ID TDX_ECHGR Reviewed; 193 AA.
AC Q8T6C4; O96380;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Thioredoxin peroxidase;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q06830};
DE AltName: Full=Peroxiredoxin;
DE AltName: Full=TPx-Eg;
DE AltName: Full=Thioredoxin-dependent peroxide reductase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
GN Name=TPX;
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li J., Zhang W.-B., Zhang L.-H., McManus D.P.;
RT "Serological studies on a full length cDNA clone of thioredoxin peroxidase
RT from Echinococcus granulosus.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-193.
RA Salinas G., Fernandez V., Fernandez C., Selkirk M.E.;
RL Submitted (NOV-1997) 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 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; AF478688; AAL84833.1; -; mRNA.
DR EMBL; AF034959; AAD02002.1; -; mRNA.
DR AlphaFoldDB; Q8T6C4; -.
DR SMR; Q8T6C4; -.
DR EnsemblMetazoa; XM_024489458.1; XP_024356136.1; GeneID_36335924.
DR WBParaSite; EgrG_000791700; EgrG_000791700; EgrG_000791700.
DR OMA; FWYPKDF; -.
DR OrthoDB; 47465at2759; -.
DR BRENDA; 1.11.1.24; 2032.
DR Proteomes; UP000492820; Unassembled WGS sequence.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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 PANTHER; PTHR10681:SF171; AT16346P-RELATED; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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..193
FT /note="Thioredoxin peroxidase"
FT /id="PRO_0000135091"
FT DOMAIN 3..161
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 48
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 48
FT /note="Interchain (with C-169); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 169
FT /note="Interchain (with C-48); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
SQ SEQUENCE 193 AA; 21406 MW; B60C58799BDFCE20 CRC64;
MAAVVGKLAP SFTCKALVDG ELKDVSLSDY RGKYVILFFY PMDFTFVCPT EIIAFNDRAD
EFHQRGCQLL ACSTDSGYCH LAWNNVSRKE GGVQGMRIPM LADTNHKISR DYGVLIEDQG
IALRGLFIID DKGVLRQITI NDLPVGRSVD EALRLLDAFQ FTDKHGEVCP ANWQPGSKTF
KPSAGDLKSF MSS
//
