ID A0A1G8MTJ7_9NOCA Unreviewed; 179 AA.
AC A0A1G8MTJ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05444695_11067 {ECO:0000313|EMBL:SDI71186.1};
OS Rhodococcus triatomae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=300028 {ECO:0000313|EMBL:SDI71186.1, ECO:0000313|Proteomes:UP000183263};
RN [1] {ECO:0000313|EMBL:SDI71186.1, ECO:0000313|Proteomes:UP000183263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44892 {ECO:0000313|EMBL:SDI71186.1,
RC ECO:0000313|Proteomes:UP000183263};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNDN01000010; SDI71186.1; -; Genomic_DNA.
DR RefSeq; WP_072738672.1; NZ_FNDN01000010.1.
DR AlphaFoldDB; A0A1G8MTJ7; -.
DR OrthoDB; 9801997at2; -.
DR Proteomes; UP000183263; 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:UP000183263}.
FT DOMAIN 94..174
FT /note="Carboxymuconolactone decarboxylase-like"
FT /evidence="ECO:0000259|Pfam:PF02627"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT ACT_SITE 133
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT DISULFID 130..133
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT DISULFID 133
FT /note="Interchain (with AhpC); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
SQ SEQUENCE 179 AA; 18838 MW; B8C8526BF14526D1 CRC64;
MSVENLKNAL PEYAKDLKLN LSSLARSTEL GEQQLWGTFL AAAAATRSAT VLREIAEEAA
DVLSAEAYNA ALGAASIMGM NNVAYRAKSY LGDDFAQVRV GLRMNIIGNP GVDKADFELW
SLAVSTINGC EHCTAAHDAV VRKEGLTKEQ VWEAVKVAAT LQGVAQAISA AEALAGVNA
//
