ID   PRXU_PEPAC              Reviewed;         203 AA.
AC   Q9L3Q5;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   29-SEP-2021, entry version 78.
DE   RecName: Full=Selenocysteine-containing peroxiredoxin PrxU;
DE            EC=1.11.1.24 {ECO:0000269|PubMed:11501765};
DE   AltName: Full=Selenoperoxiredoxin PrxU;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin PrxU {ECO:0000305};
GN   Name=prxU {ECO:0000303|PubMed:11501765};
OS   Peptoclostridium acidaminophilum (Eubacterium acidaminophilum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, AND
RP   SELENOCYSTEINE AT SEC-47.
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX   PubMed=11501765; DOI=10.1515/bc.2001.123;
RA   Sohling B., Parther T., Rucknagel K.P., Wagner M.A., Andreesen J.R.;
RT   "A selenocysteine-containing peroxiredoxin from the strictly anaerobic
RT   organism Eubacterium acidaminophilum.";
RL   Biol. Chem. 382:979-986(2001).
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:P0A251}.
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:0000269|PubMed:11501765};
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ271724; CAB71140.1; -; Genomic_DNA.
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   1: Evidence at protein level;
KW   Antioxidant; Direct protein sequencing; Oxidoreductase; Peroxidase;
KW   Redox-active center; Selenocysteine.
FT   CHAIN           1..203
FT                   /note="Selenocysteine-containing peroxiredoxin PrxU"
FT                   /id="PRO_0000391436"
FT   DOMAIN          2..160
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000250|UniProtKB:P0A251"
FT   NON_STD         47
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000269|PubMed:11501765"
FT   CONFLICT        24
FT                   /note="F -> P (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  22467 MW;  9896859F556E79CC CRC64;
     MVSVGKKAPD FEMAGFYKGE FKTFRLSEYL GKWVVLCFYP GDFTFVUATE VSAVAEKYPE
     FQKLGVEVLS VSVDSVFVHK MWNDNELSKM VEGGIPFPML SDGGGNVGTL YGVYDPEAGV
     ENRGRFLIDP DGIIQGYEVL ILPVGRNVSE TLRQIQAFQL VRETKGAEVA PSGWKPGKKT
     LKPGPGLVGN VYKEWSVKEA FED