ID   AHPF_PSEPU              Reviewed;         520 AA.
AC   P0A156; O82864;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE            EC=1.8.1.-;
GN   Name=ahpF;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KT2442-TOL;
RX   PubMed=9827328; DOI=10.1007/s007920050084;
RA   Fukumori F., Hirayama H., Takami H., Inoue A., Horikoshi K.;
RT   "Isolation and transposon mutagenesis of a Pseudomonas putida KT2442
RT   toluene-resistant variant: involvement of an efflux system in solvent
RT   resistance.";
RL   Extremophiles 2:395-400(1998).
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.
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   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AB010689; BAA31469.1; -; Genomic_DNA.
DR   RefSeq; WP_010953390.1; NZ_LT799039.1.
DR   AlphaFoldDB; P0A156; -.
DR   SMR; P0A156; -.
DR   STRING; 1240350.AMZE01000034_gene2265; -.
DR   PATRIC; fig|303.175.peg.816; -.
DR   eggNOG; COG3634; Bacteria.
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; 3.50.50.60; -; 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   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   PIRSF; PIRSF000238; AhpF; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF52833; SSF52833; 2.
DR   TIGRFAMs; TIGR03140; AhpF; 1.
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.
FT   CHAIN           1..520
FT                   /note="Alkyl hydroperoxide reductase subunit F"
FT                   /id="PRO_0000166776"
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