ID   AHPD_MYCUA              Reviewed;         178 AA.
AC   A0PSD4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   02-SEP-2026, entry version 97.
DE   RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000255|HAMAP-Rule:MF_01676};
DE            EC=1.11.1.28 {ECO:0000255|HAMAP-Rule:MF_01676};
DE   AltName: Full=Alkylhydroperoxidase AhpD {ECO:0000255|HAMAP-Rule:MF_01676};
GN   Name=ahpD {ECO:0000255|HAMAP-Rule:MF_01676};
GN   OrderedLocusNames=MUL_3000;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity.
CC       Required for the reduction of the AhpC active site cysteine residues
CC       and for the regeneration of the AhpC enzyme activity.
CC       {ECO:0000255|HAMAP-Rule:MF_01676}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[lipoyl-carrier protein] + a
CC         hydroperoxide = N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein] +
CC         an alcohol + H2O; Xref=Rhea:RHEA:62636, Rhea:RHEA-COMP:10502,
CC         Rhea:RHEA-COMP:16355, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:35924, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100;
CC         EC=1.11.1.28; Evidence={ECO:0000255|HAMAP-Rule:MF_01676};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01676}.
CC   -!- SIMILARITY: Belongs to the AhpD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01676}.
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DR   EMBL; CP000325; ABL05253.1; -; Genomic_DNA.
DR   RefSeq; WP_011740865.1; NC_008611.1.
DR   AlphaFoldDB; A0PSD4; -.
DR   SMR; A0PSD4; -.
DR   PeroxiBase; 4580; MuAhpD.
DR   KEGG; mul:MUL_3000; -.
DR   eggNOG; COG0599; Bacteria.
DR   HOGENOM; CLU_105328_0_0_11; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:TreeGrafter.
DR   GO; GO:0160319; F:lipoyl-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:TreeGrafter.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 1.20.1290.10; AhpD-like; 1.
DR   HAMAP; MF_01676; AhpD; 1.
DR   InterPro; IPR004674; AhpD.
DR   InterPro; IPR029032; AhpD-like.
DR   InterPro; IPR003779; AhpD/CMD-like.
DR   InterPro; IPR004675; AhpD_core.
DR   NCBIfam; TIGR00777; ahpD; 1.
DR   NCBIfam; TIGR00778; ahpD_dom; 1.
DR   PANTHER; PTHR33930; ALKYL HYDROPEROXIDE REDUCTASE AHPD; 1.
DR   PANTHER; PTHR33930:SF7; ALKYL HYDROPEROXIDE REDUCTASE AHPD; 1.
DR   Pfam; PF02627; CMD; 1.
DR   SUPFAM; SSF69118; AhpD-like; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..178
FT                   /note="Alkyl hydroperoxide reductase AhpD"
FT                   /id="PRO_0000359501"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT   ACT_SITE        133
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT   DISULFID        130..133
FT                   /evidence="ECO:0000250"
FT   DISULFID        133
FT                   /note="Interchain (with AhpC); in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
SQ   SEQUENCE   178 AA;  18681 MW;  ACE377FD32410516 CRC64;
     MSIENLKAAL PEYAKDLKLN LGSISRTTVL DEEQLWGTLL ASAAATRNAQ VLAEIGAEAA
     DNLSAQAYQA ALGAVSIMGM NNVFYRGRGF LEGQYDDLRA GLRMNIIANP GVDKANFELW
     SFAVSSVNGC SHCVVAHEHT LREAGVGREA VFEALKAAAI VCGVAQALTA AQTLAAVG
//