Alkyl hydroperoxide reductase subunit F - Escherichia coli (strain K12)

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P35340 (AHPF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alkyl hydroperoxide reductase subunit F
EC=1.8.1.-

Alternative name(s):
Alkyl hydroperoxide reductase F52A protein

Gene names

Name:	ahpF
Ordered Locus Names:	b0606, JW0599

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Sequence caution	The sequence AAB40807.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD NADP
Molecular function	Oxidoreductase
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on NADH or NADPH Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
alsE	P32719	1	EBI-907438,EBI-1128770
tyrR	P07604	1	EBI-907438,EBI-559274

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 521

521

Alkyl hydroperoxide reductase subunit F

PRO_0000166774

Regions

Nucleotide binding

214 – 229

FAD By similarity

Nucleotide binding

357 – 371

NAD or NADP By similarity

Nucleotide binding

478 – 488

FAD By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.6

Modified residue

354

N6-acetyllysine Ref.6

Disulfide bond

345 ↔ 348

Redox-active By similarity

Secondary structure

521

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P35340 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: F39C50F922395B48
Show »

FASTA

521

56,177

        10         20         30         40         50         60 
MLDTNMKTQL KAYLEKLTKP VELIATLDDS AKSAEIKELL AEIAELSDKV TFKEDNSLPV 

        70         80         90        100        110        120 
RKPSFLITNP GSNQGPRFAG SPLGHEFTSL VLALLWTGGH PSKEAQSLLE QIRHIDGDFE 

       130        140        150        160        170        180 
FETYYSLSCH NCPDVVQALN LMSVLNPRIK HTAIDGGTFQ NEITDRNVMG VPAVFVNGKE 

       190        200        210        220        230        240 
FGQGRMTLTE IVAKIDTGAE KRAAEELNKR DAYDVLIVGS GPAGAAAAIY SARKGIRTGL 

       250        260        270        280        290        300 
MGERFGGQIL DTVDIENYIS VPKTEGQKLA GALKVHVDEY DVDVIDSQSA SKLIPAAVEG 

       310        320        330        340        350        360 
GLHQIETASG AVLKARSIIV ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG PLFKGKRVAV 

       370        380        390        400        410        420 
IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKL RSLKNVDIIL NAQTTEVKGD 

       430        440        450        460        470        480 
GSKVVGLEYR DRVSGDIHNI ELAGIFVQIG LLPNTNWLEG AVERNRMGEI IIDAKCETNV 

       490        500        510        520 
KGVFAAGDCT TVPYKQIIIA TGEGAKASLS AFDYLIRTKT A

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Locations of genes encoding alkyl hydroperoxide reductase on the physical map of the Escherichia coli K-12 genome." Smillie D.A., Hayward R.S., Suzuki T., Fujita N., Ishihama A. J. Bacteriol. 174:3826-3827(1992) [PubMed: 1592833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-162. Strain: K12.
[6]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-354, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

RefSeq

NP_415139.2. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FL2	X-ray	1.90	A	212-521	[»]

ProteinModelPortal

P35340.

SMR

P35340. Positions 1-521.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9077N.

IntAct

P35340. 23 interactions.

2D gel databases

SWISS-2DPAGE

P35340.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000106; EBESCP00000000106; EBESCG00000000083.
EBESCT00000000107; EBESCP00000000107; EBESCG00000000083.
EBESCT00000017235; EBESCP00000016526; EBESCG00000016294.

GeneID

947540.

GenomeReviews

Gene locus JW0599 in contig AP009048_GR.
Gene locus b0606 in contig U00096_GR.

KEGG

ecj:JW0599.
eco:b0606.

PATRIC

32116392. VBIEscCol129921_0636.

Organism-specific databases

EchoBASE

EB1358.

EcoGene

EG11385. ahpF.

Phylogenomic databases

eggNOG

COG3634.

GeneTree

EBGT00050000009144.

HOGENOM

HBG289531.

OMA

MMAAINP.

PhylomeDB

P35340.

ProtClustDB

PRK15317.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11385-MONOMER.
MetaCyc:EG11385-MONOMER.

Gene expression databases

Genevestigator

P35340.

Family and domain databases

InterPro

IPR012081. Alkyl_hydroperoxide_Rdtase_suF.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR002109. Glutaredoxin.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.

K03387.

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]

PIRSF

PIRSF000238. AhpF. 1 hit.

PRINTS

PR00368. FADPNR.
PR00469. PNDRDTASEII.

SUPFAM

SSF52833. Thiordxn-like_fd. 2 hits.

TIGRFAMs

TIGR03140. AhpF. 1 hit.

PROSITE

PS51354. GLUTAREDOXIN_2. 1 hit.
PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AHPF_ECOLI

Accession

Primary (citable) accession number: P35340
Secondary accession number(s): P77251, P77462

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents