ID   TPX_PASMU               Reviewed;         165 AA.
AC   P57880;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   25-MAY-2022, entry version 122.
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=PM0820;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02904.1; -; Genomic_DNA.
DR   RefSeq; WP_010906866.1; NC_002663.1.
DR   AlphaFoldDB; P57880; -.
DR   SMR; P57880; -.
DR   STRING; 747.DR93_1660; -.
DR   EnsemblBacteria; AAK02904; AAK02904; PM0820.
DR   KEGG; pmu:PM0820; -.
DR   PATRIC; fig|272843.6.peg.829; -.
DR   HOGENOM; CLU_042529_12_2_6; -.
DR   OMA; ITQEPNY; -.
DR   Proteomes; UP000000809; 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..165
FT                   /note="Thiol peroxidase"
FT                   /id="PRO_0000187891"
FT   DOMAIN          18..165
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   165 AA;  17706 MW;  21A6EEBA9B9A11C7 CRC64;
     MSKITLAGTE IEVSGVFPQV GDVVTDFTTV SAKLEDTTLA NFAGKRKILN IFPSIDTGIC
     ATSVRKFNEQ AAKLANTAVL CLSTDLPFAQ ARFCGAEGLE NVFTVSTFRN KDVHKQLGVD
     IVEGPLAGLT ARAVIVLDEN NRVLHSELVP EIKQEPNYDA ALAVL