AC   MF_00401;
DC   Protein; auto
TR   HAMAP; MF_00401; -; 1; level=0
XX
Names: Peroxiredoxin
XX
ID   TDXH
DE   RecName: Full=Peroxiredoxin;
DE            EC=1.11.1.24;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin;
case <FTGroup:1>
DE   + AltName: Full=Thioredoxin peroxidase;
end case
XX
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC   -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC       structure.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
case <FTGroup:1>
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. Although the primary
CC       sequence of this enzyme is similar to those of the 1-Cys Prx6 enzymes,
CC       its catalytic properties resemble those of the typical 2-Cys Prxs and
CC       C(R) is provided by the other dimeric subunit to form an intersubunit
CC       disulfide. The disulfide is subsequently reduced by thioredoxin.
else
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. In this 1-Cys
CC       peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC       with a cysteine from another protein or with a small thiol molecule.
end case
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
XX
DR   Pfam; PF00578; AhpC-TSA; 1; trigger=no
DR   Pfam; PF10417; 1-cysPrx_C; 1; trigger=no
DR   PIRSF; PIRSF000239; AHPC; 1; trigger=no
DR   PROSITE; PS51352; THIOREDOXIN_2; 1; trigger=yes
XX
KW   Antioxidant
KW   Cytoplasm
KW   Oxidoreductase
KW   Peroxidase
KW   Redox-active center
case <FTGroup:1>
KW   Disulfide bond
end case
XX
GO   GO:0005737; C:cytoplasm
GO   GO:0016209; F:antioxidant activity
GO   GO:0051920; F:peroxiredoxin activity
XX
FT   From: TDXH_AERPE (Q9Y9L0)
FT   ACT_SITE        50
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT   Condition: C
FT   BINDING         126
FT                   /ligand="substrate"
FT   Condition: R
FT   DISULFID        50
FT                   /note="Interchain (with #{Cys-213}); in linked form"
FT   Optional; Group: 1; Condition: C
FT   DISULFID        207..213
FT                   /note="Alternate"
FT   Condition: C-x*-C
FT   DISULFID        213
FT                   /note="Interchain (with #{Cys-50}); in linked form"
FT   Optional; Group: 1; Condition: C
XX
Size: 199-250;
Related: None;
Template: Q9Y9L0; O58966;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in SULME, THEAC, CALS4
Plasmid: None
Comments: None
XX
# Revision 1.30 2022/05/14
//