AHPD_BRADU
ID AHPD_BRADU Reviewed; 182 AA.
AC Q9ANL0; Q79UU8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=bll1776;
GN ORFNames=id138;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=11157954; DOI=10.1128/jb.183.4.1405-1412.2001;
RA Goettfert M., Roethlisberger S., Kuendig C., Beck C., Marty R.,
RA Hennecke H.;
RT "Potential symbiosis-specific genes uncovered by sequencing a 410-kb DNA
RT region of the Bradyrhizobium japonicum chromosome.";
RL J. Bacteriol. 183:1405-1412(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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}.
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DR EMBL; AF322012; AAG60760.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC47041.1; -; Genomic_DNA.
DR RefSeq; NP_768416.1; NC_004463.1.
DR RefSeq; WP_011084585.1; NZ_CP011360.1.
DR AlphaFoldDB; Q9ANL0; -.
DR SMR; Q9ANL0; -.
DR STRING; 224911.27350029; -.
DR PeroxiBase; 4608; BjaAhpD.
DR EnsemblBacteria; BAC47041; BAC47041; BAC47041.
DR GeneID; 64067080; -.
DR KEGG; bja:bll1776; -.
DR PATRIC; fig|224911.44.peg.1244; -.
DR eggNOG; COG2128; Bacteria.
DR HOGENOM; CLU_105328_0_0_5; -.
DR InParanoid; Q9ANL0; -.
DR OMA; AIMAMNN; -.
DR PhylomeDB; Q9ANL0; -.
DR Proteomes; UP000002526; 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; 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..182
FT /note="Alkyl hydroperoxide reductase AhpD"
FT /id="PRO_0000359473"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT ACT_SITE 135
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT DISULFID 132..135
FT /evidence="ECO:0000250"
FT DISULFID 135
FT /note="Interchain (with AhpC); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
SQ SEQUENCE 182 AA; 19183 MW; 7B0DB05437592A02 CRC64;
MSPIEQIYDK IPDFAKDVRI NLTSLMADET LSPRRKYGVL VASAVATRNS ALIAAVESAA
SGVMTSVAIA AAKAAASVVV MNNVYYRFVH LASNPEYKTM PPRLRMDVIG NPGVDKSDFE
LWSLAVSSIN GCGICIDAHE RTLRAAGVNS ETIQTAVRFA AITQSVAIAL EAAGPASPQA
GD
