ID   AHPF_PSEAE              Reviewed;         521 AA.
AC   Q9I6Z2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE            EC=1.8.1.-;
GN   Name=ahpF; OrderedLocusNames=PA0140;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG03530.1; -; Genomic_DNA.
DR   PIR; D83627; D83627.
DR   RefSeq; NP_248830.1; NC_002516.2.
DR   RefSeq; WP_003111221.1; NZ_QZGE01000015.1.
DR   AlphaFoldDB; Q9I6Z2; -.
DR   SMR; Q9I6Z2; -.
DR   STRING; 287.DR97_3097; -.
DR   PaxDb; Q9I6Z2; -.
DR   PRIDE; Q9I6Z2; -.
DR   EnsemblBacteria; AAG03530; AAG03530; PA0140.
DR   GeneID; 879326; -.
DR   KEGG; pae:PA0140; -.
DR   PATRIC; fig|208964.12.peg.146; -.
DR   PseudoCAP; PA0140; -.
DR   HOGENOM; CLU_031864_4_0_6; -.
DR   InParanoid; Q9I6Z2; -.
DR   OMA; VTVFEFM; -.
DR   PhylomeDB; Q9I6Z2; -.
DR   BioCyc; PAER208964:G1FZ6-142-MON; -.
DR   BRENDA; 1.11.1.26; 5087.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..521
FT                   /note="Alkyl hydroperoxide reductase subunit F"
FT                   /id="PRO_0000287807"
FT   BINDING         213..228
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   521 AA;  55836 MW;  58BD97E3AE1E32BA CRC64;
     MLDANLKTQL KAYLEKVSQP FEIVASLDDS DKSRELLGLL QDIVGLTDKI TLKTDGSDAR
     KPSFSLNRPG ADIGLRFAGI PMGHEFTSLV LALLQVGGHP SKLDADVIEQ VKGIEGTFEF
     ETYFSLSCQN CPDVVQALNL MAVLNPNIRH VAIDGALFQD EVEARQIMSV PSIYLNGEVF
     GQGRMGVEEI LAKIDTGAAA RDAEKLTARD AFDVLVVGGG PAGAAAAIYA ARKGIRTGVA
     AERFGGQVLD TMAIENFISV QETEGPKLAR ALEEHVRHYE VDIMNLQRAS KLVPAKNAGE
     LHEVRFESGG SLKAKTLILA TGARWREMGV PGEQEYKAKG VCFCPHCDGP LFKGKRVAVI
     GGGNSGVEAA IDLAGIVAHV TLLEFDSKLR ADAVLQRKLY SLPNVEVITS ALTSEVKGDG
     QKVTGLVYKD RNSEEFKSIE LEGIFVQIGL LPNTEWLKGS VELSPRGEII VDARGETSLP
     GIFAAGDVTT VPYKQIVIAV GEGAKASLSA FDHLIRTSAP E