TDX_FASHE
ID TDX_FASHE Reviewed; 194 AA.
AC P91883;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Thioredoxin peroxidase;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q06830};
DE AltName: Full=Peroxiredoxin;
DE AltName: Full=Thiol-specific antioxidant protein;
DE AltName: Full=Thioredoxin-dependent peroxide reductase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
OS Fasciola hepatica (Liver fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC Fasciola.
OX NCBI_TaxID=6192;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9226957; DOI=10.1017/s0031182097001170;
RA McGonigle S., Curley G.P., Dalton J.P.;
RT "Cloning of peroxiredoxin, a novel antioxidant enzyme, from the helminth
RT parasite Fasciola hepatica.";
RL Parasitology 115:101-104(1997).
CC -!- FUNCTION: Antioxidant. Could be involved in protection against reactive
CC oxygen species (ROS) generated by metabolic processes and/or protection
CC of the parasite against ROS released by immune effector cells.
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:0000250|UniProtKB:Q06830}.
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 -!- 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; U88577; AAB71727.1; -; mRNA.
DR AlphaFoldDB; P91883; -.
DR SMR; P91883; -.
DR BRENDA; 1.11.1.24; 2230.
DR SABIO-RK; P91883; -.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
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..194
FT /note="Thioredoxin peroxidase"
FT /id="PRO_0000135092"
FT DOMAIN 2..160
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 47
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 47
FT /note="Interchain (with C-168); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 168
FT /note="Interchain (with C-47); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
SQ SEQUENCE 194 AA; 21661 MW; 57F57D93C638A43D CRC64;
MLQPNMPAPN FSGQAVVGKE FETISLSDYK GKWVILAFYP LDFTFVCPTE IIAISDQMEQ
FAQRNCAVIF CSTDSVYSHL QWTKMDRKVG GIGQLNFPLL ADKNMSVSRA FGVLDEEQGN
TYRGNFLIDP KGVLRQITVN DDPVGRSVEE ALRLLDAFIF HEEHGEVCPA NWKPKSKTIV
PTPDGSKAYF SSAN
