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42  structures 5798  species 0  interactions 12301  sequences 99  architectures

Family: GSHPx (PF00255)

Summary: Glutathione peroxidase

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Glutathione peroxidase". More...

Glutathione peroxidase Edit Wikipedia article

The enzyme glutathione peroxidase ( PDB 1GP1, EC 1.11.1.9) is found in the erythrocytes of mammals, and helps prevent peroxidation of cell membranes by consuming free peroxide in the cell. The summary reaction the enzyme catalizes is:

  • 2GSH + H2O2 → GSSG + 2H2O

Where GSh represents reduced monomeric glutathione, and GSSG represents oxidized glutathione. Glutathione reductase then reduces the oxidized glutathione to complete the cycle:

  • GSSG + NADPH + H+ → 2 GSH + NADP+

Glutathione peroxidase is a tetramer, and the bovine erythrocyte enzyme has a molecular weight of 84,000. It is a selenium containing enzyme with 4 selenocysteine amino acid residues that participate in the actual mechanism of this enzyme.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Glutathione peroxidase Provide feedback

No Pfam abstract.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000889

Glutathione peroxidase (GSHPx) ( EC ) is an enzyme that catalyses the reduction of hydroperoxides by glutathione [ PUBMED:7565867 ]. Its main function is to protect against the damaging effect of endogenously formed hydroperoxides. In higher vertebrates, several forms of GSHPx are known, including a ubiquitous cytosolic form (GSHPx-1), a gastrointestinal cytosolic form (GSHPx-GI), a plasma secreted form (GSHPx-P), and an epididymal secretory form (GSHPx-EP). In mammals there are eight GPx, divided in two clusters, the classical GPx (GPx1, GPx2, GPx3, GPx5 and GPx6) and phospholipid hydroperoxide GPx (GPx4, GPx7 and GPx8). The classical GPx is multimeric (commonly tetrameric) and soluble, while the phospholipid hydroperoxide (PHGPx) is monomeric and often membrane-associated [ PUBMED:23567855 ]. In addition to these characterised forms, the sequence of a protein of unknown function [ PUBMED:2771650 ] has been shown to be evolutionary related to those of GSHPx's.

In filarial nematode parasites, the major soluble cuticular protein (gp29) is a secreted GSHPx, which may provide a mechanism of resistance to the immune reaction of the mammalian host by neutralising the products of the oxidative burst of leukocytes [ PUBMED:1631065 ]. The structure of bovine seleno-glutathione peroxidase has been determined [ PUBMED:6852035 ]. The protein belongs to the alpha-beta class, with a three layer(aba) sandwich architecture. The catalytic site of GSHPx contains a conserved residue which is either a cysteine or, in many eukaryotic GSHPx, a selenocysteine [ PUBMED:2142875 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(10)
Full
(12301)
Representative proteomes UniProt
(43208)
RP15
(1797)
RP35
(5505)
RP55
(11327)
RP75
(18699)
Jalview View  View  View  View  View  View  View 
HTML View             
PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(10)
Full
(12301)
Representative proteomes UniProt
(43208)
RP15
(1797)
RP35
(5505)
RP55
(11327)
RP75
(18699)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(10)
Full
(12301)
Representative proteomes UniProt
(43208)
RP15
(1797)
RP35
(5505)
RP55
(11327)
RP75
(18699)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD
Number in seed: 10
Number in full: 12301
Average length of the domain: 103.4 aa
Average identity of full alignment: 42 %
Average coverage of the sequence by the domain: 54.94 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.0 27.0
Noise cut-off 26.9 26.9
Model length: 108
Family (HMM) version: 22
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GSHPx domain has been found. There are 42 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044TQ28 View 3D Structure Click here
A0A077ZJY1 View 3D Structure Click here
A0A0D2DV52 View 3D Structure Click here
A0A0G2KAD1 View 3D Structure Click here
A0A0H3GRA3 View 3D Structure Click here
A0A0H3GRS6 View 3D Structure Click here
A0A0K0DWI3 View 3D Structure Click here
A0A0K0DZK0 View 3D Structure Click here
A0A0N4U0Z4 View 3D Structure Click here
A0A0N4UD18 View 3D Structure Click here
A0A0P0WGL5 View 3D Structure Click here
A0A0R0GIC5 View 3D Structure Click here
A0A175W2T3 View 3D Structure Click here
A0A1C1C755 View 3D Structure Click here
A0A1D6K2D3 View 3D Structure Click here
A0A1D6K2F9 View 3D Structure Click here
A0A1D8PPH4 View 3D Structure Click here
A0A2K6VSX2 View 3D Structure Click here
A0A2R8RWH8 View 3D Structure Click here
A0A3P7E6R5 View 3D Structure Click here
A0A3P7E861 View 3D Structure Click here
A0A3Q0KGE8 View 3D Structure Click here
A0A5K4FAT9 View 3D Structure Click here
A0A5K4FEI9 View 3D Structure Click here
A0A5S6PF49 View 3D Structure Click here
A0A5S6PF50 View 3D Structure Click here
A0A5S6PGT5 View 3D Structure Click here
A0A5S6PPQ9 View 3D Structure Click here
A4I211 View 3D Structure Click here
A4I212 View 3D Structure Click here
A4ID89 View 3D Structure Click here
A6QLY2 View 3D Structure Click here
A8WFK6 View 3D Structure Click here
B4FRF0 View 3D Structure Click here
B6T5N2 View 3D Structure Click here
B7FAE9 View 3D Structure Click here
C0NI23 View 3D Structure Click here
C0P3R8 View 3D Structure Click here
C1H0Y0 View 3D Structure Click here
C6SZX7 View 3D Structure Click here