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Protein

Peroxiredoxin DOT5

Gene

DOT5

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. Has a role in telomere silencing, which is the repression of chromatin structure which leads to a stop in the transcription of nearby genes. Also has a role in the regulation of telomere length. Acts as an alkyl-hydroperoxide reductase in the nucleus during post-diauxic growth. Preferentially reduces alkyl-hydroperoxides rather than hydrogen peroxide. Acts as an antioxidant necessary for stationary phase survival.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 atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin.1 Publication
Present with 1840 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 6.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei107Cysteine 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
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:YIL010W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin DOT5Curated (EC:1.11.1.152 Publications)
Short name:
Prx
Alternative name(s):
Disrupter of telomere silencing protein 51 Publication
Nuclear thiol peroxidase1 Publication
Short name:
nTPx1 Publication
Thioredoxin peroxidase
Gene namesi
Name:DOT51 Publication
Ordered Locus Names:YIL010WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL010W.
SGDiS000001272. DOT5.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB-SubCell
  • nucleus Source: SGD

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107C → S: No TPx activity, no effect on DOT activity. 3 Publications1
Mutagenesisi112C → S: No TPx activity, no effect on DOT activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001351521 – 215Peroxiredoxin DOT5Add BLAST215

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi107 ↔ 112Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP40553.
PRIDEiP40553.

PTM databases

iPTMnetiP40553.

Expressioni

Inductioni

During the diauxic shift. In response to oxidative stress.1 Publication

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi34980. 61 interactors.
DIPiDIP-4762N.
IntActiP40553. 1 interactor.
MINTiMINT-485714.
STRINGi4932.YIL010W.

Structurei

Secondary structure

1215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi73 – 75Combined sources3
Beta strandi81 – 83Combined sources3
Helixi84 – 90Combined sources7
Beta strandi92 – 98Combined sources7
Beta strandi100 – 104Combined sources5
Helixi105 – 121Combined sources17
Turni122 – 124Combined sources3
Beta strandi126 – 132Combined sources7
Helixi135 – 145Combined sources11
Beta strandi148 – 153Combined sources6
Helixi158 – 163Combined sources6
Beta strandi166 – 171Combined sources6
Beta strandi176 – 181Combined sources6
Beta strandi184 – 191Combined sources8
Helixi194 – 211Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A4VX-ray1.80A57-215[»]
ProteinModelPortaliP40553.
SMRiP40553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40553.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 211ThioredoxinPROSITE-ProRule annotationAdd BLAST149

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000022344.
InParanoidiP40553.
KOiK03564.
OMAiVYPRAST.
OrthoDBiEOG092C5CGU.

Family and domain databases

InterProiView protein in InterPro
IPR000866. AhpC/TSA.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
PfamiView protein in Pfam
PF00578. AhpC-TSA. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS51352. THIOREDOXIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P40553-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEALRRSTR IAISKRMLEE EESKLAPIST PEVPKKKIKT GPKHNANQAV
60 70 80 90 100
VQEANRSSDV NELEIGDPIP DLSLLNEDND SISLKKITEN NRVVVFFVYP
110 120 130 140 150
RASTPGCTRQ ACGFRDNYQE LKKYAAVFGL SADSVTSQKK FQSKQNLPYH
160 170 180 190 200
LLSDPKREFI GLLGAKKTPL SGSIRSHFIF VDGKLKFKRV KISPEVSVND
210
AKKEVLEVAE KFKEE
Length:215
Mass (Da):24,120
Last modified:February 1, 1995 - v1
Checksum:iEB78A216891946C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38113 Genomic DNA. Translation: CAA86239.1.
AY558298 Genomic DNA. Translation: AAS56624.1.
BK006942 Genomic DNA. Translation: DAA08535.1.
PIRiS48445.
RefSeqiNP_012255.3. NM_001179360.3.

Genome annotation databases

EnsemblFungiiYIL010W; YIL010W; YIL010W.
GeneIDi854805.
KEGGisce:YIL010W.

Similar proteinsi

Entry informationi

Entry nameiDOT5_YEAST
AccessioniPrimary (citable) accession number: P40553
Secondary accession number(s): D6VVR9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: August 30, 2017
This is version 155 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names