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Database: UniProt
Entry: A0A1B2R5B1_9BORD
LinkDB: A0A1B2R5B1_9BORD
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ID   A0A1B2R5B1_9BORD        Unreviewed;       172 AA.
AC   A0A1B2R5B1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|HAMAP-Rule:MF_01676};
DE            EC=1.11.1.28 {ECO:0000256|HAMAP-Rule:MF_01676};
DE   AltName: Full=Alkylhydroperoxidase AhpD {ECO:0000256|HAMAP-Rule:MF_01676};
GN   Name=ahpD {ECO:0000256|HAMAP-Rule:MF_01676};
GN   ORFNames=AKI39_17885 {ECO:0000313|EMBL:AOB32182.1};
OS   Bordetella sp. H567.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1697043 {ECO:0000313|EMBL:AOB32182.1, ECO:0000313|Proteomes:UP000093512};
RN   [1] {ECO:0000313|Proteomes:UP000093512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H567 {ECO:0000313|Proteomes:UP000093512};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA   Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA   Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA   Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA   Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA   Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA   Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA   Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01676};
CC   -!- SIMILARITY: Belongs to the AhpD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01676}.
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DR   EMBL; CP012334; AOB32182.1; -; Genomic_DNA.
DR   RefSeq; WP_066639017.1; NZ_CP012334.1.
DR   AlphaFoldDB; A0A1B2R5B1; -.
DR   STRING; 1697043.AKI39_17885; -.
DR   KEGG; boh:AKI39_17885; -.
DR   PATRIC; fig|1697043.4.peg.3668; -.
DR   OrthoDB; 9801997at2; -.
DR   Proteomes; UP000093512; 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:0051920; F:peroxiredoxin activity; IEA:InterPro.
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 {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|HAMAP-
KW   Rule:MF_01676};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_01676};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01676};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW   Rule:MF_01676};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW   Rule:MF_01676}; Reference proteome {ECO:0000313|Proteomes:UP000093512}.
FT   DOMAIN          94..167
FT                   /note="Carboxymuconolactone decarboxylase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02627"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT   ACT_SITE        132
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT   DISULFID        129..132
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT   DISULFID        132
FT                   /note="Interchain (with AhpC); in linked form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
SQ   SEQUENCE   172 AA;  18350 MW;  C41D8684E1E7DDFF CRC64;
     MEFIQTIKDA VPDWAKDIRL NLDGVIARST LPAADAVGAA LAAAFASRSP TLIDAFKQGL
     SETDATAALT AAALMGMNNV WYPYVEMAED AQLKSLPAQL RMNAYSTSGG VEKKRFELFA
     LAASIVGKCH FCVQSHYALL KKEGYTVEQL RDVGRIAAVV NAAALVLTAQ GK
//
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