SWISSPROT: AHPD_ANADE

ID   AHPD_ANADE              Reviewed;         186 AA.
AC   Q2IMQ8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000255|HAMAP-Rule:MF_01676};
DE            EC=1.11.1.15 {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=Adeh_0314;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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
CC       residues and for the regeneration of the AhpC enzyme activity.
CC       {ECO:0000255|HAMAP-Rule:MF_01676}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide
CC         + an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593,
CC         Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC         EC=1.11.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01676};
CC   -!- SIMILARITY: Belongs to the AhpD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01676}.
DR   EMBL; CP000251; ABC80090.1; -; Genomic_DNA.
DR   RefSeq; WP_011419373.1; NC_007760.1.
DR   SMR; Q2IMQ8; -.
DR   STRING; 290397.Adeh_0314; -.
DR   PeroxiBase; 4611; AdAhpD.
DR   EnsemblBacteria; ABC80090; ABC80090; Adeh_0314.
DR   KEGG; ade:Adeh_0314; -.
DR   eggNOG; ENOG4108X7C; Bacteria.
DR   eggNOG; COG2128; LUCA.
DR   HOGENOM; HOG000261487; -.
DR   KO; K04756; -.
DR   OMA; AIMAMNN; -.
DR   BioCyc; ADEH290397:G1G5W-321-MONOMER; -.
DR   Proteomes; UP000001935; 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:UniProtKB-EC.
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; TIGR00778; ahpD_dom; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMQ8.
DR   SWISS-2DPAGE; Q2IMQ8.
KW   Antioxidant; Complete proteome; Disulfide bond; Oxidoreductase;
KW   Peroxidase; Redox-active center; Reference proteome.
FT   CHAIN         1    186       Alkyl hydroperoxide reductase AhpD.
FT                                /FTId=PRO_0000359468.
FT   ACT_SITE    132    132       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01676}.
FT   ACT_SITE    135    135       Cysteine sulfenic acid (-SOH)
FT                                intermediate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01676}.
FT   DISULFID    132    135       {ECO:0000250}.
FT   DISULFID    135    135       Interchain (with AhpC); in linked form.
FT                                {ECO:0000255|HAMAP-Rule:MF_01676}.
SQ   SEQUENCE   186 AA;  19330 MW;  0EBC8D63687D7E05 CRC64;
     MAALDAIREA LPEPARDIKL NLQAVLQPGP LTPAQRWGVA VATAAAARNE RLLAAILADA
     RAEVEPAVVE DALAAAAVMA MNNVYYRFRH MVGKPSYSEK PARLRMNRLV KPAASKLDFE
     LFALAVSAVN GCETCVRSHE QVVVGGGVSE DQVHDAVRIA AVVHAAAVAL ELAGHAAAPS
     AAAAAG
//