ID   AHPF_XANCH              Reviewed;         530 AA.
AC   O06465;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE            EC=1.8.1.-;
GN   Name=ahpF;
OS   Xanthomonas campestris pv. phaseoli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=317013;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9190810; DOI=10.1128/jb.179.12.3944-3949.1997;
RA   Loprasert S., Atichartpongkul S., Whangsuk W., Mongkolsuk S.;
RT   "Isolation and analysis of the Xanthomonas alkyl hydroperoxide reductase
RT   gene and the peroxide sensor regulator genes ahpC and ahpF-oxyR-orfX.";
RL   J. Bacteriol. 179:3944-3949(1997).
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}.
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; U94336; AAC45426.1; -; Genomic_DNA.
DR   RefSeq; WP_039567731.1; NZ_OCZD01000086.1.
DR   AlphaFoldDB; O06465; -.
DR   SMR; O06465; -.
DR   STRING; 317013.NY99_15100; -.
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..530
FT                   /note="Alkyl hydroperoxide reductase subunit F"
FT                   /id="PRO_0000166787"
FT   BINDING         214..229
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         356..370
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         477..487
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        344..347
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   530 AA;  56922 MW;  ABC1105C8A6FCD24 CRC64;
     MLDANLKTQL TAYLERVTRP IQINASIDDS AGSREMLDLL EELVLLSDKI SLDIHRDDNQ
     RKPSFALTTP GQDISLRFAG LPMGHEFTSL VLALLQVGGH PSKAAAELIE QVQHLEGDYQ
     FETYFSLSCQ NCPDVVQALN LAAVLNPRIK HVAIDGAWFQ DEVQARQIMS VPTVYLNGEL
     FDQGRMTLEQ IVAKLDTNAA KRDAAKIAAK EAFDVLVVGG GPAGSAAAVY AARKGIRTGV
     AAERFGGQVL DTMSIENFIS VPETEGPKMA AALEQHVRQY DVDIMNLQRA EQLIPAGADG
     LIEIKLANGA SLKSKTVILS TGARWRQMNV PGEDQYKNKG VAYCPHCDGP LFKGKRVAVI
     GGGNSGVEAA IDLAGIVAHV TLVEFDDKLR ADEVLQRKLR SLHNVRIITS AQTTEVLGDG
     QKVTGLVYKD RTGGDIQHIE LEGVFVQIGL LPNTEFLRGT VALSPRGEII VDDRGQTDVP
     GVFAAGDATT VPYKQIVIAM GEGSKAALSA FDHLIRTSAP ATADSVAQAA