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Literature summary for 2.7.1.167 extracted from

  • McArthur, F.; Andersson, C.E.; Loutet, S.; Mowbray, S.L.; Valvano, M.A.
    Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno-heptose biosynthesis (2005), J. Bacteriol., 187, 5292-5300.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D264E loss of activity Escherichia coli
D264N loss of enzymatic activity in the mutant protein is not caused by drastic alterations in protein structure Escherichia coli
E198D loss of enzymatic activity in the mutant protein is not caused by drastic alterations in protein structure Escherichia coli
N195D loss of activity Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
83000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P76658 bifunctional protein hldE includes: D-beta-D-heptose 7-phosphate kinase and D-beta-D-heptose 1-phosphate adenosyltransferase
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glycero-D-manno-heptose 7-phosphate + ATP
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Escherichia coli D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP
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?

Subunits

Subunits Comment Organism
dimer HldE comprises two functional domains: an N-terminal region with homology to the ribokinase superfamily (HldE1 domain) and a C-terminal region with homology to the cytidylyltransferase superfamily. HldE functional unit is a dimer and structural components present in each HldE1 monomer are required for enzymatic activity Escherichia coli

Synonyms

Synonyms Comment Organism
D-beta-D-heptose 7-phosphotransferase
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Escherichia coli
D-beta-D-heptose-7-phosphate kinase
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Escherichia coli
glycero-manno-heptose 7-phosphate kinase
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Escherichia coli
heptose 7-phosphate kinase
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Escherichia coli
HldE1 heptokinase
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Escherichia coli