ID   AHPF_PSEPK              Reviewed;         520 AA.
AC   P0A155; O82864;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   04-NOV-2026, entry version 119.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE            EC=1.8.1.-;
GN   Name=ahpF; OrderedLocusNames=PP_2440;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- FUNCTION: Serves to protect the cell against DNA damage by alkyl
CC       hydroperoxides. It can use either NADH or NADPH as electron donor for
CC       direct reduction of redox dyes or of alkyl hydroperoxides when combined
CC       with the AhpC protein (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN68052.1; -; Genomic_DNA.
DR   RefSeq; WP_010953390.1; NC_002947.4.
DR   AlphaFoldDB; P0A155; -.
DR   SMR; P0A155; -.
DR   STRING; 160488.PP_2440; -.
DR   PaxDb; 160488-PP_2440; -.
DR   GeneID; 83681042; -.
DR   KEGG; ppu:PP_2440; -.
DR   PATRIC; fig|160488.4.peg.2585; -.
DR   eggNOG; COG3634; Bacteria.
DR   HOGENOM; CLU_031864_4_2_6; -.
DR   OMA; AADFRTH; -.
DR   OrthoDB; 9806179at2; -.
DR   PhylomeDB; P0A155; -.
DR   BioCyc; PPUT160488:G1G01-2607-MONOMER; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:UniProtKB-ARBA.
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   FunFam; 3.50.50.60:FF:000007; Alkyl hydroperoxide reductase, F subunit; 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; IPR050097; Ferredoxin-NADP_redctase-like.
DR   InterPro; IPR008255; PNDR_II_active_site.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR03140; AhpF; 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   Disulfide bond; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..520
FT                   /note="Alkyl hydroperoxide reductase subunit F"
FT                   /id="PRO_0000166775"
FT   BINDING         213..228
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         355..369
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         476..486
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        343..346
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   520 AA;  55350 MW;  08FB3DE0D75C8A27 CRC64;
     MLDATLKSQL KTYLERVTQP IEIVASLDDG AKSRELHDLL VEIASLSNLI TFSADGTDAR
     RPSFSLNRPG ADISLRFAGI PMGHEFTSLV LALLQVGGHP SKASAEVIEQ IQALEGEFNF
     ETYFSLSCQN CPDVVQALNL MAVLNPNVRH VAIDGALFQD EVESRKIMAV PSIYLNGEVF
     GQGRMGLEEI LGKIDTNAGA RQAEKINAKE AFDVLVVGGG PAGAAAAIYA ARKGIRTGVA
     AERFGGQVLD TLAIENFISV QETEGPKLAT ALEEHVKQYD VDIMNLQRGE ALIPAAEGGL
     HEVRLAGGAS LKAKTVILAT GARWREMNVP GEQEYRGRGV AYCPHCDGPL FKGKRVAVIG
     GGNSGVEAAI DLAGIVAQVT LIEFDSQLRA DAVLQRKLRS LPNVNVITSA LTTEVLGNGE
     KVTGLRYKDR STDEQHEVAL EGIFVQIGLL PNTDWLKGTV ELSPRGEIIV DAKGQTSIPG
     VFAAGDVTTV PYKQIVIAVG EGAKASLAAF DHLIRTSAPA
//