TPX_RALSO
ID TPX_RALSO Reviewed; 166 AA.
AC Q8XVP0;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Thiol peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Peroxiredoxin tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Prx {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00269};
GN Name=tpx {ECO:0000255|HAMAP-Rule:MF_00269}; OrderedLocusNames=RSc2790;
GN ORFNames=RS00057;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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. {ECO:0000255|HAMAP-Rule:MF_00269}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00269};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00269}.
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. {ECO:0000255|HAMAP-Rule:MF_00269}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00269}.
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DR EMBL; AL646052; CAD16497.1; -; Genomic_DNA.
DR RefSeq; WP_011002697.1; NC_003295.1.
DR AlphaFoldDB; Q8XVP0; -.
DR SMR; Q8XVP0; -.
DR STRING; 267608.RSc2790; -.
DR PRIDE; Q8XVP0; -.
DR EnsemblBacteria; CAD16497; CAD16497; RSc2790.
DR GeneID; 60502291; -.
DR KEGG; rso:RSc2790; -.
DR eggNOG; COG2077; Bacteria.
DR HOGENOM; CLU_042529_12_2_4; -.
DR OMA; ITQEPNY; -.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
DR CDD; cd03014; PRX_Atyp2cys; 1.
DR HAMAP; MF_00269; Tpx; 1.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR002065; TPX.
DR InterPro; IPR018219; Tpx_CS.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
DR PROSITE; PS01265; TPX; 1.
PE 3: Inferred from homology;
KW Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..166
FT /note="Thiol peroxidase"
FT /id="PRO_0000187893"
FT DOMAIN 18..166
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT ACT_SITE 60
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT DISULFID 60..94
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
SQ SEQUENCE 166 AA; 17283 MW; 6621B12E5F391F13 CRC64;
MANVTLGGNP IEVGGALPSV GAKAPAFTLV GKDLKDVSLA DFAGKRKVLN IVPSLDTPVC
ATSTRKFNEA VSKLENTVVF SISADLPFAA GRFCTTEGLD NVVPLSTFRD AGFKQAYGVD
IKTGPLAGLT ARAVVVLDAN DNVLHAQLVP EIKEEPNYDA ALAALK
