AHPD_COXBN
ID AHPD_COXBN Reviewed; 177 AA.
AC A9KBI4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 3.
DT 25-MAY-2022, entry version 76.
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=CBUD_0522;
OS Coxiella burnetii (strain Dugway 5J108-111).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugway 5J108-111;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
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=ABS76918.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000733; ABS76918.2; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_012220673.1; NC_009727.1.
DR AlphaFoldDB; A9KBI4; -.
DR SMR; A9KBI4; -.
DR EnsemblBacteria; ABS76918; ABS76918; CBUD_0522.
DR KEGG; cbd:CBUD_0522; -.
DR HOGENOM; CLU_105328_0_0_6; -.
DR OMA; AIMAMNN; -.
DR Proteomes; UP000008555; Chromosome.
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; TIGR00778; ahpD_dom; 1.
PE 3: Inferred from homology;
KW Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center.
FT CHAIN 1..177
FT /note="Alkyl hydroperoxide reductase AhpD"
FT /id="PRO_0000359486"
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
