ID   1CPX_ONCVO              Reviewed;         232 AA.
AC   P52570;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=1-Cys peroxiredoxin;
DE            EC=1.11.1.- {ECO:0000250|UniProtKB:O17433};
DE   AltName: Full=Thiol-specific antioxidant;
DE   AltName: Full=Thioredoxin peroxidase;
GN   Name=TSA;
OS   Onchocerca volvulus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=6282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chandrashekar R., Curits K.C., Weil G.J.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 62-222.
RA   Chandrashekar R., Curtis K., Weil G.J.;
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:O17433}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an
CC         alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC         Evidence={ECO:0000250|UniProtKB:O17433};
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.
CC       {ECO:0000250|UniProtKB:P34227}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U31052; AAC27392.1; -; mRNA.
DR   EMBL; U09385; AAA50214.2; -; mRNA.
DR   AlphaFoldDB; P52570; -.
DR   SMR; P52570; -.
DR   STRING; 6282.P52570; -.
DR   PeroxiBase; 4943; Ovo1CysPrx.
DR   HOGENOM; CLU_042529_4_1_1; -.
DR   Proteomes; UP000024404; Unassembled WGS sequence.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR   CDD; cd03016; PRX_1cys; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR045020; PRX_1cys.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant; Oxidoreductase; Peroxidase; Redox-active center;
KW   Reference proteome.
FT   CHAIN           1..232
FT                   /note="1-Cys peroxiredoxin"
FT                   /id="PRO_0000135105"
FT   DOMAIN          5..176
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        49
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        49
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P30041"
SQ   SEQUENCE   232 AA;  25926 MW;  029E93F276232B37 CRC64;
     MCAPSGPGNK FPDFQAETNE GFISSFYDWI GKDSWAILFS HPRDFTPVCT TELARLVQLA
     PEFKKRNVKL IGLSCDSADS HSKWADDILA LYKMKCVGCD SEKKLPYPII ADEDRSLATE
     LGMMDPDERD EKGNTLTARC VFIIGSDKTL KLSILYPATT GRNFDEILRV VDSLQLTAVK
     LVATPVDWKD GDDCVVLPTI DDNEAKKLFG EKIHTIDLPS GKHYLRMVPH PK