ID   PRDX_ASCSU              Reviewed;         195 AA.
AC   Q9NL98;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Peroxiredoxin;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:Q06830};
DE   AltName: Full=AsPrx;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000312|EMBL:BAA90476.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=10704594; DOI=10.1016/s0020-7519(99)00180-0;
RA   Tsuji N., Kasuga-Aoki H., Isobe T., Yoshihara S.;
RT   "Cloning and characterisation of a peroxiredoxin from the swine roundworm
RT   Ascaris suum.";
RL   Int. J. Parasitol. 30:125-128(2000).
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 and as sensor of hydrogen peroxide-mediated
CC       signaling events. {ECO:0000269|PubMed:10704594}.
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         Evidence={ECO:0000250|UniProtKB:Q06830};
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC       {ECO:0000250|UniProtKB:Q06830}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in eggs, larvae, and in male and female
CC       adult worms. {ECO:0000269|PubMed:10704594}.
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 typical 2-Cys
CC       peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC       intersubunit disulfide. The disulfide is subsequently reduced by
CC       thioredoxin. {ECO:0000250|UniProtKB:Q06830}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB022045; BAA90476.1; -; mRNA.
DR   AlphaFoldDB; Q9NL98; -.
DR   SMR; Q9NL98; -.
DR   BRENDA; 1.11.1.24; 474.
DR   GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
DR   GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
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; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           1..195
FT                   /note="Peroxiredoxin"
FT                   /id="PRO_0000135084"
FT   DOMAIN          4..162
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        49
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
FT   DISULFID        49
FT                   /note="Interchain (with C-170); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
FT   DISULFID        170
FT                   /note="Interchain (with C-49); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
SQ   SEQUENCE   195 AA;  21590 MW;  923DDDB98A53E058 CRC64;
     MSKAMIGKPA PEFTATAVVD GDFKSISLSD YKGKYVVLFF YPMDFTFVCP TEIIAFSEHV
     GEFKKLGVEV LAASTDSQFS HLAWINTPRK QGGLGEMKIP IISDNNHQIS RDYGVLKEDD
     GIAYRGLFII DPKGILRQIT VNDLPVGRSV TETLRLVQAF QFVDKHGEVC PAGWTPGADT
     IKPGVKESKA YFEKH