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Protein

Peroxiredoxin TSA2

Gene

TSA2

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 (PubMed:10681558, PubMed:11741925, PubMed:15210711). Can act alternatively as peroxidase and molecular chaperone. Oxidative stress and heat shock exposure cause a reversible shift of the protein structure from low MW species to high MW complexes, triggering a peroxidase-to-chaperone functional switch. The chaperone function of the protein enhances resistance to heat shock (PubMed:15163410).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 typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.By similarity
Present with 4820 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=13.8 µM for H2O21 Publication
  2. KM=4.5 µM for cumene hydroperoxide1 Publication
  3. KM=5.1 µM for tert-butyl hydroperoxide1 Publication
  1. Vmax=0.39 µM/sec/mg enzyme for H2O21 Publication
  2. Vmax=0.28 µM/sec/mg enzyme for cumene hydroperoxide1 Publication
  3. Vmax=0.29 µM/sec/mg enzyme for tert-butyl hydroperoxide1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei48Cysteine sulfenic acid (-SOH) intermediate1 Publication1

GO - Molecular functioni

  • peroxiredoxin activity Source: SGD
  • thioredoxin peroxidase activity Source: SGD

GO - Biological processi

  • cell redox homeostasis Source: SGD
  • cellular response to oxidative stress Source: SGD
  • protein folding Source: SGD
  • protein stabilization Source: CAFA

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciYEAST:YDR453C-MONOMER.
ReactomeiR-SCE-3299685. Detoxification of Reactive Oxygen Species.
R-SCE-5628897. TP53 Regulates Metabolic Genes.
R-SCE-6798695. Neutrophil degranulation.

Protein family/group databases

MoonProtiQ04120.
PeroxiBasei4467. Sce2CysPrx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin TSA2Curated (EC:1.11.1.151 Publication)
Short name:
Prx
Alternative name(s):
Cytoplasmic thiol peroxidase 21 Publication
Short name:
cTPx 21 Publication
Thiol-specific antioxidant protein 2
Thioredoxin peroxidase type Ib1 Publication
Short name:
TPx type Ib
Gene namesi
Name:TSA21 Publication
Ordered Locus Names:YDR453CImported
ORF Names:D9461.38
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR453C.
SGDiS000002861. TSA2.

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi48C → S: No activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001350961 – 196Peroxiredoxin TSA2Add BLAST196

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Disulfide bondi48Interchain (with C-171); in linked formCombined sources1 Publication
Cross-linki89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Disulfide bondi171Interchain (with C-48); in linked formCombined sources1 Publication
Modified residuei174PhosphothreonineBy similarity1

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ04120.
PRIDEiQ04120.
TopDownProteomicsiQ04120.

Expressioni

Inductioni

By peroxides.1 Publication

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation.By similarity

Protein-protein interaction databases

BioGridi32508. 59 interactors.
DIPiDIP-4317N.
IntActiQ04120. 9 interactors.
MINTiMINT-535451.
STRINGi4932.YDR453C.

Structurei

Secondary structure

1196
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 18Combined sources6
Beta strandi21 – 27Combined sources7
Helixi28 – 30Combined sources3
Beta strandi33 – 39Combined sources7
Beta strandi45 – 47Combined sources3
Helixi48 – 57Combined sources10
Helixi59 – 64Combined sources6
Beta strandi67 – 75Combined sources9
Helixi77 – 85Combined sources9
Turni88 – 91Combined sources4
Beta strandi100 – 102Combined sources3
Helixi107 – 111Combined sources5
Turni117 – 119Combined sources3
Beta strandi124 – 129Combined sources6
Beta strandi133 – 141Combined sources9
Helixi149 – 165Combined sources17
Turni184 – 186Combined sources3
Helixi187 – 193Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5DVBX-ray2.20A/B/C/D/E/F/G/H/I/J1-196[»]
5EPTX-ray5.00A/B/C/D/E/F/G/H/I/J1-196[»]
ProteinModelPortaliQ04120.
SMRiQ04120.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 161ThioredoxinPROSITE-ProRule annotationAdd BLAST159

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
InParanoidiQ04120.
KOiK03386.
OMAiCPANWEE.
OrthoDBiEOG092C53IH.

Family and domain databases

InterProiView protein in InterPro
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR036249. Thioredoxin-like_sf.
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.

Q04120-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAEVQKQAP PFKKTAVVDG IFEEISLEKY KGKYVVLAFV PLAFSFVCPT
60 70 80 90 100
EIVAFSDAAK KFEDQGAQVL FASTDSEYSL LAWTNLPRKD GGLGPVKVPL
110 120 130 140 150
LADKNHSLSR DYGVLIEKEG IALRGLFIID PKGIIRHITI NDLSVGRNVN
160 170 180 190
EALRLVEGFQ WTDKNGTVLP CNWTPGAATI KPDVKDSKEY FKNANN
Length:196
Mass (Da):21,615
Last modified:January 23, 2007 - v3
Checksum:i43CC57C92081D745
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64886.1.
BK006938 Genomic DNA. Translation: DAA12288.1.
PIRiS69732.
RefSeqiNP_010741.1. NM_001180761.1.

Genome annotation databases

EnsemblFungiiYDR453C; YDR453C; YDR453C.
GeneIDi852064.
KEGGisce:YDR453C.

Similar proteinsi

Entry informationi

Entry nameiTSA2_YEAST
AccessioniPrimary (citable) accession number: Q04120
Secondary accession number(s): D6VT78
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 147 of the entry and version 3 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names