AHPE_MYCTO
ID AHPE_MYCTO Reviewed; 153 AA.
AC P9WIE2; L0TAL3; P65688; Q10520;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
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=MT2298;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK46582.1; -; Genomic_DNA.
DR PIR; B70778; B70778.
DR RefSeq; WP_003411527.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WIE2; -.
DR SMR; P9WIE2; -.
DR EnsemblBacteria; AAK46582; AAK46582; MT2298.
DR GeneID; 45426218; -.
DR KEGG; mtc:MT2298; -.
DR PATRIC; fig|83331.31.peg.2475; -.
DR HOGENOM; CLU_042529_14_2_11; -.
DR Proteomes; UP000001020; 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_0000428022"
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