AHPC_MYCTO
ID AHPC_MYCTO Reviewed; 195 AA.
AC P9WQB6; L0T9L3; Q79FE2; Q7BHK8; Q7D758;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Alkyl hydroperoxide reductase C;
DE Short=MtAhpC;
DE EC=1.11.1.28;
DE AltName: Full=Peroxiredoxin;
DE AltName: Full=Thioredoxin peroxidase;
GN Name=ahpC; OrderedLocusNames=MT2503;
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. Together with AhpD, DlaT and Lpd, constitutes
CC an NADH-dependent peroxidase active against hydrogen and alkyl
CC peroxides as well as serving as a peroxynitrite reductase, thus
CC protecting the bacterium against reactive nitrogen intermediates and
CC oxidative stress generated by the host immune system. Does not however
CC seem to play a role in detoxification of isoniazid.
CC {ECO:0000250|UniProtKB:P9WQB7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[lipoyl-carrier protein] + a
CC hydroperoxide = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + an
CC alcohol + H2O; Xref=Rhea:RHEA:62636, Rhea:RHEA-COMP:10502, Rhea:RHEA-
CC COMP:16355, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.11.1.28;
CC Evidence={ECO:0000250|UniProtKB:P9WQB7};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 6 homodimers
CC assemble to form a ring-like dodecamer. Identified in a complex with
CC AhpD, DlaT and Lpd. {ECO:0000250|UniProtKB:P9WQB7}.
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 can subsequently be reduced
CC through a mixed disulfide with the C-terminal cysteine of AhpD,
CC resolved by its second cysteine or by thioredoxin (TrxC).
CC {ECO:0000250|UniProtKB:P9WQB7}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK46800.1; -; Genomic_DNA.
DR RefSeq; WP_003412529.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQB6; -.
DR SMR; P9WQB6; -.
DR PRIDE; P9WQB6; -.
DR EnsemblBacteria; AAK46800; AAK46800; MT2503.
DR GeneID; 45426418; -.
DR KEGG; mtc:MT2503; -.
DR PATRIC; fig|83331.31.peg.2698; -.
DR HOGENOM; CLU_042529_21_3_11; -.
DR Proteomes; UP000001020; Chromosome.
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: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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF121; PTHR10681:SF121; 1.
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; Cytoplasm; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..195
FT /note="Alkyl hydroperoxide reductase C"
FT /id="PRO_0000426804"
FT DOMAIN 4..170
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 61
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P9WQB7"
FT DISULFID 61
FT /note="Interchain (with C-133 in AhpD); transient"
FT /evidence="ECO:0000250|UniProtKB:P9WQB7"
FT DISULFID 61
FT /note="Interchain (with C-174); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P9WQB7"
FT DISULFID 174
FT /note="Interchain (with C-61); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P9WQB7"
SQ SEQUENCE 195 AA; 21566 MW; 011C1014F07C7095 CRC64;
MPLLTIGDQF PAYQLTALIG GDLSKVDAKQ PGDYFTTITS DEHPGKWRVV FFWPKDFTFV
CPTEIAAFSK LNDEFEDRDA QILGVSIDSE FAHFQWRAQH NDLKTLPFPM LSDIKRELSQ
AAGVLNADGV ADRVTFIVDP NNEIQFVSAT AGSVGRNVDE VLRVLDALQS DELCACNWRK
GDPTLDAGEL LKASA
