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P06999

- PFKB_ECOLI

UniProt

P06999 - PFKB_ECOLI

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Protein

ATP-dependent 6-phosphofructokinase isozyme 2

Gene

pfkB

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

Functioni

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

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.2 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

Allosterically inhibited by ATP. Allosteric ATP-binding requires the presence of the substrate ATP. Inhibited by monovalent cations with ionic radii larger than Na+ (e.g. K+, Cs+). The monovalent cations increase the affinity of the allosteric site for ATP. PFK-2 is sensitive to inhibition by fructose 1,6-diphosphate.2 Publications

Kineticsi

  1. KM=8 µM for ATP1 Publication
  2. KM=6 µM for fructose 6-phosphate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271Allosteric inhibitor ATP; shared with dimeric partner1 Publication
Binding sitei27 – 271ATP; shared with dimeric partner3 Publications
Binding sitei139 – 1391Substrate
Metal bindingi190 – 1901Magnesium; catalyticCurated
Binding sitei248 – 2481ATP3 Publications
Metal bindingi250 – 2501Potassium; via carbonyl oxygen1 Publication
Metal bindingi252 – 2521Potassium; via carbonyl oxygen1 Publication
Active sitei256 – 2561By similarity
Binding sitei256 – 2561Substrate
Binding sitei280 – 2801ATP; via carbonyl oxygen3 Publications
Binding sitei284 – 2841ATP3 Publications
Metal bindingi286 – 2861Potassium; via carbonyl oxygen1 Publication
Metal bindingi289 – 2891Potassium; via carbonyl oxygen1 Publication
Metal bindingi291 – 2911Potassium; via carbonyl oxygen1 Publication
Metal bindingi293 – 2931Potassium; via carbonyl oxygen1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1873ATP3 Publications
Nucleotide bindingi224 – 2296ATP3 Publications

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: EcoCyc
  2. ATP binding Source: UniProtKB-KW
  3. identical protein binding Source: IntAct
  4. magnesium ion binding Source: EcoCyc
  5. tagatose-6-phosphate kinase activity Source: EcoCyc

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. cellular response to DNA damage stimulus Source: EcoliWiki
  3. glycolytic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:6PFK-2-MONOMER.
ECOL316407:JW5280-MONOMER.
MetaCyc:6PFK-2-MONOMER.
SABIO-RKP06999.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase isozyme 2 (EC:2.7.1.11)
Short name:
ATP-PFK 2
Short name:
Phosphofructokinase 2
Alternative name(s):
6-phosphofructokinase isozyme II
Phosphohexokinase 2
Gene namesi
Name:pfkB
Ordered Locus Names:b1723, JW5280
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10700. pfkB.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi190 – 1901E → Q: Causes a 50-fold decrease in the kcat value and a 15-fold increment in the apparent KM for ATP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309ATP-dependent 6-phosphofructokinase isozyme 2PRO_0000080083Add
BLAST

Proteomic databases

PaxDbiP06999.
PRIDEiP06999.

2D gel databases

SWISS-2DPAGEP06999.

Expressioni

Gene expression databases

GenevestigatoriP06999.

Interactioni

Subunit structurei

Homodimer.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-6966085,EBI-6966085

Protein-protein interaction databases

DIPiDIP-10465N.
MINTiMINT-8178151.
STRINGi511145.b1723.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi12 – 209Combined sources
Beta strandi24 – 296Combined sources
Beta strandi34 – 396Combined sources
Helixi40 – 5011Combined sources
Beta strandi55 – 617Combined sources
Helixi63 – 7513Combined sources
Beta strandi80 – 845Combined sources
Beta strandi93 – 975Combined sources
Turni98 – 1003Combined sources
Beta strandi103 – 1075Combined sources
Helixi115 – 12511Combined sources
Beta strandi133 – 1386Combined sources
Helixi146 – 15813Combined sources
Beta strandi162 – 1665Combined sources
Helixi169 – 1757Combined sources
Turni176 – 1783Combined sources
Beta strandi181 – 1844Combined sources
Helixi188 – 1958Combined sources
Helixi204 – 21411Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi221 – 2244Combined sources
Helixi226 – 2283Combined sources
Beta strandi230 – 2334Combined sources
Beta strandi238 – 2414Combined sources
Helixi254 – 26714Combined sources
Helixi272 – 28615Combined sources
Helixi297 – 30711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQDX-ray1.98A/B1-309[»]
3N1CX-ray2.00A/B/C/D1-309[»]
3UMOX-ray1.70A/B1-309[»]
3UMPX-ray1.85A/B1-309[»]
3UQDX-ray2.14A/B/C/D1-309[»]
3UQEX-ray2.20A/B1-309[»]
ProteinModelPortaliP06999.
SMRiP06999. Positions 1-309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06999.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 143Substrate binding
Regioni27 – 293Substrate binding
Regioni39 – 435Substrate binding
Regioni90 – 923Substrate binding
Regioni187 – 1893Allosteric inhibitor ATP binding

