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HAMAP rule MF_00401

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General rule information [?]

Accession MF_00401
Dates 1-JUN-2001 (Created)
14-MAY-2022 (Last updated, Version 30)
Name Peroxiredoxin
Scope(s) Bacteria
Archaea
Template(s) Q9Y9L0 (TDXH_AERPE); O58966 (TDXH_PYRHO); [ Recover all ]
Triggered by HAMAP; MF_00401 (Get profile general information and statistics)

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 + AltName: Full=Thioredoxin peroxidase;
end case

Comments [?]

FUNCTIONThiol-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=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]- disulfide + an alcohol + 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;
SUBUNITHomodecamer. Pentamer of dimers that assemble into a ring structure.
SUBCELLULAR LOCATIONCytoplasm.
case <FTGroup:1>
MISCELLANEOUSThe 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
MISCELLANEOUSThe 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
SIMILARITYBelongs to the peroxiredoxin family. Prx6 subfamily.

Keywords [?]

Antioxidant
Cytoplasm
Oxidoreductase
Peroxidase
Redox-active center
case <FTGroup:1>
Disulfide bond
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;
Pfam PF10417; 1-cysPrx_C; 1;
PIRSF PIRSF000239; AHPC; 1;
PROSITE PS51352; THIOREDOXIN_2; 1;

Features [?]

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 [?]

Size range 199-250 amino acids
Related rules None
Fusion Nter: None Cter: None



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