UniProt functional annotation for P9WIE3



	UniProt functional annotation for P9WIE3

UniProt code: P9WIE3.

Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).

Taxonomy: Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.

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. May represent an important antioxidant defense against cytotoxic peroxides, especially peroxynitrite, which can be formed by activated macrophages during infection. {ECO:0000269|PubMed:19737009, ECO:0000269|PubMed:24379404}.

Catalytic activity: Reaction=[mycoredoxin]-L-dithiol + a hydroperoxide = [mycoredoxin]-L- disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62640, Rhea:RHEA- COMP:16137, Rhea:RHEA-COMP:16138, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.29; Evidence={ECO:0000269|PubMed:19737009};

Subunit: Homodimer (PubMed:19737009, PubMed:27417938). Forms both dimers and octamers; a tightly-associated dimer and a ring-like octamer (PubMed:15701515). {ECO:0000269|PubMed:15701515, ECO:0000269|PubMed:19737009, ECO:0000269|PubMed:27417938}.

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. C(P) can be reduced through a mixed disulfide with the N-terminal cysteine of mycoredoxin-1 (Mrx1), resolved by its C-terminal cysteine, or by a mixed disulfide with mycothiol, resolved by a second molecule of mycothiol or by mycoredoxin-1. {ECO:0000305|PubMed:24379404, ECO:0000305|PubMed:27417938}.

Similarity: Belongs to the peroxiredoxin family. AhpE subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Taxonomy:		Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.



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. May represent an important antioxidant defense against cytotoxic peroxides, especially peroxynitrite, which can be formed by activated macrophages during infection. {ECO:0000269\|PubMed:19737009, ECO:0000269\|PubMed:24379404}.


Catalytic activity:		Reaction=[mycoredoxin]-L-dithiol + a hydroperoxide = [mycoredoxin]-L- disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62640, Rhea:RHEA- COMP:16137, Rhea:RHEA-COMP:16138, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.29; Evidence={ECO:0000269\|PubMed:19737009};
Subunit:		Homodimer (PubMed:19737009, PubMed:27417938). Forms both dimers and octamers; a tightly-associated dimer and a ring-like octamer (PubMed:15701515). {ECO:0000269\|PubMed:15701515, ECO:0000269\|PubMed:19737009, ECO:0000269\|PubMed:27417938}.
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. C(P) can be reduced through a mixed disulfide with the N-terminal cysteine of mycoredoxin-1 (Mrx1), resolved by its C-terminal cysteine, or by a mixed disulfide with mycothiol, resolved by a second molecule of mycothiol or by mycoredoxin-1. {ECO:0000305\|PubMed:24379404, ECO:0000305\|PubMed:27417938}.
Similarity:		Belongs to the peroxiredoxin family. AhpE subfamily. {ECO:0000305}.