Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06999

- PFKB_ECOLI

UniProt

P06999 - PFKB_ECOLI

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Magnesium.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

    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 – 74
    Beta strandi12 – 209
    Beta strandi24 – 296
    Beta strandi34 – 396
    Helixi40 – 5011
    Beta strandi55 – 617
    Helixi63 – 7513
    Beta strandi80 – 845
    Beta strandi93 – 975
    Turni98 – 1003
    Beta strandi103 – 1075
    Helixi115 – 12511
    Beta strandi133 – 1386
    Helixi146 – 15813
    Beta strandi162 – 1665
    Helixi169 – 1757
    Turni176 – 1783
    Beta strandi181 – 1844
    Helixi188 – 1958
    Helixi204 – 21411
    Beta strandi217 – 2193
    Beta strandi221 – 2244
    Helixi226 – 2283
    Beta strandi230 – 2334
    Beta strandi238 – 2414
    Helixi254 – 26714
    Helixi272 – 28615
    Helixi297 – 30711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MVRIYTLTLA PSLDSATITP QIYPEGKLRC TAPVFEPGGG GINVARAIAH    50
    LGGSATAIFP AGGATGEHLV SLLADENVPV ATVEAKDWTR QNLHVHVEAS 100
    GEQYRFVMPG AALNEDEFRQ LEEQVLEIES GAILVISGSL PPGVKLEKLT 150
    QLISAAQKQG IRCIVDSSGE ALSAALAIGN IELVKPNQKE LSALVNRELT 200
    QPDDVRKAAQ EIVNSGKAKR VVVSLGPQGA LGVDSENCIQ VVPPPVKSQS 250
    TVGAGDSMVG AMTLKLAENA SLEEMVRFGV AAGSAATLNQ GTRLCSHDDT 300
    QKIYAYLSR 309
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 131 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