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Protein

Glutathione peroxidase-like peroxiredoxin HYR1

Gene

HYR1

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

Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cerevisiae peroxiredoxins (GPX1, GPX2, and HYR1/GPX3) with respect to peroxide and lipid hydroperoxide reduction. The three enzymes are not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, HYR1/GPX3 is directly oxidized at Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then forms either an intramolecular disulfide bond (Cys-36 with Cys-82) or a transient, intermolecular disulfide bond with 'Cys-598' of YAP1, which is further resolved into a YAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598'), which causes its nuclear accumulation and activation, and a reduced Cys-36 in HYR1/GPX3.9 Publications

Miscellaneous

Present with 8000 molecules/cell in log phase SD medium.1 Publication
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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei36Cysteine sulfenic acid (-SOH) intermediate1 Publication1 Publication1

GO - Molecular functioni

  • glutathione peroxidase activity Source: SGD
  • peroxiredoxin activity Source: UniProtKB-EC
  • phospholipid-hydroperoxide glutathione peroxidase activity Source: SGD

GO - Biological processi

  • cellular response to oxidative stress Source: SGD

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciYEAST:YIR037W-MONOMER.
ReactomeiR-SCE-2142712. Synthesis of 12-eicosatetraenoic acid derivatives.
R-SCE-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.
R-SCE-3299685. Detoxification of Reactive Oxygen Species.
R-SCE-5628897. TP53 Regulates Metabolic Genes.
R-SCE-74259. Purine catabolism.

Protein family/group databases

PeroxiBasei3742. SceGPx03.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase-like peroxiredoxin HYR1Curated (EC:1.11.1.152 Publications)
Alternative name(s):
Glutathione peroxidase homolog 31 Publication
Short name:
GPx 3
Hydrogen peroxide resistance protein 11 Publication
Oxidant receptor peroxidase 11 Publication
Phospholipid hydroperoxide glutathione peroxidase 31 Publication
Short name:
PHGPx3
Gene namesi
Name:HYR11 Publication
Synonyms:GPX31 Publication, ORP11 Publication
Ordered Locus Names:YIR037WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIR037W.
SGDiS000001476. HYR1.

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

Cytoplasm, Mitochondrion, Peroxisome

Pathology & Biotechi

Disruption phenotypei

Sensitive to hydrogen peroxide and tert-butyl hydroperoxide (t-BHP).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi82C → S: Loss of enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000666431 – 163Glutathione peroxidase-like peroxiredoxin HYR1Add BLAST163

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi36 ↔ 82Redox-active1 Publication
Disulfide bondi36Interchain (with C-598 in YAP1); transient2 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP40581.
PRIDEiP40581.
TopDownProteomicsiP40581.

PTM databases

iPTMnetiP40581.

Expressioni

Inductioni

In contrast to the other two peroxiredoxins, HYR1/GPX3 expression is constitutive, not stress-induced.1 Publication

Interactioni

Subunit structurei

Interacts with YAP1 and probably YBP1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TMEM159Q96B963EBI-7869,EBI-7055862From Homo sapiens.

Protein-protein interaction databases

BioGridi35028. 79 interactors.
DIPiDIP-1275N.
IntActiP40581. 17 interactors.
MINTiMINT-401428.
STRINGi4932.YIR037W.

Structurei

Secondary structure

1163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Helixi19 – 22Combined sources4
Beta strandi26 – 36Combined sources11
Helixi39 – 52Combined sources14
Helixi53 – 55Combined sources3
Beta strandi57 – 64Combined sources8
Beta strandi97 – 100Combined sources4
Helixi105 – 113Combined sources9
Beta strandi117 – 119Combined sources3
Beta strandi129 – 132Combined sources4
Beta strandi134 – 136Combined sources3
Beta strandi138 – 142Combined sources5
Helixi148 – 151Combined sources4
Helixi152 – 159Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CMIX-ray2.02A1-163[»]
ProteinModelPortaliP40581.
SMRiP40581.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40581.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277054.
InParanoidiP40581.
KOiK00432.
OMAiIAQTCHI.
OrthoDBiEOG092C4H0P.

Family and domain databases

CDDicd00340. GSH_Peroxidase. 1 hit.
InterProiView protein in InterPro
IPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiView protein in Pfam
PF00255. GSHPx. 1 hit.
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.

Sequencei

Sequence statusi: Complete.

P40581-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEFYKLAPV DKKGQPFPFD QLKGKVVLIV NVASKCGFTP QYKELEALYK
60 70 80 90 100
RYKDEGFTII GFPCNQFGHQ EPGSDEEIAQ FCQLNYGVTF PIMKKIDVNG
110 120 130 140 150
GNEDPVYKFL KSQKSGMLGL RGIKWNFEKF LVDKKGKVYE RYSSLTKPSS
160
LSETIEELLK EVE
Length:163
Mass (Da):18,641
Last modified:February 1, 1995 - v1
Checksum:i46C42B81E895C1A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22446 Genomic DNA. Translation: AAA64283.1.
Z38061 Genomic DNA. Translation: CAA86197.1.
BK006942 Genomic DNA. Translation: DAA08584.1.
PIRiS48499.
RefSeqiNP_012303.1. NM_001179559.1.

Genome annotation databases

EnsemblFungiiYIR037W; YIR037W; YIR037W.
GeneIDi854855.
KEGGisce:YIR037W.

Similar proteinsi

Entry informationi

Entry nameiGPX3_YEAST
AccessioniPrimary (citable) accession number: P40581
Secondary accession number(s): D6VVW8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 27, 2017
This is version 154 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be a glutathione peroxidase (PubMed:10480913) or a phospholipid hydroperoxide glutathione peroxidase (PubMed:11445588), but functions as an atypical 2-Cys peroxiredoxin using thioredoxin as reducing power instead (PubMed:12437921).3 Publications

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