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Protein

Alkyl hydroperoxide reductase subunit F

Gene

ahpF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi214 – 22916FADBy similarityAdd
BLAST
Nucleotide bindingi357 – 37115NAD or NADPBy similarityAdd
BLAST
Nucleotide bindingi478 – 48811FADBy similarityAdd
BLAST

GO - Molecular functioni

  • alkyl hydroperoxide reductase activity Source: EcoliWiki
  • electron carrier activity Source: InterPro
  • FAD binding Source: EcoCyc
  • flavin adenine dinucleotide binding Source: EcoliWiki
  • NAD binding Source: InterPro
  • NADPH binding Source: EcoliWiki
  • protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD, NADP

Enzyme and pathway databases

BioCyciEcoCyc:EG11385-MONOMER.
ECOL316407:JW0599-MONOMER.
MetaCyc:EG11385-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyl hydroperoxide reductase subunit F (EC:1.8.1.-)
Alternative name(s):
Alkyl hydroperoxide reductase F52A protein
Gene namesi
Name:ahpF
Ordered Locus Names:b0606, JW0599
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11385. ahpF.

Subcellular locationi

GO - Cellular componenti

  • alkyl hydroperoxide reductase complex Source: EcoCyc
  • cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Alkyl hydroperoxide reductase subunit FPRO_0000166774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysine1 Publication
Disulfide bondi345 ↔ 348Redox-activeBy similarity
Modified residuei354 – 3541N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiP35340.
PaxDbiP35340.
PRIDEiP35340.

2D gel databases

SWISS-2DPAGEP35340.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4260706. 6 interactions.
DIPiDIP-9077N.
IntActiP35340. 21 interactions.
STRINGi511145.b0606.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1512Combined sources
Beta strandi21 – 266Combined sources
Helixi31 – 4414Combined sources
Beta strandi50 – 545Combined sources
Beta strandi58 – 603Combined sources
Beta strandi62 – 687Combined sources
Beta strandi77 – 804Combined sources
Helixi84 – 863Combined sources
Helixi87 – 9711Combined sources
Helixi106 – 1138Combined sources
Beta strandi119 – 1257Combined sources
Helixi132 – 14514Combined sources
Beta strandi149 – 1557Combined sources
Turni156 – 1583Combined sources
Helixi160 – 1656Combined sources
Beta strandi170 – 1767Combined sources
Beta strandi179 – 1857Combined sources
Helixi188 – 1958Combined sources
Helixi203 – 2086Combined sources
Beta strandi213 – 2186Combined sources
Helixi222 – 23211Combined sources
Turni233 – 2353Combined sources
Beta strandi238 – 2414Combined sources
Helixi247 – 2515Combined sources
Beta strandi261 – 2655Combined sources
Helixi266 – 27813Combined sources
Turni279 – 2813Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi303 – 3075Combined sources
Beta strandi312 – 3209Combined sources
Beta strandi324 – 3263Combined sources
Turni332 – 3376Combined sources
Turni339 – 3413Combined sources
Beta strandi342 – 3443Combined sources
Helixi346 – 3494Combined sources
Helixi350 – 3534Combined sources
Beta strandi357 – 3615Combined sources
Helixi365 – 37511Combined sources
Beta strandi378 – 3847Combined sources
Beta strandi386 – 3894Combined sources
Helixi394 – 4018Combined sources
Beta strandi406 – 43126Combined sources
Turni432 – 4343Combined sources
Beta strandi437 – 4415Combined sources
Beta strandi443 – 4475Combined sources
Beta strandi451 – 4544Combined sources
Helixi456 – 4583Combined sources
Turni459 – 4613Combined sources
Beta strandi483 – 4853Combined sources
Helixi497 – 51721Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FL2X-ray1.90A212-521[»]
4O5QX-ray2.00A1-521[»]
4O5UX-ray2.65A1-521[»]
4XVGX-ray2.20A1-521[»]
4YKFX-ray2.50A1-521[»]
4YKGX-ray2.40A1-521[»]
ProteinModelPortaliP35340.
SMRiP35340. Positions 1-521.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35340.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4108JU3. Bacteria.
COG3634. LUCA.
HOGENOMiHOG000169462.
InParanoidiP35340.
KOiK03387.
OMAiAVRKPSF.
PhylomeDBiP35340.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
3.50.50.60. 2 hits.
InterProiIPR012081. Alkyl_hydroperoxide_Rdtase_suF.
IPR023753. FAD/NAD-binding_dom.
IPR002109. Glutaredoxin.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF13192. Thioredoxin_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000238. AhpF. 1 hit.
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR03140. AhpF. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35340-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDTNMKTQL KAYLEKLTKP VELIATLDDS AKSAEIKELL AEIAELSDKV
60 70 80 90 100
TFKEDNSLPV RKPSFLITNP GSNQGPRFAG SPLGHEFTSL VLALLWTGGH
110 120 130 140 150
PSKEAQSLLE QIRHIDGDFE FETYYSLSCH NCPDVVQALN LMSVLNPRIK
160 170 180 190 200
HTAIDGGTFQ NEITDRNVMG VPAVFVNGKE FGQGRMTLTE IVAKIDTGAE
210 220 230 240 250
KRAAEELNKR DAYDVLIVGS GPAGAAAAIY SARKGIRTGL MGERFGGQIL
260 270 280 290 300
DTVDIENYIS VPKTEGQKLA GALKVHVDEY DVDVIDSQSA SKLIPAAVEG
310 320 330 340 350
GLHQIETASG AVLKARSIIV ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG
360 370 380 390 400
PLFKGKRVAV IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKL
410 420 430 440 450
RSLKNVDIIL NAQTTEVKGD GSKVVGLEYR DRVSGDIHNI ELAGIFVQIG
460 470 480 490 500
LLPNTNWLEG AVERNRMGEI IIDAKCETNV KGVFAAGDCT TVPYKQIIIA
510 520
TGEGAKASLS AFDYLIRTKT A
Length:521
Mass (Da):56,177
Last modified:November 1, 1997 - v2
Checksum:iF39C50F922395B48
GO

