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Database: UniProt
Entry: B3R4U6_CUPTR
LinkDB: B3R4U6_CUPTR
Original site: B3R4U6_CUPTR 
ID   B3R4U6_CUPTR            Unreviewed;       173 AA.
AC   B3R4U6;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 96.
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   OrderedLocusNames=RALTA_A1373 {ECO:0000313|EMBL:CAQ69329.1};
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ69329.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAQ69329.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ69329.1; -; Genomic_DNA.
DR   RefSeq; WP_012352654.1; NC_010528.1.
DR   AlphaFoldDB; B3R4U6; -.
DR   PeroxiBase; 12499; CtaiAhpD01_LMG19424.
DR   GeneID; 29761759; -.
DR   KEGG; cti:RALTA_A1373; -.
DR   eggNOG; COG0599; Bacteria.
DR   HOGENOM; CLU_105328_0_0_4; -.
DR   BioCyc; CTAI977880:RALTA_RS06580-MONOMER; -.
DR   Proteomes; UP000001692; Chromosome 1.
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; 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          93..172
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   173 AA;  18415 MW;  9997A6E2AE7CC4A8 CRC64;
     MEFLSTIKNL IPDYAKDIRL NVDGTIARSS LEGNDAVGVA LAAAFAAQSK VLVDAIRNAG
     VLSPDETNGA LTAAALMGMN NTWYPYVEMA DDPDLASQPA GLRMNAYATH GGVDKRRFEM
     YALAASIVGK CHFCVKSHYQ LLKNEQGMTA QQLRDVGRIA AVIVAAANVI AAQ
//
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