ID   AHPD_GRABC              Reviewed;         175 AA.
AC   Q0BUC5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   25-MAY-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};
GN   OrderedLocusNames=GbCGDNIH1_0679;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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=ABI61577.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000394; ABI61577.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043452720.1; NC_008343.2.
DR   AlphaFoldDB; Q0BUC5; -.
DR   SMR; Q0BUC5; -.
DR   STRING; 391165.GbCGDNIH1_0679; -.
DR   PeroxiBase; 4629; GbeAhpD.
DR   EnsemblBacteria; ABI61577; ABI61577; GbCGDNIH1_0679.
DR   KEGG; gbe:GbCGDNIH1_0679; -.
DR   eggNOG; COG2128; Bacteria.
DR   HOGENOM; CLU_105328_0_0_5; -.
DR   Proteomes; UP000001963; 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; 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_0000359491"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT   ACT_SITE        133
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT   DISULFID        130..133
FT                   /evidence="ECO:0000250"
FT   DISULFID        133
FT                   /note="Interchain (with AhpC); in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
SQ   SEQUENCE   175 AA;  18531 MW;  ADAC7F9710210FB4 CRC64;
     MSIENLKNAL PEYAKDLKLN LGSLANEDVL NQQQKAGTFI ASALASRSNL VTSAILAEFG
     PQLSAEALAA AKAAAAIMGM NNVYYRFVHL VGGDYANLPA RLRMNVMAKP GVDKVDFELW
     SLAVSAINGC GMCMESHEKI VRQNGLTQEQ VQAAIRIAAT VHAVAATLDG EAALS