Sequence similaritiesi

Belongs to the carbohydrate kinase PfkB family.Curated

Phylogenomic databases

eggNOGiCOG1105.
HOGENOMiHOG000265281.
InParanoidiP06999.
KOiK16370.
OMAiNVARTIH.
OrthoDBiEOG61KBKF.
PhylomeDBiP06999.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
InterProiIPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011611. PfkB_dom.
IPR029056. Ribokinase-like.
IPR017583. Tagatose/fructose_Pkinase.
[Graphical view]
PfamiPF00294. PfkB. 1 hit.
[Graphical view]
PIRSFiPIRSF000535. 1PFK/6PFK/LacC. 1 hit.
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR03168. 1-PFK. 1 hit.
PROSITEiPS00583. PFKB_KINASES_1. 1 hit.
PS00584. PFKB_KINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06999-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVRIYTLTLA PSLDSATITP QIYPEGKLRC TAPVFEPGGG GINVARAIAH
60 70 80 90 100
LGGSATAIFP AGGATGEHLV SLLADENVPV ATVEAKDWTR QNLHVHVEAS
110 120 130 140 150
GEQYRFVMPG AALNEDEFRQ LEEQVLEIES GAILVISGSL PPGVKLEKLT
160 170 180 190 200
QLISAAQKQG IRCIVDSSGE ALSAALAIGN IELVKPNQKE LSALVNRELT
210 220 230 240 250
QPDDVRKAAQ EIVNSGKAKR VVVSLGPQGA LGVDSENCIQ VVPPPVKSQS
260 270 280 290 300
TVGAGDSMVG AMTLKLAENA SLEEMVRFGV AAGSAATLNQ GTRLCSHDDT

QKIYAYLSR
Length:309
Mass (Da):32,456
Last modified:November 1, 1997 - v2
Checksum:iA93BEBE0D5801309
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 3813GKLRC…VFEPG → ENCAVPHRCSNP in AAA24321. (PubMed:6235149)CuratedAdd
BLAST
Sequence conflicti26 – 3813GKLRC…VFEPG → ENCAVPHRCSNP in AAA24320. (PubMed:6310120)CuratedAdd
BLAST
Sequence conflicti155 – 17117AAQKQ…SSGEA → LRKNKGSAASSTVLGQG in AAA24321. (PubMed:6235149)CuratedAdd
BLAST
Sequence conflicti245 – 2462PV → AL in AAA24321. (PubMed:6235149)Curated
Sequence conflicti257 – 2582SM → RL in AAA24321. (PubMed:6235149)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02500 Genomic DNA. Translation: AAA24321.1.
U00096 Genomic DNA. Translation: AAC74793.1.
AP009048 Genomic DNA. Translation: BAA15500.2.
K00128 Genomic DNA. Translation: AAA24320.1.
PIRiC64931. KIECFB.
RefSeqiNP_416237.3. NC_000913.3.
YP_489984.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74793; AAC74793; b1723.
BAA15500; BAA15500; BAA15500.
GeneIDi12934082.
946230.
KEGGiecj:Y75_p1698.
eco:b1723.
PATRICi32118753. VBIEscCol129921_1794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02500 Genomic DNA. Translation: AAA24321.1 .
U00096 Genomic DNA. Translation: AAC74793.1 .
AP009048 Genomic DNA. Translation: BAA15500.2 .
K00128 Genomic DNA. Translation: AAA24320.1 .
PIRi C64931. KIECFB.
RefSeqi NP_416237.3. NC_000913.3.
YP_489984.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CQD X-ray 1.98 A/B 1-309 [» ]
3N1C X-ray 2.00 A/B/C/D 1-309 [» ]
3UMO X-ray 1.70 A/B 1-309 [» ]
3UMP X-ray 1.85 A/B 1-309 [» ]
3UQD X-ray 2.14 A/B/C/D 1-309 [» ]
3UQE X-ray 2.20 A/B 1-309 [» ]
ProteinModelPortali P06999.
SMRi P06999. Positions 1-309.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10465N.
MINTi MINT-8178151.
STRINGi 511145.b1723.

2D gel databases

SWISS-2DPAGE P06999.

