ID   AHPC_FERAY              Reviewed;         168 AA.
AC   P26830;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Alkyl hydroperoxide reductase C;
DE            EC=1.11.1.26 {ECO:0000250|UniProtKB:P0A251};
DE   AltName: Full=Peroxiredoxin;
DE   AltName: Full=Thioredoxin peroxidase;
DE   Flags: Fragment;
OS   Ferdinandcohnia aciditolerans (strain JCM 32973 / CCTCC AB 2017280 / YN-1)
OS   (Bacillus aciditolerans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Fredinandcohnia.
OX   NCBI_TaxID=72581;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1917890; DOI=10.1093/oxfordjournals.jbchem.a123440;
RA   Xu X., Koyama N., Cui M., Yamagishi A., Nosoh Y., Oshima T.;
RT   "Nucleotide sequence of the gene encoding NADH dehydrogenase from an
RT   alkalophile, Bacillus sp. strain YN-1.";
RL   J. Biochem. 109:678-683(1991).
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=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC         Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.11.1.26;
CC         Evidence={ECO:0000250|UniProtKB:P0A251};
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC       assemble to form a ring-like decamer. {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. The disulfide is subsequently reduced by AhpF.
CC       {ECO:0000250|UniProtKB:P0A251}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; D10701; BAA01544.1; -; Genomic_DNA.
DR   AlphaFoldDB; P26830; -.
DR   SMR; P26830; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0102039; F:alkylhydroperoxide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR017559; AhpC.
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:SF121; PTHR10681:SF121; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR03137; AhpC; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Cytoplasm; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           <1..168
FT                   /note="Alkyl hydroperoxide reductase C"
FT                   /id="PRO_0000135132"
FT   DOMAIN          <1..138
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        28
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A251"
FT   DISULFID        28
FT                   /note="Interchain (with C-147); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P0A251"
FT   DISULFID        147
FT                   /note="Interchain (with C-28); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P0A251"
FT   NON_TER         1
SQ   SEQUENCE   168 AA;  18480 MW;  2D58C57BB7726CDE CRC64;
     EFIEVSEESF KGQWSVLCFY PADFTFVCPT ELEDLQNEYA ALKELGVEVF SASTDTHFTH
     KGWHDSSETI GKITYAMIGD PSQTLSRNFD VLNEVSGLAD RGTFIIDPDG VVQAAEINAE
     GIGRDASTLV NKIKAAQYVR NNPGEVCPAK WQEGDETLKP SLDLVGKI