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Information on EC 2.7.1.49 - hydroxymethylpyrimidine kinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q08224

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EC Tree
IUBMB Comments
CTP, UTP and GTP can act as donors.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q08224
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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
hmp kinase, hmppk, hmp-p kinase, tthmppk, hydroxymethylpyrimidine kinase, sthmppk, 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase, 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-amino-5-hydroxymethyl-2-methylpyrimidine kinase
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hydroxymethylpyrimidine kinase (phosphorylating)
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-
-
-
additional information
-
the enzyme is probably identical with EC 2.7.4.7, 4-amino-5-hydroxymethyl-2-methylpyrimidine monophosphate kinase, or HMP-P kinase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:4-amino-5-hydroxymethyl-2-methylpyrimidine 5-phosphotransferase
CTP, UTP and GTP can act as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-55-5
-
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-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine
show the reaction diagram
-
-
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
show the reaction diagram
ATP + 4-amino-5-hydroxy-2-methylpyrimidine
ADP + 4-amino-2-methyl-5-phosphopyrimidine
show the reaction diagram
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
show the reaction diagram
-
-
-
-
?
ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
show the reaction diagram
-
enzyme also performs the reaction of EC 2.7.4.7, phosphomethylpyrimidine kinase
-
-
?
CTP + 5-hydroxy-2-methylpyrimidine
CDP + 2-methyl-5-phosphopyrimidine
show the reaction diagram
-
-
-
?
GTP + 5-hydroxy-2-methylpyrimidine
GDP + 2-methyl-5-phosphopyrimidine
show the reaction diagram
-
-
-
?
UTP + 5-hydroxy-2-methylpyrimidine
UDP + 5-hydroxy-2-methylpyrimidine monophosphate
show the reaction diagram
-
-
-
?
additional information
?
-
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-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine
show the reaction diagram
-
-
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
show the reaction diagram
-
involved in thiamine biosynthetic pathway, first steps
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
show the reaction diagram
-
-
-
-
?
ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
show the reaction diagram
-
enzyme also performs the reaction of EC 2.7.4.7, phosphomethylpyrimidine kinase
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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at 20 mM MgCl2
additional information
-
no metal requirement
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
stable to treatment with p-hydroxymercuribenzoate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
thiamine synthesis from hydroxymethylpyrimidine activities in wild-type and mutant strains
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
-
x * 65000, recombinant His-tagged isozymes Thi20p or Thi21p, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 65000, recombinant His-tagged isozymes Thi20p or Thi21p, SDS-PAGE
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 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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
phosphomethylpyrimidine kinase activity, EC 2.7.4.7, is abolished in C-terminally truncated isozymes Thi20p and Thi21p, the mutant yeast strains sow no thiamin phosphate synthesis activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
stable to heating for 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
protected from inactivation by cysteine
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isozymes Thi20p or Thi21p from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
coexpression of and functional complementation by His-tagged soluble Thi20p or Thi21p isozymes with a thiamin synthetase in an Escherichia coli strain SN372L-3-9-10 deficient in thiamin biosynthesis
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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
-
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), Saccharomyces cerevisiae
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, Saccharomyces cerevisiae YPH500
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), Saccharomyces cerevisiae
Manually annotated by BRENDA team