AC   MF_00269;
DC   Protein; auto
TR   HAMAP; MF_00269; -; 1; level=0
XX
Names: Tpx
XX
ID   TPX
DE   RecName: Full=Thiol peroxidase;
DE            Short=Tpx;
DE            EC=1.11.1.24;
DE   AltName: Full=Peroxiredoxin tpx;
DE            Short=Prx;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin;
GN   Name=tpx;
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: Homodimer.
case <FTTag:disulf>
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 atypical 2-Cys
CC       peroxiredoxin, C(R) is present in the same subunit to form an
CC       intramolecular disulfide. The disulfide is subsequently reduced by
CC       thioredoxin.
end case
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
XX
DR   Pfam; PF08534; Redoxin; 1; trigger=no
DR   PROSITE; PS01265; TPX; 1; trigger=no
DR   PROSITE; PS51352; THIOREDOXIN_2; 1; trigger=no
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KW   Antioxidant
KW   Oxidoreductase
KW   Peroxidase
KW   Redox-active center
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
GO   GO:0016209; F:antioxidant activity
GO   GO:0008379; F:thioredoxin peroxidase activity
XX
FT   From: TPX_ECOLI (P0A862)
FT   DOMAIN          19..168
FT                   /note="Thioredoxin"
FT   ACT_SITE        61
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT   Condition: C
FT   DISULFID        61..95
FT                   /note="Redox-active"
FT   Tag: disulf; Condition: C-x*-C
XX
Size: 161-175;
Related: None;
Template: P0A862;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.22 2020/04/03
//