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Database: UniProt
Entry: A0A255XTB6_9PROT
LinkDB: A0A255XTB6_9PROT
Original site: A0A255XTB6_9PROT 
ID   A0A255XTB6_9PROT        Unreviewed;       177 AA.
AC   A0A255XTB6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=CHR90_08775 {ECO:0000313|EMBL:OYQ19500.1};
OS   Elstera cyanobacteriorum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Elstera.
OX   NCBI_TaxID=2022747 {ECO:0000313|EMBL:OYQ19500.1, ECO:0000313|Proteomes:UP000216361};
RN   [1] {ECO:0000313|EMBL:OYQ19500.1, ECO:0000313|Proteomes:UP000216361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH019 {ECO:0000313|EMBL:OYQ19500.1,
RC   ECO:0000313|Proteomes:UP000216361};
RA   Cai H.;
RT   "Elstera cyanobacteriorum sp. nov., a novel bacterium isolated from
RT   cyanobacterial aggregates in a eutrophic lake.";
RL   Submitted (JUL-2017) 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}.
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:OYQ19500.1}.
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DR   EMBL; NOXS01000031; OYQ19500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255XTB6; -.
DR   OrthoDB; 9801997at2; -.
DR   Proteomes; UP000216361; 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:UP000216361}.
FT   DOMAIN          98..175
FT                   /note="Carboxymuconolactone decarboxylase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02627"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT   ACT_SITE        134
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT   DISULFID        131..134
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
FT   DISULFID        134
FT                   /note="Interchain (with AhpC); in linked form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01676"
SQ   SEQUENCE   177 AA;  18534 MW;  D29D3B3CCACD3E0E CRC64;
     MSIETLKSAL PDYAKDLRLN LSSVLSQPML SANQTWGTAL ATAIAARNPA VIAAINAELQ
     GKIDATNITA AKTAAALMGM NNIYYRYVHL SPTADFKTMR AGLRMNGMVG HGADGLDFEL
     WSLAVSAVNG CGMCIESHEH EVFKKGATKE QVQAVVKIAA VITAVSAALE GAAALGE
//
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