Information on EC 2.7.1.89 - thiamine kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.89
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RECOMMENDED NAME
GeneOntology No.
thiamine kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + thiamine = ADP + thiamine phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Thiamine metabolism
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thiamine salvage I
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vitamin B1 metabolism
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SYSTEMATIC NAME
IUBMB Comments
ATP:thiamine phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
62213-38-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
K12
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
a thiK deletion strain (DELTAthiK) reveals decreased thiamine sensitivity, since this enzyme is required for the phosphorylation of thiamine to thiamine diphosphate. Deleting the thiamine kinase ThiK abolishes thiamine and triazolethiamine-dependent inhibition of reporter gene expression. The reporter gene expression in the thiK deletion strain is dramatically decreased in the presence of pyrithiamine
metabolism
thiamine is synthesized from two precursors, hydroxymethylpyrimidine diphosphate and hydroxyethylthiazole phosphate, which are produced independently and finally joined to form thiamine phosphate
physiological function
riboswitches are conserved regions within mRNA molecules that bind specific metabolites and regulate gene expression. TPP-riboswitches, which respond to thiamine diophosphate, are involved in the regulation of thiamine metabolism. Thiamine analogues containing a central 1,2,3-triazole group induce repression of thiM-riboswitch dependent gene expression in different Escherichiac coli strains. Triazolethiamine shows concentration-dependent reporter gene repression that is dependent on the presence of thiamine kinase ThiK, whereas the effect of pyrithiamine, a known TPP-riboswitch modulator, is ThiK-independent, overview. ThiK dependency is bypassed by triazolethiamine-derivatives that bear phosphate mimicking and metal-ion chelating moieties
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + adenosylcobinamide
ADP + adenosylcobinamide monophosphate
show the reaction diagram
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?
ATP + thiamine
ADP + thiamine monophosphate
show the reaction diagram
ATP + thiamine
ADP + thiamine phosphate
show the reaction diagram
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?
additional information
?
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triazolethiamine is likely to be recognized and phosphorylated by endogenous bacterial enzymes, such as ThiK
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + thiamine
ADP + thiamine monophosphate
show the reaction diagram
ATP + thiamine
ADP + thiamine phosphate
show the reaction diagram
P75948
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?
additional information
?
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P75948
triazolethiamine is likely to be recognized and phosphorylated by endogenous bacterial enzymes, such as ThiK
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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marked stimulation
Mg2+
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absolute requirement
NH4+
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marked stimulation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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dependent on the presence of
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028
thiamine
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at 37°C, pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
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SDS-PAGE, His-tagged enzyme
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
construction of a thiK deletion mutant strain, phenotype
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