HAMAP rule MF_00401
General rule information
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| Accession | MF_00401 |
| Dates | 1-JUN-2001 (Created) 14-MAY-2022 (Last updated, Version 30) |
| Name | Peroxiredoxin |
| Scope | Bacteria
Archaea |
| Templates | Q9Y9L0 (TDXH_AERPE); O58966 (TDXH_PYRHO): [Recover all] |
| Triggered by |
Propagated annotation
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Identifier, protein and gene names
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| Identifier |
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| Protein name |
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case <FTGroup:1>
| Protein name |
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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 | RHEA:62620: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O
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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case <FTGroup:1>
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.
GO:0016209; Molecular function: antioxidant activity.
GO:0051920; Molecular function: peroxiredoxin activity.
Cross-references
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| Pfam | PF00578; AhpC-TSA; 1; |
| PF10417; 1-cysPrx_C; 1; | |
| PIRSF | PIRSF000239; AHPC; 1; |
| PROSITE | PS51352; THIOREDOXIN_2; 1; trigger=PRU00691; |
Features
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| From: TDXH_AERPE (Q9Y9L0) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 50 | 50 | Cysteine sulfenic acid (-SOH) intermediate | C | ||||||||
| BINDING | 126 | 126 | /ligand="substrate | R | ||||||||
| DISULFID (Optional) | 50 | 50 | Interchain (with #{Cys-213}); in linked form | C | 1 | |||||||
| DISULFID | 207 | 213 | Alternate | C-x*-C | ||||||||
| DISULFID (Optional) | 213 | 213 | 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 | None |