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Information on EC 2.7.4.7 - phosphooxymethylpyrimidine kinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q08224

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Saccharomyces cerevisiae
UNIPROT: Q08224 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
thid2, phosphomethylpyrimidine kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-methyl-4-amino-5-hydroxymethylpyrimidine monophosphate kinase
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HMP-P kinase
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hydroxymethylpyrimidine phosphokinase
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kinase, phosphomethylpyrimidine (phosphorylating)
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phosphomethylpyrimidine kinase
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-
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Thi20p protein
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Thi21p protein
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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-
PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
37278-18-5
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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
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-
-
?
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
show the reaction diagram
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specific for ATP
product demonstrated in crude extract
?
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 SUBSTRATE
NATURAL 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-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
show the reaction diagram
-
specific for ATP
product demonstrated in crude extract
?
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
show the reaction diagram
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enzyme is required for thiamin biosynthesis
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-
?
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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-hydroxymercuribenzoate
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1 mM, complete inhibition
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lewin, L.M.; Brown, G.M.
The biosynthesis of thiamine. III. Mechanism of enzymatic formation of the pyrophosphate ester of 2-methyl-4-amino-5-hydroxymethylpyrimidine
J. Biol. Chem.
236
2768-2771
1961
Saccharomyces cerevisiae
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Manually annotated by BRENDA team
Haas, A.L.; Laun, N.P.; Begley, T.P.
Thi20, a remarkable enzyme from Saccharomyces cerevisiae with dual thiamin biosynthetic and degradation activities
Bioorg. Chem.
33
338-344
2005
Saccharomyces cerevisiae (Q08224)
Manually annotated by BRENDA team
Kawasaki, Y.; Onozuka, M.; Mizote, T.; Nosaka, K.
Biosynthesis of hydroxymethylpyrimidine pyrophosphate in Saccharomyces cerevisiae
Curr. Genet.
47
156-162
2005
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Onozuka, M.; Konno, H.; Kawasaki, Y.; Akaji, K.; Nosaka, K.
Involvement of thiaminase II encoded by the THI20 gene in thiamin salvage of Saccharomyces cerevisiae
FEMS Yeast Res.
8
266-275
2008
Saccharomyces cerevisiae (Q08224)
Manually annotated by BRENDA team
French, J.B.; Begley, T.P.; Ealick, S.E.
Structure of trifunctional THI20 from yeast
Acta Crystallogr. Sect. D
67
784-791
2011
Saccharomyces cerevisiae (Q08224)
Manually annotated by BRENDA team