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AHPD_RHOE4
ID   AHPD_RHOE4              Reviewed;         179 AA.
AC   C0ZYQ9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=RER_27860;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) 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: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   -!- SUBUNIT: Homotrimer. {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; AP008957; BAH33494.1; -; Genomic_DNA.
DR   RefSeq; WP_003942122.1; NC_012490.1.
DR   AlphaFoldDB; C0ZYQ9; -.
DR   SMR; C0ZYQ9; -.
DR   STRING; 234621.RER_27860; -.
DR   EnsemblBacteria; BAH33494; BAH33494; RER_27860.
DR   GeneID; 64140627; -.
DR   KEGG; rer:RER_27860; -.
DR   eggNOG; COG0599; Bacteria.
DR   HOGENOM; CLU_105328_0_0_11; -.
DR   OMA; AIMAMNN; -.
DR   Proteomes; UP000002204; 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.
FT   CHAIN           1..179
FT                   /note="Alkyl hydroperoxide reductase AhpD"
FT                   /id="PRO_1000215889"
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   179 AA;  19105 MW;  A32DCB2D9C96B50E CRC64;
     MSVENLKNSL PEYAKDLKLN LSSIARTTVL NEQQLWGTLL ATAAATKSAS TLKEIASEAA
     DNLSAEAYNA ALGAASIMGM NNVFYRTKGY LDGKYDDLRA GLRMNIIGNP GVDKADFELW
     SLAVSAINGC NHCLEAHENT LRQEGVDREV IFEAIRAGSI VAGVAQAVEA NEILSAAQV
 
 
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