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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi214 – 229FADBy similarityAdd BLAST16
Nucleotide bindingi357 – 371NAD or NADPBy similarityAdd BLAST15
Nucleotide bindingi478 – 488FADBy similarityAdd BLAST11

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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 databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001667741 – 521Alkyl hydroperoxide reductase subunit FAdd BLAST521

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53N6-acetyllysine1 Publication1
Disulfide bondi345 ↔ 348Redox-activeBy similarity
Modified residuei354N6-acetyllysine1 Publication1

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 interactors.
DIPiDIP-9077N.
IntActiP35340. 21 interactors.
STRINGi511145.b0606.

Structurei

Secondary structure

1521
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 15Combined sources12
Beta strandi21 – 26Combined sources6
Helixi31 – 44Combined sources14
Beta strandi50 – 54Combined sources5
Beta strandi58 – 60Combined sources3
Beta strandi62 – 68Combined sources7
Beta strandi77 – 80Combined sources4
Helixi84 – 86Combined sources3
Helixi87 – 97Combined sources11
Helixi106 – 113Combined sources8
Beta strandi119 – 125Combined sources7
Helixi132 – 145Combined sources14
Beta strandi149 – 155Combined sources7
Turni156 – 158Combined sources3
Helixi160 – 165Combined sources6
Beta strandi170 – 176Combined sources7
Beta strandi179 – 185Combined sources7
Helixi188 – 195Combined sources8
Helixi203 – 208Combined sources6
Beta strandi213 – 218Combined sources6
Helixi222 – 232Combined sources11
Turni233 – 235Combined sources3
Beta strandi238 – 241Combined sources4
Helixi247 – 251Combined sources5
Beta strandi261 – 265Combined sources5
Helixi266 – 278Combined sources13
Turni279 – 281Combined sources3
Beta strandi282 – 285Combined sources4
Beta strandi290 – 294Combined sources5
Beta strandi303 – 307Combined sources5
Beta strandi312 – 320Combined sources9
Beta strandi324 – 326Combined sources3
Turni332 – 337Combined sources6
Turni339 – 341Combined sources3
Beta strandi342 – 344Combined sources3
Helixi346 – 349Combined sources4
Helixi350 – 353Combined sources4
Beta strandi357 – 361Combined sources5
Helixi365 – 375Combined sources11
Beta strandi378 – 384Combined sources7
Beta strandi386 – 389Combined sources4
Helixi394 – 401Combined sources8
Beta strandi406 – 431Combined sources26
Turni432 – 434Combined sources3
Beta strandi437 – 441Combined sources5
Beta strandi443 – 447Combined sources5
Beta strandi451 – 454Combined sources4
Helixi456 – 458Combined sources3
Turni459 – 461Combined sources3
Beta strandi483 – 485Combined sources3
Helixi497 – 517Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

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: November 2, 2016
This is version 150 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.