AHPD_BRUA2
ID AHPD_BRUA2 Reviewed; 175 AA.
AC Q2YKW2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=BAB2_0532;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(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; AM040265; CAJ12698.1; -; Genomic_DNA.
DR RefSeq; WP_002965934.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YKW2; -.
DR SMR; Q2YKW2; -.
DR STRING; 359391.BAB2_0532; -.
DR PeroxiBase; 7298; BabAhpD_2308.
DR EnsemblBacteria; CAJ12698; CAJ12698; BAB2_0532.
DR GeneID; 3827507; -.
DR KEGG; bmf:BAB2_0532; -.
DR PATRIC; fig|359391.11.peg.2721; -.
DR HOGENOM; CLU_105328_0_0_5; -.
DR OMA; AIMAMNN; -.
DR PhylomeDB; Q2YKW2; -.
DR Proteomes; UP000002719; 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; Reference proteome.
FT CHAIN 1..175
FT /note="Alkyl hydroperoxide reductase AhpD"
FT /id="PRO_0000359477"
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
