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Database: UniProt
Entry: A0A022LGH3_9ACTN
LinkDB: A0A022LGH3_9ACTN
Original site: A0A022LGH3_9ACTN 
ID   A0A022LGH3_9ACTN        Unreviewed;       174 AA.
AC   A0A022LGH3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=H483_0112585 {ECO:0000313|EMBL:EYT61828.1};
OS   Dietzia sp. UCD-THP.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC   Dietzia.
OX   NCBI_TaxID=1292020 {ECO:0000313|EMBL:EYT61828.1, ECO:0000313|Proteomes:UP000019757};
RN   [1] {ECO:0000313|EMBL:EYT61828.1, ECO:0000313|Proteomes:UP000019757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-THP {ECO:0000313|EMBL:EYT61828.1,
RC   ECO:0000313|Proteomes:UP000019757};
RX   PubMed=23661480;
RA   Diep A.L., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT   "Draft Genome Sequence of Dietzia sp. Strain UCD-THP (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:E00197-E00113(2013).
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:EYT61828.1}.
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DR   EMBL; AOSR01000039; EYT61828.1; -; Genomic_DNA.
DR   RefSeq; WP_017837725.1; NZ_KB714654.1.
DR   AlphaFoldDB; A0A022LGH3; -.
DR   eggNOG; COG0599; Bacteria.
DR   HOGENOM; CLU_105328_0_0_11; -.
DR   Proteomes; UP000019757; 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}.
FT   DOMAIN          94..168
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   174 AA;  18770 MW;  E08B08463F8CA11C CRC64;
     MSIENLKSGL PEFAKDLKLN LGSLARSTEL TPQQLWGTFL ATAAATRSET VLSEIADEAR
     EHLTEEAFNA ALGAASIMAM NNVAYRAKEF LGDDYTQVRM GLRMNIIANP GVEKADFELW
     SMAVSTINGC ENCTAAHDDV IRKEGITKEQ AWEAVKIAGT VAGVAQAVEI HANV
//
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