteomic databases
MaxQBi | P34227 |
PaxDbi | P34227 |
PRIDEi | P34227 |
TopDownProteomicsi | P34227 |
Genome annotation databases
EnsemblFungii | YBL064C_mRNA; YBL064C; YBL064C |
GeneIDi | 852215 |
KEGGi | sce:YBL064C |
Organism-specific databases
SGDi | S000000160, PRX1 |
VEuPathDBi | FungiDB:YBL064C |
Phylogenomic databases
eggNOGi | KOG0854, Eukaryota |
GeneTreei | ENSGT00940000171910 |
HOGENOMi | CLU_042529_4_2_1 |
InParanoidi | P34227 |
OMAi | KVMVIPS |
Enzyme and pathway databases
BRENDAi | 1.11.1.25, 984 |
Reactomei | R-SCE-6798695, Neutrophil degranulation |
Miscellaneous databases
PROi | PR:P34227 |
RNActi | P34227, protein |
Family and domain databases
CDDi | cd03016, PRX_1cys, 1 hit |
InterProi | View protein in InterPro IPR000866, AhpC/TSA IPR024706, Peroxiredoxin_AhpC-typ IPR019479, Peroxiredoxin_C IPR045020, PRX_1cys IPR036249, Thioredoxin-like_sf IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF10417, 1-cysPrx_C, 1 hit PF00578, AhpC-TSA, 1 hit |
PIRSFi | PIRSF000239, AHPC, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS51352, THIOREDOXIN_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PRX1_YEAST | |
Accessioni | P34227Primary (citable) accession number: P34227 Secondary accession number(s): D6VPT6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1994 |
Last sequence update: | February 1, 1994 | |
Last modified: | February 23, 2022 | |
This is version 179 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
3D-structure, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome II
Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families