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Database: UniProt
Entry: A0A0B4Y453_9PROT
LinkDB: A0A0B4Y453_9PROT
Original site: A0A0B4Y453_9PROT 
ID   A0A0B4Y453_9PROT        Unreviewed;       178 AA.
AC   A0A0B4Y453;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=TH3_16455 {ECO:0000313|EMBL:AJD53393.1};
OS   Thalassospira xiamenensis M-5 = DSM 17429.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassospiraceae; Thalassospira.
OX   NCBI_TaxID=1123366 {ECO:0000313|EMBL:AJD53393.1, ECO:0000313|Proteomes:UP000007127};
RN   [1] {ECO:0000313|EMBL:AJD53393.1, ECO:0000313|Proteomes:UP000007127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M-5 {ECO:0000313|EMBL:AJD53393.1,
RC   ECO:0000313|Proteomes:UP000007127};
RX   PubMed=23209216; DOI=10.1128/JB.01904-12;
RA   Lai Q., Shao Z.;
RT   "Genome sequence of Thalassospira xiamenensis type strain M-5.";
RL   J. Bacteriol. 194:6957-6957(2012).
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; CP004388; AJD53393.1; -; Genomic_DNA.
DR   RefSeq; WP_007090069.1; NZ_FTON01000005.1.
DR   AlphaFoldDB; A0A0B4Y453; -.
DR   STRING; 1123366.TH3_16455; -.
DR   GeneID; 31928964; -.
DR   KEGG; txi:TH3_16455; -.
DR   eggNOG; COG2128; Bacteria.
DR   HOGENOM; CLU_105328_0_0_5; -.
DR   Proteomes; UP000007127; 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; 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          95..177
FT                   /note="Carboxymuconolactone decarboxylase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02627"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT   ACT_SITE        135
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT   DISULFID        132..135
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT   DISULFID        135
FT                   /note="Interchain (with AhpC); in linked form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
SQ   SEQUENCE   178 AA;  19055 MW;  D34D1DA742DD33D6 CRC64;
     MSSISEIKDV MPDYAKDLKL NLSSLANNPG MTDQQVYGTA LACAYASRNA KLLKAVAAEA
     KTKLSDEAFQ AAKGAAAIMG MNNIYYRFTH LVSEPEYATM PARLRMNIIG KPGIDKADFE
     LFSLAVSAIN GCGMCIDSHE KVLKNAGIKK ETVQNAVRIA SVIHAVAVVL DAEDALAE
//
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