ID A0A170ZSG4_9ACTN Unreviewed; 181 AA.
AC A0A170ZSG4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|HAMAP-Rule:MF_01676};
DE EC=1.11.1.28 {ECO:0000256|HAMAP-Rule:MF_01676};
DE AltName: Full=Alkylhydroperoxidase AhpD {ECO:0000256|HAMAP-Rule:MF_01676};
GN Name=ahpD {ECO:0000256|HAMAP-Rule:MF_01676};
GN ORFNames=STXM2123_4075 {ECO:0000313|EMBL:GAT83374.1};
OS Streptomyces sp. F-3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT83374.1, ECO:0000313|Proteomes:UP000078145};
RN [1] {ECO:0000313|EMBL:GAT83374.1, ECO:0000313|Proteomes:UP000078145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT "Streptomyces sp. F-3 geneom sequencing.";
RL Submitted (MAY-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01676};
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01676}.
CC -!- SIMILARITY: Belongs to the AhpD family. {ECO:0000256|HAMAP-
CC Rule:MF_01676}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAT83374.1}.
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DR EMBL; BDDR01000026; GAT83374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A170ZSG4; -.
DR STRING; 1840095.STXM2123_4075; -.
DR Proteomes; UP000078145; Unassembled WGS sequence.
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; TIGR00777; ahpD; 1.
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 {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|HAMAP-
KW Rule:MF_01676};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_01676};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01676};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_01676};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW Rule:MF_01676}; Reference proteome {ECO:0000313|Proteomes:UP000078145}.
FT DOMAIN 100..180
FT /note="Carboxymuconolactone decarboxylase-like"
FT /evidence="ECO:0000259|Pfam:PF02627"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT ACT_SITE 138
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT DISULFID 135..138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT DISULFID 138
FT /note="Interchain (with AhpC); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
SQ SEQUENCE 181 AA; 19293 MW; 2EEB1B9AD6D62088 CRC64;
MSDAVSLDSL KSALPDYAKD LKLNLGSVIG NSDLPAQQLW GTVLATAIAS RSPIVLRELE
PEAKANLSPE AYTAAKAAAA VMAMNNVFYR TRHLLSDKEY GTLRAGLRMN VIGNPGVDKV
DFELWSFAVS AVNGCGMCLD SHEQVLRKAG VERETIQEAF KIAAVIQAVA TTLDAEAALA
D
//
