Peroxiredoxin HYR1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40581 (GPX3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Peroxiredoxin HYR1
EC=1.11.1.15

Alternative name(s):
Glutathione peroxidase 3
Hydrogen peroxide resistance protein 1
Oxidant receptor peroxidase 1
Phospholipid hydroperoxide glutathione peroxidase 3
Short name=PHGPx3

Gene names

Name:	HYR1
Synonyms:	GPX3, ORP1
Ordered Locus Names:	YIR037W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	163 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 HYP1/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, HYP1 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') and a reduced Cys-36 in HYP1/GPX3. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH. Ref.15
Subunit structure	Interacts with YAP1 and probably YBP1. Ref.10
Subcellular location	Cytoplasm Ref.13.
Induction	In contrast to the other two peroxiredoxins, HYP1/GPX3 expression is constitutive, not stress-induced. Ref.5
Post-translational modification	Reversible disulfide bond formation between Cys-36 and Cys-82 upon peroxide reduction; probably reverted by thioredoxin (TRX2).
Miscellaneous	Present with 8000 molecules/cell in log phase SD medium. Ref.14
Sequence similarities	Belongs to the glutathione peroxidase family.
Caution	Was originally thought to be a glutathione peroxidase or a phospholipid hydroperoxide glutathione peroxidase. HYP1 does not require glutathione for hydroperoxide reduction.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to oxidative stress Inferred from mutant phenotype Ref.6. Source: SGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione peroxidase activity Inferred from mutant phenotype Ref.5. Source: SGD peroxiredoxin activity Inferred from electronic annotation. Source: EC phospholipid-hydroperoxide glutathione peroxidase activity Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
ADE17	P38009	1	EBI-7869,EBI-14223
ALO1	P54783	1	EBI-7869,EBI-2519
CAR2	P07991	1	EBI-7869,EBI-12430
ERG11	P10614	1	EBI-7869,EBI-5127
GAP1	P19145	1	EBI-7869,EBI-7314
GLN1	P32288	1	EBI-7869,EBI-7665
HXT7	P39004	1	EBI-7869,EBI-8790
PDR12	Q02785	1	EBI-7869,EBI-13065
PEX11	Q12462	1	EBI-7869,EBI-13198
PMP2	P40975	1	EBI-7869,EBI-2043041
PMP3	P87284	1	EBI-7869,EBI-13555
RNR2	P09938	1	EBI-7869,EBI-15240
YBL039W-B	P0C268	1	EBI-7869,EBI-2044092

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 163

163

Peroxiredoxin HYR1

PRO_0000066643

Sites

Active site

Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Disulfide bond

36 ↔ 82

Redox-active

Disulfide bond

Interchain (with C-598 in YAP1); transient

Experimental info

Mutagenesis

C → S: Loss of enzyme activity. Ref.15

Secondary structure

163

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P40581 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 46C42B81E895C1A3
Show »

FASTA

163

18,641

        10         20         30         40         50         60 
MSEFYKLAPV DKKGQPFPFD QLKGKVVLIV NVASKCGFTP QYKELEALYK RYKDEGFTII 

        70         80         90        100        110        120 
GFPCNQFGHQ EPGSDEEIAQ FCQLNYGVTF PIMKKIDVNG GNEDPVYKFL KSQKSGMLGL 

