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Annotation rule MF_00401
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General rule information [?]

Accession MF_00401
Dates 1-JUN-2001 (Created)
2-APR-2020 (Last updated, Version 29)
Name Peroxiredoxin
Scope
Bacteria
Archaea
Templates Q9Y9L0 (TDXH_AERPE); O58966 (TDXH_PYRHO): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
TDXH
Protein name
RecName: Full=Peroxiredoxin;
EC 1.11.1.24;
AltName: Full=Thioredoxin-dependent peroxiredoxin;
case <FTGroup:1>
Protein name
Full=Thioredoxin peroxidase;
end case

Comments [?]

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 [?]

case <FTGroup:1>
end case

Gene Ontology [?]

GO:0005737; Cellular component: cytoplasm.
GO:0016209; Molecular function: antioxidant activity.
GO:0051920; Molecular function: peroxiredoxin activity.

Cross-references [?]

Pfam PF00578; AhpC-TSA; 1;
PF10417; 1-cysPrx_C; 1;
PIRSF PIRSF000239; AHPC; 1;
PROSITE PS51352; THIOREDOXIN_2; 1; trigger=PRU00691;

Features [?]

From: TDXH_AERPE (Q9Y9L0)
Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     50     50       Cysteine sulfenic acid (-SOH) intermediate     C  
BINDING     126     126       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 [?]

Size range 199-250 amino acids
Related rules None
Fusion None