Proteomic databases

PaxDbi P06999.
PRIDEi P06999.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74793 ; AAC74793 ; b1723 .
BAA15500 ; BAA15500 ; BAA15500 .
GeneIDi 12934082.
946230.
KEGGi ecj:Y75_p1698.
eco:b1723.
PATRICi 32118753. VBIEscCol129921_1794.

Organism-specific databases

EchoBASEi EB0694.
EcoGenei EG10700. pfkB.

Phylogenomic databases

eggNOGi COG1105.
HOGENOMi HOG000265281.
InParanoidi P06999.
KOi K16370.
OMAi NVARTIH.
OrthoDBi EOG61KBKF.
PhylomeDBi P06999.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
BioCyci EcoCyc:6PFK-2-MONOMER.
ECOL316407:JW5280-MONOMER.
MetaCyc:6PFK-2-MONOMER.
SABIO-RK P06999.

Miscellaneous databases

EvolutionaryTracei P06999.
PROi P06999.

Gene expression databases

Genevestigatori P06999.

Family and domain databases

Gene3Di 3.40.1190.20. 1 hit.
InterProi IPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011611. PfkB_dom.
IPR029056. Ribokinase-like.
IPR017583. Tagatose/fructose_Pkinase.
[Graphical view ]
Pfami PF00294. PfkB. 1 hit.
[Graphical view ]
PIRSFi PIRSF000535. 1PFK/6PFK/LacC. 1 hit.
SUPFAMi SSF53613. SSF53613. 1 hit.
TIGRFAMsi TIGR03168. 1-PFK. 1 hit.
PROSITEi PS00583. PFKB_KINASES_1. 1 hit.
PS00584. PFKB_KINASES_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of gene pfkB encoding the minor phosphofructokinase of Escherichia coli K-12."
    Daldal F.
    Gene 28:337-342(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Molecular cloning of the gene for phosphofructokinase-2 of Escherichia coli and the nature of a mutation, pfkB1, causing a high level of the enzyme."
    Daldal F.
    J. Mol. Biol. 168:285-305(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
  6. "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.
  7. "Evidence for a catalytic Mg2+ ion and effect of phosphate on the activity of Escherichia coli phosphofructokinase-2: regulatory properties of a ribokinase family member."
    Parducci R.E., Cabrera R., Baez M., Guixe V.
    Biochemistry 45:9291-9299(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF GLU-190, ENZYME REGULATION.
  8. "Crystallographic structure of phosphofructokinase-2 from Escherichia coli in complex with two ATP molecules. Implications for substrate inhibition."
    Cabrera R., Ambrosio A.L., Garratt R.C., Guixe V., Babul J.
    J. Mol. Biol. 383:588-602(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ATP AND ALLOSTERIC INHIBITOR ATP.
  9. "The crystal complex of phosphofructokinase-2 of Escherichia coli with fructose-6-phosphate: kinetic and structural analysis of the allosteric ATP inhibition."
    Cabrera R., Baez M., Pereira H.M., Caniuguir A., Garratt R.C., Babul J.
    J. Biol. Chem. 286:5774-5783(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE.
  10. "Structure of E. coli PFK2 in complex with substrates and products."
    Pereira H.M., Caniuguir A., Baez M., Cabrera R., Garratt R.C., Babul J.
    Submitted (NOV-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) IN COMPLEX WITH ADP; ATP; FRUCTOSE-1-6-DIPHOSPHATE AND FRUCTOSE-6-PHOSPHATE.
  11. "Structure of E. coli PFK2 mutant Y23D."
    Pereira H.M., Caniuguir A., Baez M., Cabrera R., Garratt R.C., Babul J.
    Submitted (NOV-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP AND DIPHOSPHATE.
  12. "A ribokinase family conserved monovalent cation binding site enhances the MgATP-induced inhibition in E. coli phosphofructokinase-2."
    Baez M., Cabrera R., Pereira H.M., Blanco A., Villalobos P., Ramirez-Sarmiento C.A., Caniuguir A., Guixe V., Garratt R.C., Babul J.
    Biophys. J. 105:185-193(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ATP AND POTASSIUM, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

Entry informationi

Entry nameiPFKB_ECOLI
AccessioniPrimary (citable) accession number: P06999
Secondary accession number(s): P78065, P78260
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Only 10% of the activity present in the wild-type strain is phosphofructokinase-2.
This enzyme is not to be confused with 6-phosphofructo-2-kinase which is also called phosphofructokinase 2.
E.coli has two 6-phosphofructokinases enzymes.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3