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P0A796 (PFKA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase isozyme 1

Short name=ATP-PFK 1
Short name=Phosphofructokinase 1
EC=2.7.1.11
Alternative name(s):
6-phosphofructokinase isozyme I
Phosphohexokinase 1
Gene names
Name:pfkA
Ordered Locus Names:b3916, JW3887
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. HAMAP-Rule MF_00339

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339

Cofactor

Magnesium.

Enzyme regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate. HAMAP-Rule MF_00339

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00339.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320ATP-dependent 6-phosphofructokinase isozyme 1 HAMAP-Rule MF_00339
PRO_0000111950

Regions

Nucleotide binding73 – 742ATP HAMAP-Rule MF_00339
Nucleotide binding103 – 1064ATP HAMAP-Rule MF_00339
Region22 – 265Allosteric activator ADP binding; shared with dimeric partner HAMAP-Rule MF_00339
Region55 – 606Allosteric activator ADP binding; shared with dimeric partner HAMAP-Rule MF_00339
Region126 – 1283Substrate binding HAMAP-Rule MF_00339
Region170 – 1723Substrate binding HAMAP-Rule MF_00339
Region186 – 1883Allosteric activator ADP binding HAMAP-Rule MF_00339
Region214 – 2163Allosteric activator ADP binding HAMAP-Rule MF_00339
Region250 – 2534Substrate binding HAMAP-Rule MF_00339

Sites

Active site1281Proton acceptor Ref.2 Ref.8
Metal binding1041Magnesium; catalytic
Binding site121ATP; via amide nitrogen
Binding site1551Allosteric activator ADP
Binding site1631Substrate; shared with dimeric partner
Binding site2121Allosteric activator ADP By similarity
Binding site2231Substrate
Binding site2441Substrate; shared with dimeric partner

Experimental info

Mutagenesis1281D → S: 18000-fold reduction of catalytic rate. Ref.2
Mutagenesis1721R → S: 3.4-fold reduction in turnover numbers. Ref.2
Sequence conflict741F → C in CAA26356. Ref.1
Sequence conflict103 – 1042GD → DG in CAA26356. Ref.1
Sequence conflict1631R → P in CAA26356. Ref.1
Sequence conflict317 – 3193KKL → EKM in CAA26356. Ref.1

Secondary structure

.................................................. 320
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A796 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: D03D79F6A5536A41

FASTA32034,842
        10         20         30         40         50         60 
MIKKIGVLTS GGDAPGMNAA IRGVVRSALT EGLEVMGIYD GYLGLYEDRM VQLDRYSVSD 

        70         80         90        100        110        120 
MINRGGTFLG SARFPEFRDE NIRAVAIENL KKRGIDALVV IGGDGSYMGA MRLTEMGFPC 

       130        140        150        160        170        180 
IGLPGTIDND IKGTDYTIGF FTALSTVVEA IDRLRDTSSS HQRISVVEVM GRYCGDLTLA 

       190        200        210        220        230        240 
AAIAGGCEFV VVPEVEFSRE DLVNEIKAGI AKGKKHAIVA ITEHMCDVDE LAHFIEKETG 

       250        260        270        280        290        300 
RETRATVLGH IQRGGSPVPY DRILASRMGA YAIDLLLAGY GGRCVGIQNE QLVHHDIIDA 

       310        320 
IENMKRPFKG DWLDCAKKLY 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase."
Hellinga H.W., Evans P.R.
Eur. J. Biochem. 149:363-373(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Mutations in the active site of Escherichia coli phosphofructokinase."
Hellinga H.W., Evans P.R.
Nature 327:437-439(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION, ACTIVE SITE, MUTAGENESIS OF ASP-128 AND ARG-172.
[3]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"A role of RnlA in the RNase LS activity from Escherichia coli."
Otsuka Y., Koga M., Iwamoto A., Yonesaki T.
Genes Genet. Syst. 82:291-299(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-8.
Strain: K12.
[7]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[8]"Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products."
Shirakihara Y., Evans P.R.
J. Mol. Biol. 204:973-994(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; ADP; FRUCTOSE 1,6-BISPHOSPHATE AND ALLOSTERIC ACTIVATOR, ACTIVE SITE.
[9]"Crystal structure of unliganded phosphofructokinase from Escherichia coli."
Rypniewski W.R., Evans P.R.
J. Mol. Biol. 207:805-821(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02519 Genomic DNA. Translation: CAA26356.1.
L19201 Genomic DNA. Translation: AAB03048.1.
U00096 Genomic DNA. Translation: AAC76898.1.
AP009048 Genomic DNA. Translation: BAE77394.1.
PIRKIECFA. G65197.
RefSeqNP_418351.1. NC_000913.3.
YP_491535.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PFKX-ray2.40A/B1-320[»]
2PFKX-ray2.40A/B/C/D1-320[»]
ProteinModelPortalP0A796.
SMRP0A796. Positions 1-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35841N.
IntActP0A796. 7 interactions.
MINTMINT-1322275.
STRING511145.b3916.

2D gel databases

SWISS-2DPAGEP0A796.

Proteomic databases

PaxDbP0A796.
PRIDEP0A796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76898; AAC76898; b3916.
BAE77394; BAE77394; BAE77394.
GeneID12932230.
948412.
KEGGecj:Y75_p3271.
eco:b3916.
PATRIC32123343. VBIEscCol129921_4032.

Organism-specific databases

EchoBASEEB0693.
EcoGeneEG10699. pfkA.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAGFGGRCV.
OrthoDBEOG644ZRM.
PhylomeDBP0A796.

Enzyme and pathway databases

BioCycEcoCyc:6PFK-1-MONOMER.
ECOL316407:JW3887-MONOMER.
MetaCyc:6PFK-1-MONOMER.
SABIO-RKP0A796.
UniPathwayUPA00109; UER00182.

Gene expression databases

GenevestigatorP0A796.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase_I_B1.
InterProIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 1 hit.
TIGRFAMsTIGR02482. PFKA_ATP. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A796.
PROP0A796.

Entry information

Entry namePFKA_ECOLI
AccessionPrimary (citable) accession number: P0A796
Secondary accession number(s): P06998, Q2M8L2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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