Information on EC 2.7.4.7 - phosphomethylpyrimidine kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.7.4.7
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RECOMMENDED NAME
GeneOntology No.
phosphomethylpyrimidine kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + (4-amino-2-methylpyrimidin-5-yl)methyl phosphate = ADP + (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-amino-2-methyl-5-diphosphomethylpyrimidine biosynthesis
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4-amino-2-methyl-5-diphosphomethylpyrimidine biosynthesis (yeast)
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hydroxymethylpyrimidine salvage
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Metabolic pathways
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thiamine formation from pyrithiamine and oxythiamine (yeast)
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Thiamine metabolism
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thiamine salvage IV (yeast)
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vitamin B1 metabolism
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SYSTEMATIC NAME
IUBMB Comments
ATP:(4-amino-2-methylpyrimidin-5-yl)methyl-phosphate phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
37278-18-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
bifunctional hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (4-amino-2-methylpyrimidin-5-yl)methyl phosphate
ADP + (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate
show the reaction diagram
-
-
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
show the reaction diagram
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
show the reaction diagram
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
show the reaction diagram
additional information
?
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Thi20p is involved in thiamine synthesis from pyrithiamin and oxythiamin
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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 + (4-amino-2-methylpyrimidin-5-yl)methyl phosphate
ADP + (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate
show the reaction diagram
Q08224
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-
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
show the reaction diagram
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involved in thiamine biosynthesis
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ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
show the reaction diagram
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required for activity
Mn2+
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may substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(6R)-6-[(2E)-4-oxo-6-phenylhex-2-en-1-yl]-5,6-dihydro-2H-pyran-2-one
lactone isolated from Cryptocarya rugulosa, covalent inhibition
(6R)-6-[(2E)-6-(4-ethynylphenyl)-4-oxohex-2-en-1-yl]-5,6-dihydro-2H-pyran-2-one
derivative of a lactone isolated from Cryptocarya rugulosa, covalent inhibition
(6S)-6-[(2E)-6-(4-ethynylphenyl)-4-oxohex-2-en-1-yl]tetrahydro-2H-pyran-2-one
derivative of a lactone isolated from Cryptocarya rugulosa, covalent inhibition
p-hydroxymercuribenzoate
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1 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
2-methyl-4-amino-5-hydroxymethylpyrimidine
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pH 8.0, 25C, recombinant ThiD
0.023
2-methyl-4-amino-5-hydroxymethylpyrimidine phosphate
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pH 8.0, 25C, recombinant ThiD
0.193
ATP
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pH 8.0, 25C, recombinant ThiD
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0867
2-methyl-4-amino-5-hydroxymethylpyrimidine
Escherichia coli
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pH 8.0, 25C, recombinant ThiD
0.07
2-methyl-4-amino-5-hydroxymethylpyrimidine phosphate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
(6R)-6-[(2E)-4-oxo-6-phenylhex-2-en-1-yl]-5,6-dihydro-2H-pyran-2-one
Staphylococcus aureus
P66915
pH not specified in the publication, temperature not specified in the publication
0.014
(6R)-6-[(2E)-6-(4-ethynylphenyl)-4-oxohex-2-en-1-yl]-5,6-dihydro-2H-pyran-2-one
Staphylococcus aureus
P66915
pH not specified in the publication, temperature not specified in the publication
0.032
(6S)-6-[(2E)-6-(4-ethynylphenyl)-4-oxohex-2-en-1-yl]tetrahydro-2H-pyran-2-one
Staphylococcus aureus
P66915
pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
putative plastid target signal in BTH1 suggests plastidic localization
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Peptoclostridium difficile (strain 630)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 31232, deduced from nucleotide sequence; 4 * 33000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.7 A resolution. Enzyme is composed of a ThiD-like N-terminal domain that catalyzes the phosphorylation of 4-amino-5-hydroxymethyl-2-methylpyrimidine and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate and a TenA-like C-terminal domain with thiaminase activity. The structure reveals an overall dimeric organization in which N-terminal domains and C-terminal domains form ThiD-like and TenA-like local dimers. A relatively flexible linker region composed of a loop and a short helix joins the two domains. This linker region and a flexible N-terminal extension occupy the interface between the ThiD-like and TenA-like dimers. The N-terminal extension is composed of a single beta-strand that packs against and extends the length of the internal beta-sheet of the ThiD-like domain and a short alpha-helix
hanging drop vapor diffusion, 6 mg/ml HMPP kinase, hanging drops contain 0.002 mL protein solution and 0.002 ml reservoir solution, crystal without HMP are obtained using a reservoir solution containing 1.35 M MgSO4, 150 mM MES, pH 7.0, crystals with HMP are obtained with 1.4 M MgSO4 and 150 M MES, crystals of native HMP-P kinase diffract to 2.3 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
his-tagged recombinant ThiD
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of BTH1 cDNA in Escherichia coli
expression in Escherichia coli
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overexpression in Escherichia coli
overexpression of ThiD in Escherichia coli
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