AHPF_ECOLI
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 03-AUG-2022, entry version 185.
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; Proteobacteria; 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 SWISS-2DPAGE; P35340; -.
DR jPOST; P35340; -.
DR PaxDb; P35340; -.
DR PRIDE; P35340; -.
DR EnsemblBacteria; AAC73707; AAC73707; b0606.
DR EnsemblBacteria; BAA35236; BAA35236; BAA35236.
DR GeneID; 66671118; -.
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; VTVFEFM; -.
DR PhylomeDB; P35340; -.
DR BioCyc; EcoCyc:EG11385-MON; -.
DR BioCyc; MetaCyc:EG11385-MON; -.
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 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; IC: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; 3.50.50.60; -; 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 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
