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Annotation rule MF_00269 |
Accession | MF_00269 |
Dates | 1-JUN-2001 (Created) 3-APR-2020 (Last updated, Version 22) |
Name | Tpx |
Scope | Bacteria |
Template | P0A862 (TPX_ECOLI) |
Triggered by |
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Protein name |
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Gene name |
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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 | Homodimer. |
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. The disulfide is subsequently reduced by thioredoxin. |
Similarity | Belongs to the peroxiredoxin family. Tpx subfamily. |
From: TPX_ECOLI (P0A862) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DOMAIN | 19 | 168 | Thioredoxin | |||||||||
ACT_SITE | 61 | 61 | Cysteine sulfenic acid (-SOH) intermediate | C | ||||||||
DISULFID | 61 | 95 | Redox-active | disulf | C-x*-C |
Size range | 161-175 amino acids |
Related rules | None |
Fusion | None |