Sequence cautioni

The sequence AAB40807 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82598 Genomic DNA. Translation: AAB40807.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73707.2.
AP009048 Genomic DNA. Translation: BAA35236.1.
D13187 Genomic DNA. Translation: BAA02486.1.
RefSeqiNP_415139.2. NC_000913.3.
WP_000887629.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73707; AAC73707; b0606.
BAA35236; BAA35236; BAA35236.
GeneIDi947540.
KEGGiecj:JW0599.
eco:b0606.
PATRICi32116392. VBIEscCol129921_0636.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82598 Genomic DNA. Translation: AAB40807.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73707.2.
AP009048 Genomic DNA. Translation: BAA35236.1.
D13187 Genomic DNA. Translation: BAA02486.1.
RefSeqiNP_415139.2. NC_000913.3.
WP_000887629.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FL2X-ray1.90A212-521[»]
4O5QX-ray2.00A1-521[»]
4O5UX-ray2.65A1-521[»]
4XVGX-ray2.20A1-521[»]
4YKFX-ray2.50A1-521[»]
4YKGX-ray2.40A1-521[»]
ProteinModelPortaliP35340.
SMRiP35340. Positions 1-521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260706. 6 interactions.
DIPiDIP-9077N.
IntActiP35340. 21 interactions.
STRINGi511145.b0606.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

2D gel databases

SWISS-2DPAGEP35340.

Proteomic databases

EPDiP35340.
PaxDbiP35340.
PRIDEiP35340.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73707; AAC73707; b0606.
BAA35236; BAA35236; BAA35236.
GeneIDi947540.
KEGGiecj:JW0599.
eco:b0606.
PATRICi32116392. VBIEscCol129921_0636.

Organism-specific databases

EchoBASEiEB1358.
EcoGeneiEG11385. ahpF.

Phylogenomic databases

eggNOGiENOG4108JU3. Bacteria.
COG3634. LUCA.
HOGENOMiHOG000169462.
InParanoidiP35340.
KOiK03387.
OMAiAVRKPSF.
PhylomeDBiP35340.

Enzyme and pathway databases

BioCyciEcoCyc:EG11385-MONOMER.
ECOL316407:JW0599-MONOMER.
MetaCyc:EG11385-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP35340.
PROiP35340.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
3.50.50.60. 2 hits.
InterProiIPR012081. Alkyl_hydroperoxide_Rdtase_suF.
IPR023753. FAD/NAD-binding_dom.
IPR002109. Glutaredoxin.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF13192. Thioredoxin_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000238. AhpF. 1 hit.
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR03140. AhpF. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAHPF_ECOLI
AccessioniPrimary (citable) accession number: P35340
Secondary accession number(s): P77251, P77462
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.