UniProtKB - P06999 (PFKB_ECOLI)
Protein
ATP-dependent 6-phosphofructokinase isozyme 2
Gene
pfkB
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.1 Publication
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.
Catalytic activityi
- EC:2.7.1.112 Publications
Cofactori
Mg2+1 Publication
Activity 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
- KM=8 µM for ATP1 Publication
- KM=6 µM for fructose 6-phosphate1 Publication
: glycolysis Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.Proteins known to be involved in the 4 steps of the subpathway in this organism are:
- no protein annotated in this organism
- Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi)
- ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase isozyme 1 (pfkA), ATP-dependent 6-phosphofructokinase isozyme 2 (pfkB)
- Fructose-bisphosphate aldolase class 2 (fbaA), Fructose-bisphosphate aldolase (fbaA)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 27 | ATP 1; substrate ATP; shared with dimeric partnerCombined sources4 Publications | 1 | |
Binding sitei | 27 | ATP 2; allosteric inhibitor ATP; shared with dimeric partnerCombined sources1 Publication | 1 | |
Binding sitei | 139 | Substrate | 1 | |
Metal bindingi | 190 | Magnesium; catalyticCurated | 1 | |
Binding sitei | 248 | ATP 1; substrate ATPCombined sources4 Publications | 1 | |
Metal bindingi | 250 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 252 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Active sitei | 256 | By similarity | 1 | |
Binding sitei | 256 | Substrate | 1 | |
Binding sitei | 280 | ATP 1; via carbonyl oxygen; substrate ATPCombined sources4 Publications | 1 | |
Binding sitei | 284 | ATP 1; substrate ATPCombined sources4 Publications | 1 | |
Metal bindingi | 286 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 289 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 291 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 293 | Potassium; via carbonyl oxygen1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 185 – 187 | ATP 1; substrate ATPCombined sources4 Publications | 3 | |
Nucleotide bindingi | 224 – 229 | ATP 1; substrate ATPCombined sources4 Publications | 6 |
GO - Molecular functioni
- 6-phosphofructokinase activity Source: EcoCyc
- ATP binding Source: UniProtKB-KW
- identical protein binding Source: IntAct
- magnesium ion binding Source: EcoCyc
- phosphofructokinase activity Source: GO_Central
- tagatose-6-phosphate kinase activity Source: EcoCyc
GO - Biological processi
- cellular response to DNA damage stimulus Source: EcoliWiki
- glycolytic process Source: EcoCyc
Keywordsi
Molecular function | Kinase, Transferase |
Biological process | Glycolysis |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium |
Enzyme and pathway databases
BioCyci | EcoCyc:6PFK-2-MONOMER MetaCyc:6PFK-2-MONOMER |
BRENDAi | 2.7.1.11, 2026 |
SABIO-RKi | P06999 |
UniPathwayi | UPA00109;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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 190 | E → Q: Causes a 50-fold decrease in the kcat value and a 15-fold increment in the apparent KM for ATP. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000080083 | 1 – 309 | ATP-dependent 6-phosphofructokinase isozyme 2Add BLAST | 309 |
Proteomic databases
jPOSTi | P06999 |
PaxDbi | P06999 |
PRIDEi | P06999 |
2D gel databases
SWISS-2DPAGEi | P06999 |
Interactioni
Subunit structurei
Homodimer.
5 PublicationsBinary interactionsi
P06999
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-6966085,EBI-6966085 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4263076, 25 interactors |
DIPi | DIP-10465N |
MINTi | P06999 |
STRINGi | 511145.b1723 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P06999 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P06999 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 12 – 14 | Substrate binding | 3 | |
Regioni | 27 – 29 | Substrate binding | 3 | |
Regioni | 39 – 43 | Substrate binding | 5 | |
Regioni | 90 – 92 | Substrate binding | 3 | |
Regioni | 187 – 189 | ATP 2 binding; allosteric inhibitor ATPCombined sources1 Publication | 3 |
Sequence similaritiesi
Belongs to the carbohydrate kinase PfkB family.Curated
Phylogenomic databases
eggNOGi | COG1105, Bacteria |
HOGENOMi | CLU_050013_0_2_6 |
InParanoidi | P06999 |
PhylomeDBi | P06999 |
Family and domain databases
CDDi | cd01164, FruK_PfkB_like, 1 hit |
Gene3Di | 3.40.1190.20, 1 hit |
InterProi | View protein in InterPro IPR002173, Carboh/pur_kinase_PfkB_CS IPR011611, PfkB_dom IPR029056, Ribokinase-like IPR017583, Tagatose/fructose_Pkinase |
Pfami | View protein in Pfam PF00294, PfkB, 1 hit |
PIRSFi | PIRSF000535, 1PFK/6PFK/LacC, 1 hit |
SUPFAMi | SSF53613, SSF53613, 1 hit |
TIGRFAMsi | TIGR03168, 1-PFK, 1 hit |
PROSITEi | View protein in PROSITE PS00583, PFKB_KINASES_1, 1 hit PS00584, PFKB_KINASES_2, 1 hit |
i Sequence
Sequence statusi: Complete.
