ID   R20K_CLOPA              Reviewed;         178 AA.
AC   P23161;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Putative peroxiredoxin in rubredoxin operon;
DE            EC=1.11.1.-;
DE   AltName: Full=ORF C;
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
RX   PubMed=1637309; DOI=10.1042/bj2850255;
RA   Mathieu I., Meyer J., Moulis J.-M.;
RT   "Cloning, sequencing and expression in Escherichia coli of the rubredoxin
RT   gene from Clostridium pasteurianum.";
RL   Biochem. J. 285:255-262(1992).
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=[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an
CC         alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC       {ECO:0000250|UniProtKB:P0A251}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}.
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. {ECO:0000250|UniProtKB:P0A251}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M60116; AAA23278.1; -; Genomic_DNA.
DR   PIR; S29119; S29119.
DR   RefSeq; WP_003447686.1; NZ_LFYL01000002.1.
DR   AlphaFoldDB; P23161; -.
DR   SMR; P23161; -.
DR   PRIDE; P23161; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:RHEA.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; Oxidoreductase; Peroxidase; Redox-active center.
FT   CHAIN           1..178
FT                   /note="Putative peroxiredoxin in rubredoxin operon"
FT                   /id="PRO_0000135131"
FT   DOMAIN          3..163
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        50
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A251"
FT   DISULFID        50
FT                   /note="Interchain (with C-167); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P0A251"
FT   DISULFID        167
FT                   /note="Interchain (with C-50); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P0A251"
SQ   SEQUENCE   178 AA;  20036 MW;  DF9AD3D8F1B93A64 CRC64;
     MERLVGKPAP EFEMKAVKGD GRGFTEVKLG DYKGKWLVMF FYPLDFTFVC PTEITGFSKR
     AEEFRDLKAE LLAVSCDSQY SHETWINQDI KQGGLGKINF PIASDKTTEV STKYGIQIEE
     EGISLRGLFI IDPEGIVRYS VVHDLNVGRS VDETLRVLKA FQTGGMCALD WHEGDDNL