ID   AHPF_ECOLI              Reviewed;         521 AA.
AC   P35340; P77251; P77462;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE            EC=1.8.1.-;
DE   AltName: Full=Alkyl hydroperoxide reductase F52A protein;
GN   Name=ahpF; OrderedLocusNames=b0606, JW0599;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-162.
RC   STRAIN=K12;
RX   PubMed=1592833; DOI=10.1128/jb.174.11.3826-3827.1992;
RA   Smillie D.A., Hayward R.S., Suzuki T., Fujita N., Ishihama A.;
RT   "Locations of genes encoding alkyl hydroperoxide reductase on the physical
RT   map of the Escherichia coli K-12 genome.";
RL   J. Bacteriol. 174:3826-3827(1992).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-354, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
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.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAB40807.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U82598; AAB40807.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73707.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35236.1; -; Genomic_DNA.
DR   EMBL; D13187; BAA02486.1; -; Genomic_DNA.
DR   RefSeq; NP_415139.2; NC_000913.3.
DR   RefSeq; WP_000887629.1; NZ_STEB01000031.1.
DR   PDB; 1FL2; X-ray; 1.90 A; A=212-521.
DR   PDB; 4O5Q; X-ray; 2.00 A; A=1-521.
DR   PDB; 4O5U; X-ray; 2.65 A; A=1-521.
DR   PDB; 4XVG; X-ray; 2.20 A; A=1-521.
DR   PDB; 4YKF; X-ray; 2.50 A; A=1-521.
DR   PDB; 4YKG; X-ray; 2.40 A; A=1-521.
DR   PDBsum; 1FL2; -.
DR   PDBsum; 4O5Q; -.
DR   PDBsum; 4O5U; -.
DR   PDBsum; 4XVG; -.
DR   PDBsum; 4YKF; -.
DR   PDBsum; 4YKG; -.
DR   AlphaFoldDB; P35340; -.
DR   SMR; P35340; -.
DR   BioGRID; 4260706; 10.
DR   ComplexPortal; CPX-4862; Alkyl hydroperoxide reductase complex.
DR   DIP; DIP-9077N; -.
DR   IntAct; P35340; 21.
DR   STRING; 511145.b0606; -.
DR   DrugBank; DB03147; Flavin adenine dinucleotide.
DR   iPTMnet; P35340; -.
DR   jPOST; P35340; -.
DR   PaxDb; 511145-b0606; -.
DR   EnsemblBacteria; AAC73707; AAC73707; b0606.
DR   GeneID; 75170611; -.
DR   GeneID; 947540; -.
DR   KEGG; ecj:JW0599; -.
DR   KEGG; eco:b0606; -.
DR   PATRIC; fig|511145.12.peg.636; -.
DR   EchoBASE; EB1358; -.
DR   eggNOG; COG3634; Bacteria.
DR   HOGENOM; CLU_031864_0_0_6; -.
DR   InParanoid; P35340; -.
DR   OMA; VPYTEGP; -.
DR   OrthoDB; 9806179at2; -.
DR   PhylomeDB; P35340; -.
DR   BioCyc; EcoCyc:EG11385-MONOMER; -.
DR   BioCyc; MetaCyc:EG11385-MONOMER; -.
DR   BRENDA; 1.11.1.26; 2026.
DR   EvolutionaryTrace; P35340; -.
DR   PRO; PR:P35340; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009321; C:alkyl hydroperoxide reductase complex; IDA:EcoCyc.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IGI:EcoliWiki.
DR   GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:ComplexPortal.
DR   GO; GO:0006979; P:response to oxidative stress; NAS:ComplexPortal.
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.
DR   SWISS-2DPAGE; P35340; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Disulfide bond; FAD; Flavoprotein; NAD; NADP;
KW   Oxidoreductase; Redox-active center; Reference proteome.
FT   CHAIN           1..521
FT                   /note="Alkyl hydroperoxide reductase subunit F"
FT                   /id="PRO_0000166774"
FT   BINDING         214..229
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         357..371
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         478..488
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         53
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   MOD_RES         354
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   DISULFID        345..348
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   HELIX           4..15
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          21..26
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   HELIX           31..44
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          62..68
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   HELIX           87..97
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   HELIX           106..113
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   HELIX           132..145
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          149..155
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   HELIX           160..165
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          170..176
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          179..185
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   HELIX           188..195
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   HELIX           203..208
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          213..218
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   HELIX           222..232
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          238..241
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   HELIX           247..251
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          261..265
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   HELIX           266..278
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   TURN            279..281
FT                   /evidence="ECO:0007829|PDB:4O5Q"
FT   STRAND          282..285
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          290..294
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          303..307
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          312..320
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          324..326
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   TURN            332..337
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   TURN            339..341
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          342..344
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   HELIX           346..349
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   HELIX           350..353
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          357..361
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   HELIX           365..375
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          378..384
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          386..389
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   HELIX           394..401
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          406..431
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   TURN            432..434
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          437..441
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          443..447
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          451..454
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   HELIX           456..458
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   TURN            459..461
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   STRAND          483..485
FT                   /evidence="ECO:0007829|PDB:1FL2"
FT   HELIX           497..517
FT                   /evidence="ECO:0007829|PDB:1FL2"
SQ   SEQUENCE   521 AA;  56177 MW;  F39C50F922395B48 CRC64;
     MLDTNMKTQL KAYLEKLTKP VELIATLDDS AKSAEIKELL AEIAELSDKV TFKEDNSLPV
     RKPSFLITNP GSNQGPRFAG SPLGHEFTSL VLALLWTGGH PSKEAQSLLE QIRHIDGDFE
     FETYYSLSCH NCPDVVQALN LMSVLNPRIK HTAIDGGTFQ NEITDRNVMG VPAVFVNGKE
     FGQGRMTLTE IVAKIDTGAE KRAAEELNKR DAYDVLIVGS GPAGAAAAIY SARKGIRTGL
     MGERFGGQIL DTVDIENYIS VPKTEGQKLA GALKVHVDEY DVDVIDSQSA SKLIPAAVEG
     GLHQIETASG AVLKARSIIV ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG PLFKGKRVAV
     IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKL RSLKNVDIIL NAQTTEVKGD
     GSKVVGLEYR DRVSGDIHNI ELAGIFVQIG LLPNTNWLEG AVERNRMGEI IIDAKCETNV
     KGVFAAGDCT TVPYKQIIIA TGEGAKASLS AFDYLIRTKT A
//