P06999-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 26 – 38 | GKLRC…VFEPG → ENCAVPHRCSNP in AAA24321 (PubMed:6235149).CuratedAdd BLAST | 13 | |
Sequence conflicti | 26 – 38 | GKLRC…VFEPG → ENCAVPHRCSNP in AAA24320 (PubMed:6310120).CuratedAdd BLAST | 13 | |
Sequence conflicti | 155 – 171 | AAQKQ…SSGEA → LRKNKGSAASSTVLGQG in AAA24321 (PubMed:6235149).CuratedAdd BLAST | 17 | |
Sequence conflicti | 245 – 246 | PV → AL in AAA24321 (PubMed:6235149).Curated | 2 | |
Sequence conflicti | 257 – 258 | SM → RL in AAA24321 (PubMed:6235149).Curated | 2 |
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 WP_000251727.1, NZ_SSZK01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC74793; AAC74793; b1723 BAA15500; BAA15500; BAA15500 |
GeneIDi | 57731119 946230 |
KEGGi | ecj:JW5280 eco:b1723 |
PATRICi | fig|1411691.4.peg.533 |
Similar proteinsi
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 WP_000251727.1, NZ_SSZK01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
SMRi | P06999 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263076, 25 interactors |
DIPi | DIP-10465N |
MINTi | P06999 |
STRINGi | 511145.b1723 |
2D gel databases
SWISS-2DPAGEi | P06999 |
Proteomic databases
jPOSTi | P06999 |
PaxDbi | P06999 |
PRIDEi | P06999 |
Genome annotation databases
EnsemblBacteriai | AAC74793; AAC74793; b1723 BAA15500; BAA15500; BAA15500 |
GeneIDi | 57731119 946230 |
KEGGi | ecj:JW5280 eco:b1723 |
PATRICi | fig|1411691.4.peg.533 |
Organism-specific databases
EchoBASEi | EB0694 |
Phylogenomic databases
eggNOGi | COG1105, Bacteria |
HOGENOMi | CLU_050013_0_2_6 |
InParanoidi | P06999 |
PhylomeDBi | P06999 |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00182 |
BioCyci | EcoCyc:6PFK-2-MONOMER MetaCyc:6PFK-2-MONOMER |
BRENDAi | 2.7.1.11, 2026 |
SABIO-RKi | P06999 |
Miscellaneous databases
EvolutionaryTracei | P06999 |
PROi | PR:P06999 |
Family and domain databases
CDDi | cd01164, FruK_PfkB_like, 1 hit |
Gene3Di | 3.40.1190.20, 1 hit |
InterProi | View protein in InterPro IPR002173, Carboh/pur_kinase_PfkB_CS IPR011611, PfkB_dom IPR029056, Ribokinase-like IPR017583, Tagatose/fructose_Pkinase |
Pfami | View protein in Pfam PF00294, PfkB, 1 hit |
PIRSFi | PIRSF000535, 1PFK/6PFK/LacC, 1 hit |
SUPFAMi | SSF53613, SSF53613, 1 hit |
TIGRFAMsi | TIGR03168, 1-PFK, 1 hit |
PROSITEi | View protein in PROSITE PS00583, PFKB_KINASES_1, 1 hit PS00584, PFKB_KINASES_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PFKB_ECOLI | |
Accessioni | P06999Primary (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: | April 7, 2021 | |
This is version 176 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families