ID   AHPC_ACICA              Reviewed;          25 AA.
AC   P82954;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 49.
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;
GN   Name=ahpC;
OS   Acinetobacter calcoaceticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND INDUCTION.
RC   STRAIN=69-V;
RX   PubMed=11425483; DOI=10.1111/j.1574-6968.2001.tb10723.x;
RA   Benndorf D., Loffhagen N., Babel W.;
RT   "Protein synthesis patterns in Acinetobacter calcoaceticus induced by
RT   phenol and catechol show specificities of responses to chemostress.";
RL   FEMS Microbiol. Lett. 200:247-252(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=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   -!- INDUCTION: By oxidative stress, primary alcohols, monocyclic aromatics
CC       and heat shock. {ECO:0000269|PubMed:11425483}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P82954; -.
DR   SMR; P82954; -.
DR   STRING; 471.BUM88_05750; -.
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.
PE   1: Evidence at protein level;
KW   Antioxidant; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   Oxidoreductase; Peroxidase; Redox-active center; Stress response.
FT   CHAIN           1..>25
FT                   /note="Alkyl hydroperoxide reductase C"
FT                   /id="PRO_0000135112"
FT   NON_TER         25
FT                   /evidence="ECO:0000303|PubMed:11425483"
SQ   SEQUENCE   25 AA;  2836 MW;  7B3112366157F2D8 CRC64;
     SLINTEVKPF QATAYHNGQF VEVNE