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Protein

Peroxiredoxin PRX1, mitochondrial

Gene

PRX1

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

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 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 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

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

Kineticsi

  1. KM=6.2 µM for H2O21 Publication
  2. KM=10.9 µM for tert-butyl hydroperoxide1 Publication
  3. KM=8.1 µM for TRX31 Publication
  1. Vmax=8.5 µmol/min/mg enzyme for H2O21 Publication
  2. Vmax=7.4 µmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication
  3. 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 keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei91Cysteine sulfenic acid (-SOH) intermediate1 Publication1

GO - Molecular functioni

  • thioredoxin peroxidase activity Source: SGD

GO - Biological processi

  • cell redox homeostasis Source: SGD
  • cellular response to oxidative stress Source: SGD
  • response to cadmium ion Source: SGD

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciYEAST:G3O-28961-MONOMER.
ReactomeiR-SCE-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin PRX1, mitochondrialCurated (EC:1.11.1.151 Publication)
Short name:
Prx
Alternative name(s):
1-Cys PRX
Mitochondrial thiol peroxidase1 Publication
Short name:
mTPx1 Publication
Thioredoxin peroxidase
Gene namesi
Name:PRX11 Publication
Ordered Locus Names:YBL064C
ORF Names:YBL0503, YBL0524
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL064C.
SGDiS000000160. PRX1.

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

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi38C → S: Impairs dimer formation. 1 Publication1
Mutagenesisi91C → S: No activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 13MitochondrionSequence analysisAdd BLAST13
ChainiPRO_000013515114 – 261Peroxiredoxin PRX1, mitochondrialAdd BLAST248

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi38Interchain1 Publication
Modified residuei53PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP34227.
PRIDEiP34227.
TopDownProteomicsiP34227.

2D gel databases

UCD-2DPAGEiP34227.

PTM databases

iPTMnetiP34227.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication1 Publication

Protein-protein interaction databases

BioGridi32635. 68 interactors.
DIPiDIP-6412N.
IntActiP34227. 13 interactors.
MINTiMINT-642862.
STRINGi4932.YBL064C.

Structurei

3D structure databases

ProteinModelPortaliP34227.
SMRiP34227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini49 – 212ThioredoxinPROSITE-ProRule annotationAdd BLAST164

Sequence similaritiesi

Belongs to the peroxiredoxin family. Prx6 subfamily.Curated

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

GeneTreeiENSGT00550000074794.
HOGENOMiHOG000022346.
InParanoidiP34227.
KOiK03386.
OMAiMSAGRNF.
OrthoDBiEOG092C3W08.

Family and domain databases

InterProiView protein in InterPro
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
PfamiView protein in Pfam
PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS51352. THIOREDOXIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34227-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:261
Mass (Da):29,496
Last modified:February 1, 1994 - v1
Checksum:iF611A9ED85E4681A
GO

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.
PIRiS39825.
RefSeqiNP_009489.1. NM_001178304.1.

Genome annotation databases

EnsemblFungiiYBL064C; YBL064C; YBL064C.
GeneIDi852215.
KEGGisce:YBL064C.

Similar proteinsi

Entry informationi

Entry nameiPRX1_YEAST
AccessioniPrimary (citable) accession number: P34227
Secondary accession number(s): D6VPT6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 27, 2017
This is version 150 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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