Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P36014 (GPX1_YEAST)

Entry version 166 (10 Feb 2021)
Sequence version 1 (01 Jun 1994)
Previous versions | rss
Add a publicationFeedback
Protein

Glutathione peroxidase-like peroxiredoxin 1

Gene

GPX1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588). Has peroxidase activity using thioredoxin or glutathione as a reducing power (PubMed:20572871, PubMed:22659048). Involved in peroxisome formation (PubMed:22659048).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 atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide.1 Publication

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 both glutathione and thioredoxin almost equally as reducing power instead (PubMed:20572871).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=141 µM for H2O2 (using glutathione as electron donor)1 Publication
  2. KM=75 µM for tert-butyl hydroperoxide (using glutathione as electron donor)1 Publication
  3. KM=120 µM for H2O2 (using thioredoxin as electron donor)1 Publication
  4. KM=223 µM for tert-butyl hydroperoxide (using glutathione as electron donor)1 Publication
  1. Vmax=2.98 µmol/min/mg enzyme for H2O2 (using glutathione as electron donor)1 Publication
  2. Vmax=0.579 µmol/min/mg enzyme for tert-butyl hydroperoxide (using glutathione as electron donor)1 Publication
  3. Vmax=0.739 µmol/min/mg enzyme for H2O2 (using thioredoxin as electron donor)1 Publication
  4. Vmax=1.25 µmol/min/mg enzyme for tert-butyl hydroperoxide (using thioredoxin as electron donor)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei36Cysteine sulfenic acid (-SOH) intermediate2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • glutathione peroxidase activity Source: SGD
  • peroxidase activity Source: GO_Central
  • phospholipid-hydroperoxide glutathione peroxidase activity Source: SGD
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Protein family/group databases

PeroxiBase, a peroxidase database

More...PeroxiBasei		3740, SceGPx01

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glutathione peroxidase-like peroxiredoxin 1Curated (EC:1.11.1.242 Publications, EC:1.11.1.92 Publications)
Alternative name(s):
Glutathione peroxidase homolog 11 Publication
Short name:
GPx 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GPX11 Publication
Ordered Locus Names:YKL026CImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XI

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000001509, GPX1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YKL026C

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Impairs growth and peroxisome formation in oleic acid medium.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi36C → S: Prevents oxidation of the protein. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000666411 – 167Glutathione peroxidase-like peroxiredoxin 1Add BLAST167

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi36 ↔ 82Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P36014

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P36014

PRoteomics IDEntifications database

More...PRIDEi		P36014

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By glucose starvation.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		34105, 31 interactors

Database of interacting proteins

More...DIPi		DIP-5437N

Protein interaction database and analysis system

More...IntActi		P36014, 1 interactor

Molecular INTeraction database

More...MINTi		P36014

STRING: functional protein association networks

More...STRINGi		4932.YKL026C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P36014, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P36014

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1651, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000165680

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_029507_3_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P36014

Identification of Orthologs from Complete Genome Data

More...OMAi		GKVVKFW

Family and domain databases

Conserved Domains Database

More...CDDi		cd00340, GSH_Peroxidase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.30.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000889, Glutathione_peroxidase
IPR029759, GPX_AS
IPR029760, GPX_CS
IPR036249, Thioredoxin-like_sf

The PANTHER Classification System

More...PANTHERi		PTHR11592, PTHR11592, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00255, GSHPx, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000303, Glutathion_perox, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01011, GLUTPROXDASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52833, SSF52833, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00460, GLUTATHIONE_PEROXID_1, 1 hit
PS00763, GLUTATHIONE_PEROXID_2, 1 hit
PS51355, GLUTATHIONE_PEROXID_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P36014-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQEFYSFSPI DENGNPFPFN SLRNKVVLIV NVASHCAFTP QYKELEYLYE 
        60         70         80         90        100
KYKSHGLVIV AFPCGQFGNQ EFEKDKEINK FCQDKYGVTF PILHKIRCNG 
       110        120        130        140        150
QKQDPVYKFL KNSVSGKSGI KMIKWNFEKF VVDRNGKVVK RFSCMTRPLE 
       160 
LCPIIEELLN QPPEEQI
Length:167
Mass (Da):19,485
Last modified:June 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8C421FFF813391DD
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Z28026 Genomic DNA Translation: CAA81861.1
AY557895 Genomic DNA Translation: AAS56221.1
BK006944 Genomic DNA Translation: DAA09128.1

Protein sequence database of the Protein Information Resource

More...PIRi		S37843

NCBI Reference Sequences

More...RefSeqi		NP_012899.3, NM_001179592.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YKL026C_mRNA; YKL026C; YKL026C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		853842

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YKL026C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28026 Genomic DNA Translation: CAA81861.1
AY557895 Genomic DNA Translation: AAS56221.1
BK006944 Genomic DNA Translation: DAA09128.1
PIRiS37843
RefSeqiNP_012899.3, NM_001179592.3

3D structure databases

SMRiP36014
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi34105, 31 interactors
DIPiDIP-5437N
IntActiP36014, 1 interactor
MINTiP36014
STRINGi4932.YKL026C

Protein family/group databases

PeroxiBasei3740, SceGPx01

Proteomic databases

MaxQBiP36014
PaxDbiP36014
PRIDEiP36014

Genome annotation databases

EnsemblFungiiYKL026C_mRNA; YKL026C; YKL026C
GeneIDi853842
KEGGisce:YKL026C

Organism-specific databases

SGDiS000001509, GPX1
VEuPathDBiFungiDB:YKL026C

Phylogenomic databases

eggNOGiKOG1651, Eukaryota
GeneTreeiENSGT00940000165680
HOGENOMiCLU_029507_3_2_1
InParanoidiP36014
OMAiGKVVKFW

Miscellaneous databases

Protein Ontology

More...PROi		PR:P36014
RNActiP36014, protein

Family and domain databases

CDDicd00340, GSH_Peroxidase, 1 hit
Gene3Di3.40.30.10, 1 hit
InterProiView protein in InterPro
IPR000889, Glutathione_peroxidase
IPR029759, GPX_AS
IPR029760, GPX_CS
IPR036249, Thioredoxin-like_sf
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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGPX1_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P36014
Secondary accession number(s): D6VXQ8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 10, 2021
This is version 166 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again