HAMAP rule MF_00401
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00401 |
| Accession | MF_00401 |
| Dates | 28-FEB-2005 (Created)
03-SEP-2024 (Last updated, Version 25) |
| Name | Peroxiredoxin |
| Scope(s) |
Bacteria Archaea |
| Template(s) | Q9Y9L0; O58966; [ Recover all ] |
| Triggered by |
HAMAP; MF_00401 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | TDXH |
| Protein name | RecName: Full=Peroxiredoxin; EC=1.11.1.24; AltName: Full=Thioredoxin-dependent peroxiredoxin; |
| case <FTGroup:1> | |
| Protein name | + AltName: Full=Thioredoxin peroxidase; |
| end case | |
Comments
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| FUNCTION | 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. |
| CATALYTIC ACTIVITY | Reaction=a hydroperoxide + [thioredoxin]-dithiol = an alcohol + [thioredoxin]-disulfide + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA- COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; |
| SUBUNIT | Homodecamer. Pentamer of dimers that assemble into a ring structure. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| case <FTGroup:1> | |
| 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. Although the primary sequence of this enzyme is similar to those of the 1-Cys Prx6 enzymes, its catalytic properties resemble those of the typical 2-Cys Prxs and C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin. |
| else | |
| 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 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule. |
| end case | |
| SIMILARITY | Belongs to the peroxiredoxin family. Prx6 subfamily. |
Keywords
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| Antioxidant | |
| Cytoplasm | |
| Oxidoreductase | |
| Peroxidase | |
| Redox-active center | |
| case <FTGroup:1> | |
| Disulfide bond | |
| end case | |
Gene Ontology
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| GO:0005737; Cellular component:cytoplasm |
| GO:0016209; Molecular function:antioxidant activity |
| GO:0051920; Molecular function:peroxiredoxin activity |
Cross-references
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| Pfam | PF00578; AhpC-TSA; 1; |
| Pfam | PF10417; 1-cysPrx_C; 1; |
| PIRSF | PIRSF000239; AHPC; 1; |
| PROSITE | PS51352; THIOREDOXIN_2; 1; |
Features
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| From: TDXH_AERPE (Q9Y9L0) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 50 | 50 | /note="Cysteine sulfenic acid (-SOH) intermediate" | C | ||||||||
| BINDING | 126 | 126 | /ligand="substrate" | R | ||||||||
| DISULFID | 50 | 50 | /note="Interchain (with #{Cys-213}); in linked form" | C | 1 | |||||||
| DISULFID | 207 | 213 | /note="Alternate" | C-x*-C | ||||||||
| DISULFID | 213 | 213 | /note="Interchain (with #{Cys-50}); in linked form" | C | 1 | |||||||
Additional information
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| Size range | 199-250 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |