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InterPro: IPR002173 Carbohydrate/puine kinase, PfkB, conserved site

Protein matchesHelp
UniProtKB
Matches:
6412 proteins
AccessionHelp IPR002173 Carboh/pur_kinase_PfkB_CS
TypeHelp Conserved_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR001805 Adenosine kinase
IPR005926 Tagatose-6-phosphate kinase
IPR011611 Carbohydrate/purine kinase
IPR011877 Ribokinase, bacterial
IPR011913 RfaE bifunctional protein, domain I
IPR017583 1-phosphofructokinase
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

It has been shown [1, 2, 3] that the following carbohydrate and purine kinases are evolutionary related and can be grouped into a single family, which is known [1] as the 'pfkB family':

  • Fructokinase (EC:2.7.1.4) (gene scrK).
  • 6-phosphofructokinase isozyme 2 (EC:2.7.1.11) (phosphofructokinase-2) (gene pfkB). pfkB is a minor phosphofructokinase isozyme in Escherichia coli and is not evolutionary related to the major isozyme (gene pfkA). Plant 6-phosphofructokinase also belong to this family.
  • Ribokinase (EC:2.7.1.15) (gene rbsK).
  • Adenosine kinase (EC:2.7.1.20) (gene ADK).
  • 2-dehydro-3-deoxygluconokinase (EC:2.7.1.45) (gene: kdgK).
  • 1-phosphofructokinase (EC:2.7.1.56) (fructose 1-phosphate kinase) (gene fruK).
  • Inosine-guanosine kinase (EC:2.7.1.73) (gene gsk).
  • Tagatose-6-phosphate kinase (EC:2.7.1.144) (phosphotagatokinase) (gene lacC).
  • E. coli hypothetical protein yeiC.
  • E. coli hypothetical protein yeiI.
  • E. coli hypothetical protein yhfQ.
  • E. coli hypothetical protein yihV.
  • Yeast hypothetical protein YJR105w.

All the above kinases are proteins of from 280 to 430 amino acid residues that share a few region of sequence similarity.

  • Note: some bacterial fructokinases belong to the ROK family (see IPR000600).
  • Structural linksHelp
    SCOP: c.72.1.1
    CATH: 3.40.1190.20
    Database linksHelp
    PDBe-motif: PS00583 , PS00584
    Enzyme: EC:2.7.1
    PROSITE doc: PDOC00504
    Blocks: IPB002173

    Taxonomic coverageHelp

    Overlapping InterPro entriesHelp
    IPR002173 Numbers of overlapping proteins Average numbers of overlapping amino acids

    Example proteinsHelp
    A2WXV8 Fructokinase-1

    O82616 Putative fructokinase-5

    P25332 Probable ribokinase

    P55263 Adenosine kinase

    P55264 Adenosine kinase

    More proteins


    Example Proteins Key


    InterPro entry accession number/name and structure databases Colour code
    IPR002173 Carbohydrate/puine kinase, PfkB, conserved site
    IPR011611 Carbohydrate/purine kinase
    IPR002139 Ribokinase
    IPR001805 Adenosine kinase
    SWISS-MODEL
    PDB Chain
    ModBase
    SCOP Domain
    CATH Domain

    PublicationsHelp
    1. Wu LF, Reizer A, Reizer J, Cai B, Tomich JM, Saier MH Jr.
    Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: evidence for a kinase superfamily including both phosphofructokinases of Escherichia coli.
    J. Bacteriol. 173 3117-27 1991 [PubMed: 1850730]
    http://jb.asm.org/cgi/content/abstract/173/10/3117
    2. Orchard LM, Kornberg HL.
    Sequence similarities between the gene specifying 1-phosphofructokinase (fruK), genes specifying other kinases in Escherichia coli K12, and lacC of Staphylococcus aureus.
    Proc. Biol. Sci. 242 87-90 1990 [PubMed: 1981619]
    http://www.journals.royalsoc.ac.uk/openurl.asp?genre=article&issn=0962-8452&volume=242&issue=1304&spage=87
    3. Blatch GL, Scholle RR, Woods DR.
    Nucleotide sequence and analysis of the Vibrio alginolyticus sucrose uptake-encoding region.
    Gene 95 17-23 1990 [PubMed: 2174811]
    http://dx.doi.org/10.1016/0378-1119(90)90408-J

    Additional ReadingHelp
    Zhang Y, El Kouni MH, Ealick SE.
    Structure of Toxoplasma gondii adenosine kinase in complex with an ATP analog at 1.1 angstroms resolution.
    Acta Crystallogr. D Biol. Crystallogr. 62 2006 140-5 [PubMed: 16421444]
    http://dx.doi.org/10.1107/S090744490503430X
    Inagaki E, Ukita Y, Kumei M, Kajihara Y, Tahirov TH.
    Crystallization and preliminary crystallographic analysis of 2-keto-3-deoxygluconate kinase from Thermus thermophilus.
    Acta Crystallogr. D Biol. Crystallogr. 60 2004 761-3 [PubMed: 15039578]
    http://dx.doi.org/10.1107/S0907444904002665
    Muchmore SW, Smith RA, Stewart AO, Cowart MD, Gomtsyan A, Matulenko MA, Yu H, Severin JM, Bhagwat SS, Lee CH, Kowaluk EA, Jarvis MF, Jakob CL.
    Crystal structures of human adenosine kinase inhibitor complexes reveal two distinct binding modes.
    J. Med. Chem. 49 2006 6726-31 [PubMed: 17154503]
    http://dx.doi.org/10.1021/jm060189a
    Zhang Y, El Kouni MH, Ealick SE.
    Substrate analogs induce an intermediate conformational change in Toxoplasma gondii adenosine kinase.
    Acta Crystallogr. D Biol. Crystallogr. 63 2007 126-34 [PubMed: 17242506]
    http://dx.doi.org/10.1107/S0907444906043654
    Ohshima N, Inagaki E, Yasuike K, Takio K, Tahirov TH.
    Structure of Thermus thermophilus 2-Keto-3-deoxygluconate kinase: evidence for recognition of an open chain substrate.
    J. Mol. Biol. 340 2004 477-89 [PubMed: 15210349]
    http://dx.doi.org/10.1016/j.jmb.2004.04.074
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    InterPro 23.1