       130        140        150        160 
RGIKWNFEKF LVDKKGKVYE RYSSLTKPSS LSETIEELLK EVE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and phenotypic characterization of a glutathione-peroxidase like gene involved in the oxidative stress response of Saccharomyces cerevisiae." Budde E., Stahl U. Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38626 / AH22 / NRRL Y-12843.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. Barrell B.G. Nature 387:84-87(1997) [PubMed: 9169870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Phospholipid hydroperoxide glutathione peroxidase (PHGPx): more than an antioxidant enzyme?" Ursini F., Maiorino M., Roveri A. Biomed. Environ. Sci. 10:327-332(1997) [PubMed: 9315326] [Abstract] Cited for: FUNCTION, PROTEIN OXIDATION.
[5]	"Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae." Inoue Y., Matsuda T., Sugiyama K., Izawa S., Kimura A. J. Biol. Chem. 274:27002-27009(1999) [PubMed: 10480913] [Abstract] Cited for: FUNCTION, INDUCTION.
[6]	"Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases." Avery A.M., Avery S.V. J. Biol. Chem. 276:33730-33735(2001) [PubMed: 11445588] [Abstract] Cited for: FUNCTION, FUNCTION AS A PHGPX.
[7]	"The yeast glutaredoxins are active as glutathione peroxidases." Collinson E.J., Wheeler G.L., Garrido E.O., Avery A.M., Avery S.V., Grant C.M. J. Biol. Chem. 277:16712-16717(2002) [PubMed: 11875065] [Abstract] Cited for: FUNCTION AS A GLUTAREDOXIN.
[8]	"A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation." Delaunay A., Pflieger D., Barrault M.-B., Vinh J., Toledano M.B. Cell 111:471-481(2002) [PubMed: 12437921] [Abstract] Cited for: FUNCTION, OXIDATION OF YAP1.
[9]	"Structure, mechanism and regulation of peroxiredoxins." Wood Z.A., Schroder E., Robin Harris J., Poole L.B. Trends Biochem. Sci. 28:32-40(2003) [PubMed: 12517450] [Abstract] Cited for: FUNCTION AS A PEROXIREDOXIN.
[10]	"Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor." Veal E.A., Ross S.J., Malakasi P., Peacock E., Morgan B.A. J. Biol. Chem. 278:30896-30904(2003) [PubMed: 12743123] [Abstract] Cited for: FUNCTION, INTERACTION WITH YBP1.
[11]	"Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling." Azevedo D., Tacnet F., Delaunay A., Rodrigues-Pousada C., Toledano M.B. Free Radic. Biol. Med. 35:889-900(2003) [PubMed: 14556853] [Abstract] Cited for: FUNCTION, ACTIVATING SUBSTANCES.
[12]	"Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress." Carmel-Harel O., Storz G. Annu. Rev. Microbiol. 54:439-461(2000) [PubMed: 11018134] [Abstract] Cited for: REVIEW.
[13]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[14]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[15]	"Crystal structure of glutathione-dependent phospholipid peroxidase Hyr1 from the yeast Saccharomyces cerevisiae." Zhang W.J., He Y.-X., Yang Z., Yu J., Chen Y., Zhou C.-Z. Proteins 73:1058-1062(2008) [PubMed: 18767166] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-82.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U22446 Genomic DNA. Translation: AAA64283.1.
Z38061 Genomic DNA. Translation: CAA86197.1.
BK006942 Genomic DNA. Translation: DAA08584.1.

PIR

S48499.

RefSeq

NP_012303.1. NM_001179559.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CMI	X-ray	2.02	A	1-163	[»]

ProteinModelPortal

P40581.

SMR

P40581. Positions 2-162.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1275N.

IntAct

P40581. 17 interactions.

MINT

MINT-401428.

STRING

P40581.

Protein family/group databases

PeroxiBase

3742. SceGPx03.

Proteomic databases

PeptideAtlas

P40581.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YIR037W; YIR037W; YIR037W.

GeneID

854855.

KEGG

sce:YIR037W.

NMPDR

fig|4932.3.peg.1848.

Organism-specific databases

CYGD

YIR037w.

SGD

S000001476. HYR1.

Phylogenomic databases

eggNOG

fuNOG08894.

GeneTree

EFGT00050000003335.

HOGENOM

HBG648990.

OMA

QEYKDQG.

OrthoDB

EOG4QRMDK.

Gene expression databases

ArrayExpress

P40581.

Genevestigator

P40581.

GermOnline

YIR037W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000889. Glutathione_peroxidase.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

K00432.

PANTHER

PTHR11592. Glut_peroxidase. 1 hit.

Pfam

PF00255. GSHPx. 1 hit.
[Graphical view]

PIRSF

PIRSF000303. Glutathion_perox. 1 hit.

PRINTS

PR01011. GLUTPROXDASE.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

977764.

Entry information

Entry name

GPX3_YEAST

Accession

Primary (citable) accession number: P40581
Secondary accession number(s): D6VVW8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents