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Database: UniProt
Entry: X8BGB3_MYCXE
LinkDB: X8BGB3_MYCXE
Original site: X8BGB3_MYCXE 
ID   X8BGB3_MYCXE            Unreviewed;       178 AA.
AC   X8BGB3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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   ECO:0000313|EMBL:EUA42521.1};
GN   ORFNames=I553_6381 {ECO:0000313|EMBL:EUA42521.1};
OS   Mycobacterium xenopi 4042.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1299334 {ECO:0000313|EMBL:EUA42521.1};
RN   [1] {ECO:0000313|EMBL:EUA42521.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4042 {ECO:0000313|EMBL:EUA42521.1};
RA   Brown-Elliot B., Wallace R., Lenaerts A., Ordway D., DeGroote M.A.,
RA   Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA   Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL   Submitted (JAN-2014) 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:EUA42521.1}.
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DR   EMBL; JAOB01000042; EUA42521.1; -; Genomic_DNA.
DR   AlphaFoldDB; X8BGB3; -.
DR   PATRIC; fig|1299334.3.peg.4545; -.
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}.
FT   DOMAIN          101..175
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   178 AA;  18754 MW;  E5407861EE7B8388 CRC64;
     MSIENLKSAL PEYAKDLKLN LGSITRTTAL NEEQLWGTLL ASAAATRNTQ VLAEIGAEAA
     DYLSAEAYQA ALGAAAIMGM NNVFYRARGF LGGQYDDLRP GLRMNIIANP GVDKANFELW
     SFAVSSINGC PDCVNAHERT LRDAGVGRET IYEALKVAAI VAGVAQATTT AQALAAAS
//
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