ID   AHPE_MYCBO              Reviewed;         153 AA.
AC   P65689; A0A1R3Y0L1; Q10520; X2BK87;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Alkyl hydroperoxide reductase E;
DE            EC=1.11.1.29 {ECO:0000250|UniProtKB:P9WIE3};
DE   AltName: Full=Mycoredoxin-dependent peroxiredoxin {ECO:0000305};
DE   AltName: Full=Peroxiredoxin AhpE;
DE            Short=Prx;
DE   AltName: Full=Thioredoxin peroxidase;
DE            Short=TPx;
GN   Name=ahpE; OrderedLocusNames=BQ2027_MB2262C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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. May represent an important antioxidant
CC       defense against cytotoxic peroxides, especially peroxynitrite, which
CC       can be formed by activated macrophages during infection.
CC       {ECO:0000250|UniProtKB:P9WIE3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[mycoredoxin]-L-dithiol + a hydroperoxide = [mycoredoxin]-L-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62640, Rhea:RHEA-
CC         COMP:16137, Rhea:RHEA-COMP:16138, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.29;
CC         Evidence={ECO:0000250|UniProtKB:P9WIE3};
CC   -!- SUBUNIT: Homodimer. Forms both dimers and octamers; a tightly-
CC       associated dimer and a ring-like octamer.
CC       {ECO:0000250|UniProtKB:P9WIE3}.
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 1-Cys
CC       peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC       with a cysteine from another protein or with a small thiol molecule.
CC       C(P) can be reactivated through a mixed disulfide with the N-terminal
CC       cysteine of mycoredoxin-1 (Mrx1), resolved by its C-terminal cysteine,
CC       or by a mixed disulfide with mycothiol, resolved by a second molecule
CC       of mycothiol or by mycoredoxin-1. {ECO:0000250|UniProtKB:P9WIE3}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpE subfamily.
CC       {ECO:0000305}.
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DR   EMBL; LT708304; SIU00873.1; -; Genomic_DNA.
DR   RefSeq; NP_855911.1; NC_002945.3.
DR   RefSeq; WP_003411527.1; NC_002945.4.
DR   AlphaFoldDB; P65689; -.
DR   SMR; P65689; -.
DR   PeroxiBase; 6017; MboAhpE.
DR   EnsemblBacteria; SIU00873; SIU00873; BQ2027_MB2262C.
DR   GeneID; 45426218; -.
DR   PATRIC; fig|233413.5.peg.2483; -.
DR   OMA; VCTKELC; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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   Antioxidant; Oxidoreductase; Peroxidase; Redox-active center.
FT   CHAIN           1..153
FT                   /note="Alkyl hydroperoxide reductase E"
FT                   /id="PRO_0000135149"
FT   DOMAIN          2..153
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   153 AA;  16819 MW;  B24927599A0A80E2 CRC64;
     MLNVGATAPD FTLRDQNQQL VTLRGYRGAK NVLLVFFPLA FTGICQGELD QLRDHLPEFE
     NDDSAALAIS VGPPPTHKIW ATQSGFTFPL LSDFWPHGAV SQAYGVFNEQ AGIANRGTFV
     VDRSGIIRFA EMKQPGEVRD QRLWTDALAA LTA