AHPD_BRUAB
ID AHPD_BRUAB Reviewed; 175 AA.
AC Q578J2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=BruAb2_0523;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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 ---------------------------------------------------------------------------
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; AE017224; AAX75942.1; -; Genomic_DNA.
DR RefSeq; WP_002965934.1; NC_006933.1.
DR AlphaFoldDB; Q578J2; -.
DR SMR; Q578J2; -.
DR PeroxiBase; 4605; BabAhpD_9-941.
DR EnsemblBacteria; AAX75942; AAX75942; BruAb2_0523.
DR GeneID; 3827507; -.
DR KEGG; bmb:BruAb2_0523; -.
DR HOGENOM; CLU_105328_0_0_5; -.
DR OMA; AIMAMNN; -.
DR Proteomes; UP000000540; Chromosome II.
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..175
FT /note="Alkyl hydroperoxide reductase AhpD"
FT /id="PRO_0000359476"
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 175 AA; 18783 MW; D8E719C8EBB56ED5 CRC64;
MSIDDLKSKI PDFAKDVRLN LSSMASDETL TPQQKYGLFV ACGIASRNAD VRKALVAEAA
GKVDASVIQA AKAAASIMGM NNVYYRFVHL ASNKDYRTMP ARLRMNVISN PGVDKIDFEL
WSLAVSAING CGMCIDAHED VLRKANVTAE AIQAAVRFAS IIQSAAIALE AADTE