ID   AHPD_COXBU              Reviewed;         177 AA.
AC   Q83BM5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 3.
DT   27-MAR-2024, entry version 112.
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=CBU_1478;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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=a hydroperoxide + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[lipoyl-
CC         carrier protein] = an alcohol + H2O + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [lipoyl-carrier protein]; 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   -!- SIMILARITY: Belongs to the AhpD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01676}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO90975.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE016828; AAO90975.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_820461.2; NC_002971.3.
DR   RefSeq; WP_010958252.1; NC_002971.4.
DR   RefSeq; WP_012220673.1; NZ_CCYB01000024.1.
DR   AlphaFoldDB; Q83BM5; -.
DR   SMR; Q83BM5; -.
DR   STRING; 227377.CBU_1478; -.
DR   PeroxiBase; 4610; CbuAhpD_RSA493.
DR   EnsemblBacteria; AAO90975; AAO90975; CBU_1478.
DR   GeneID; 1209388; -.
DR   KEGG; cbu:CBU_1478; -.
DR   PATRIC; fig|227377.7.peg.1478; -.
DR   eggNOG; COG0599; Bacteria.
DR   HOGENOM; CLU_105328_0_0_6; -.
DR   OrthoDB; 9801997at2; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0032843; F:hydroperoxide reductase activity; IBA:GO_Central.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; IPR004675; AhpD_core.
DR   InterPro; IPR003779; CMD-like.
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..177
FT                   /note="Alkyl hydroperoxide reductase AhpD"
FT                   /id="PRO_0000359485"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT   ACT_SITE        136
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT   DISULFID        133..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        136
FT                   /note="Interchain (with AhpC); in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
SQ   SEQUENCE   177 AA;  19564 MW;  88F1FEDA6BD68A3B CRC64;
     MLQTYKDQLP DYAKDLKLNL TQVLSESPSS ELSNQQITGV ALAVAYATRN RQLIELIFQK
     AEAELDESTL QAIKAAASIM AMNNIYYRFV HLVKDSEYQR LPANLRMNII ANPGIDKKDF
     ELYSLAVSAI NGCGLCIDAH ANTLIKAGFS KHSIQHVIRI AAVLNGLAQV SIIENKT
//