ID   AHPD_STRVD              Reviewed;         174 AA.
AC   Q9X5V1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 57.
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}; Synonyms=ahpX;
OS   Streptomyces viridosporus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=67581;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T7A;
RX   PubMed=10902909; DOI=10.3109/10425170009033969;
RA   Ramachandran S., Magnuson T.S., Crawford D.L.;
RT   "Isolation and analysis of three peroxide sensor regulatory gene homologs
RT   ahpC, ahpX and oxyR in Streptomyces viridosporus T7A -- a lignocellulose
RT   degrading actinomycete.";
RL   DNA Seq. 11:51-60(2000).
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=(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: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}.
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   EMBL; AF127576; AAD33341.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X5V1; -.
DR   SMR; Q9X5V1; -.
DR   PeroxiBase; 4602; SvAhpD.
DR   GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032843; F:hydroperoxide reductase activity; IEA:InterPro.
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   Gene3D; 1.20.1290.10; -; 1.
DR   HAMAP; MF_01676; AhpD; 1.
DR   InterPro; IPR004674; AhpD.
DR   InterPro; IPR029032; AhpD-like.
DR   InterPro; IPR004675; AhpD_core.
DR   InterPro; IPR003779; CMD-like.
DR   Pfam; PF02627; CMD; 1.
DR   SUPFAM; SSF69118; SSF69118; 1.
DR   TIGRFAMs; TIGR00777; ahpD; 1.
DR   TIGRFAMs; TIGR00778; ahpD_dom; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           1..174
FT                   /note="Alkyl hydroperoxide reductase AhpD"
FT                   /id="PRO_0000359511"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT   ACT_SITE        134
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT   DISULFID        131..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        134
FT                   /note="Interchain (with AhpC); in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
SQ   SEQUENCE   174 AA;  18808 MW;  EA39EBEECDB18AE7 CRC64;
     MSLDSLKSRI PDYAKDLKLN LGSVIGNSGL PAQQLWGTVL STAIASRSAI VLRELEPEAK
     ANLSPEAYTA AKAAAAVMAM NNVFYRTRHL LSDHEYGNLR AGLRMNVIGN PGVDKVDFEF
     WSFAVSAING CGMCLDSTKQ VLRKAGVERR SSRRRSDCRG TQAVAATLDA EAFS