ID Q4JY01_CORJK Unreviewed; 526 AA.
AC Q4JY01;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Alkyl hydroperoxide reductase {ECO:0000313|EMBL:CAI36306.1};
GN Name=ahpF {ECO:0000313|EMBL:CAI36306.1};
GN OrderedLocusNames=jk0154 {ECO:0000313|EMBL:CAI36306.1};
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI36306.1, ECO:0000313|Proteomes:UP000000545};
RN [1] {ECO:0000313|EMBL:CAI36306.1, ECO:0000313|Proteomes:UP000000545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411 {ECO:0000313|EMBL:CAI36306.1,
RC ECO:0000313|Proteomes:UP000000545};
RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000849};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000238-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000238-1};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR931997; CAI36306.1; -; Genomic_DNA.
DR RefSeq; WP_011272886.1; NC_007164.1.
DR AlphaFoldDB; Q4JY01; -.
DR STRING; 306537.jk0154; -.
DR GeneID; 3432039; -.
DR KEGG; cjk:jk0154; -.
DR PATRIC; fig|306537.10.peg.167; -.
DR eggNOG; COG3634; Bacteria.
DR HOGENOM; CLU_031864_4_2_11; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000000545; Chromosome.
DR GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0000302; P:response to reactive oxygen species; IEA:InterPro.
DR CDD; cd03026; AhpF_NTD_C; 1.
DR CDD; cd02974; AhpF_NTD_N; 1.
DR Gene3D; 3.40.30.80; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR044141; AhpF_NTD_C.
DR InterPro; IPR044142; AhpF_NTD_N.
DR InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR03140; AhpF; 1.
DR PANTHER; PTHR48105:SF6; ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PIRSF; PIRSF000238; AhpF; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000238-2}; FAD {ECO:0000256|PIRSR:PIRSR000238-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000238-1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000238-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000545}.
FT DOMAIN 129..199
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 217..509
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT COILED 33..60
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 218..233
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 483..493
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 349..352
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 526 AA; 56242 MW; 8FB131F54F17985B CRC64;
MAKQLLDDNL RKQLGQLVPR ITKDIELVYS LDERSASEDL EKLLQDIAEL SDKITARRDD
DAHERKPSFS IVRTGSDISV AFAGIPMGHE FSSLVLALLQ VGGNPIKEDK DLIEQVENLD
GDYEFVTYMS LTCQNCPTVV QALNTMAVLN PRIKHTAVEG SLFQDEVNEN NVLAVPTIYL
NGEEFGQGRT TIEDFVRKLD SGSAAREAKK LNEKDAYEVL VVGQGPAGAA ASIYVARKGL
SVGLIGERFG GQVLDTNSIE NFISVPSTEG PKLAAEFEEH VGQYDIDVVK AQAATGLTPA
TEEGGLHTVH FGDDATLRAR ALVIATGAQW RTLGVPGEEE YRNKGVTFCP HCDGPLFKGK
SVAVIGGGNS GIEAALDLAG VVKHVTVLEF GEACRADDIL MQRVEETANI DVITSAATTE
IVGDGKNVTG LNYTDRTNDE SKSLDVAGVF IQIGLVPNTQ WLGESGLELN KMGEIVVDEH
NATNVPGVYA AGDCTAVPFK QIVIAQGAGA NAALGAWQYT VTAPKA
//
