ID A0A0P0NAL2_9SPHI Unreviewed; 194 AA.
AC A0A0P0NAL2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AQ505_00610 {ECO:0000313|EMBL:ALL04124.1};
OS Pedobacter sp. PACM 27299.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL04124.1, ECO:0000313|Proteomes:UP000062859};
RN [1] {ECO:0000313|EMBL:ALL04124.1, ECO:0000313|Proteomes:UP000062859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL04124.1,
RC ECO:0000313|Proteomes:UP000062859};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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 -!- SIMILARITY: Belongs to the AhpD family. {ECO:0000256|HAMAP-
CC Rule:MF_01676}.
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DR EMBL; CP012996; ALL04124.1; -; Genomic_DNA.
DR RefSeq; WP_062546388.1; NZ_CP012996.1.
DR AlphaFoldDB; A0A0P0NAL2; -.
DR STRING; 1727164.AQ505_00610; -.
DR KEGG; pep:AQ505_00610; -.
DR OrthoDB; 9801997at2; -.
DR Proteomes; UP000062859; 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 {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:UP000062859}.
FT DOMAIN 138..185
FT /note="Carboxymuconolactone decarboxylase-like"
FT /evidence="ECO:0000259|Pfam:PF02627"
FT ACT_SITE 155
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT ACT_SITE 158
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT DISULFID 155..158
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT DISULFID 158
FT /note="Interchain (with AhpC); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
SQ SEQUENCE 194 AA; 21374 MW; 37ED2670B1FDE7B5 CRC64;
MTAATETIQE LLALVGLETE YRNESLTLLE KGNSRYVRDL KLNLSSTFTS SHLSDKECAL
IALSIAVNNN NKVLIDFFEK LAITKEATAE EIAEAVGCAS LLALNNVFYR FRHFTGKEKY
TQIPARVRMQ IMSSPVTGKE FFELMSIAVS AVNGCEMCVN AHEHSILALG ATEERVFDAV
RIASIVTSAG KVIY
//
