ID   TPX_CHLTE               Reviewed;         168 AA.
AC   Q8KED5;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=CT0754;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(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; AE006470; AAM71991.1; -; Genomic_DNA.
DR   RefSeq; NP_661649.1; NC_002932.3.
DR   AlphaFoldDB; Q8KED5; -.
DR   SMR; Q8KED5; -.
DR   STRING; 194439.CT0754; -.
DR   EnsemblBacteria; AAM71991; AAM71991; CT0754.
DR   KEGG; cte:CT0754; -.
DR   PATRIC; fig|194439.7.peg.686; -.
DR   eggNOG; COG2077; Bacteria.
DR   HOGENOM; CLU_042529_12_2_10; -.
DR   OMA; ITQEPNY; -.
DR   OrthoDB; 1738458at2; -.
DR   Proteomes; UP000001007; 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..168
FT                   /note="Thiol peroxidase"
FT                   /id="PRO_0000187872"
FT   DOMAIN          20..168
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT   ACT_SITE        62
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT   DISULFID        62..96
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
SQ   SEQUENCE   168 AA;  17714 MW;  4FB46D04B5028073 CRC64;
     MIMATITLKG NSIHTAGELP AVGSQLPAFT LVKSDLSEVS PADFAGKKLV LNIFPSLDTA
     VCAASVRRFN KEAGERGDAV VLCISADLPF AQGRFCTTEG LDNVVPLSVY RSPEFGLDYG
     LTITDGPLKG LLSRAVIVTD ASGKVLYAEQ VPEIVQEPDY DKALAALA