ID   TDX1_BRUMA              Reviewed;         229 AA.
AC   P48822;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Peroxiredoxin 1;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:Q06830};
DE   AltName: Full=Thiol-specific antioxidant protein 1;
DE   AltName: Full=Thioredoxin peroxidase 1;
DE            Short=Bm-TPx-1;
DE   AltName: Full=Thioredoxin-dependent peroxide reductase 1;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin 1 {ECO:0000305};
GN   Name=TSA1;
OS   Brugia malayi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9566515; DOI=10.1016/s0166-6851(97)00213-2;
RA   Ghosh I., Eisinger S.W., Raghavan N., Scott A.L.;
RT   "Thioredoxin peroxidases from Brugia malayi.";
RL   Mol. Biochem. Parasitol. 91:207-220(1998).
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; U34251; AAC23701.1; -; mRNA.
DR   AlphaFoldDB; P48822; -.
DR   SMR; P48822; -.
DR   STRING; 6279.P48822; -.
DR   Proteomes; UP000006672; Unassembled WGS sequence.
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; Reference proteome.
FT   CHAIN           1..229
FT                   /note="Peroxiredoxin 1"
FT                   /id="PRO_0000135089"
FT   DOMAIN          33..192
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        78
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
FT   DISULFID        78
FT                   /note="Interchain (with C-200); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
FT   DISULFID        200
FT                   /note="Interchain (with C-78); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:Q06830"
SQ   SEQUENCE   229 AA;  25367 MW;  B386EB6C52619497 CRC64;
     MIRSVLASVS PLRQILASQL CTSSITLAGI RPLGPKNKAP DFSGTAVVNG DFKTISMKDY
     KGKWLILFFY PLDFTFVCPT EITAFSDRCA EFQKLNTELI ACSCDSHFSH LAWIQTPRSE
     VGGLGDMKIP VLADFNKDIA NAFGVLDHET GISYRGLFLI DPSGEIRHSL VNDLSVGRSV
     DEAFRTLKAF QFVEKHGEVC PANWSDDKPT IKPGIKESKE YFKKVDGHT