ID AHPD_ANADF Reviewed; 185 AA.
AC A7HCA3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=Anae109_2147;
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5;
RX PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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=a hydroperoxide + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[lipoyl-
CC carrier protein] = an alcohol + H2O + N(6)-[(R)-lipoyl]-L-lysyl-
CC [lipoyl-carrier protein]; Xref=Rhea:RHEA:62636, Rhea:RHEA-COMP:10502,
CC Rhea:RHEA-COMP:16355, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:35924, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100;
CC EC=1.11.1.28; 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; CP000769; ABS26349.1; -; Genomic_DNA.
DR RefSeq; WP_012096930.1; NC_009675.1.
DR AlphaFoldDB; A7HCA3; -.
DR SMR; A7HCA3; -.
DR STRING; 404589.Anae109_2147; -.
DR KEGG; afw:Anae109_2147; -.
DR eggNOG; COG2128; Bacteria.
DR HOGENOM; CLU_105328_0_0_7; -.
DR OrthoDB; 9801997at2; -.
DR Proteomes; UP000006382; 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:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.20.1290.10; AhpD-like; 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 NCBIfam; TIGR00778; ahpD_dom; 1.
DR PANTHER; PTHR33930; ALKYL HYDROPEROXIDE REDUCTASE AHPD; 1.
DR PANTHER; PTHR33930:SF7; ALKYL HYDROPEROXIDE REDUCTASE AHPD; 1.
DR Pfam; PF02627; CMD; 1.
DR SUPFAM; SSF69118; AhpD-like; 1.
PE 3: Inferred from homology;
KW Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..185
FT /note="Alkyl hydroperoxide reductase AhpD"
FT /id="PRO_0000359469"
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 185 AA; 19133 MW; 7764DC8C4ABBE19F CRC64;
MSPVDRLREA LPDAARDVRL NLQAVLQGGA LTEGQRWGVA VASAAAARQP ALLSAVLAEA
RSRGLDSAAE DGLAAAALMA MNNVYYRFRH MVGKPGYTEM PARLRMGRLA QPATSRADLE
LFSLAASAIN GCEACVRTHE DVVVKGGIGE EAVHDAVRIA AVIHAAAVAL EAGEVAGGHE
AVSAA
//
