AHPD_COXBU
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 25-MAY-2022, entry version 105.
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}; OrderedLocusNames=CBU_1478;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; 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=(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 -!- 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};
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; AE016828; AAO90975.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_820461.2; NC_002971.3.
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 OMA; AIMAMNN; -.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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; -; 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; TIGR00778; ahpD_dom; 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
