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Information on EC 2.7.1.50 - hydroxyethylthiazole kinase and Organism(s) Bacillus subtilis and UniProt Accession P39593

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Bacillus subtilis
UNIPROT: P39593 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
hydroxyethylthiazole kinase, 4-methyl-5-beta-hydroxyethylthiazole kinase, thz kinase, 4-methyl-5-hydroxyethylthiazole kinase, thiazole kinase, grmzm2g094558, at3g24030, sathim, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-methyl-5-(beta-hydroxyethyl)thiazole kinase
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4-methyl-5-beta-hydroxyethylthiazole kinase
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4-methyl-5-beta-hydroxyethylthiazole kinase
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kinase, hydroxyethylthiazole (phosphorylating)
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TH kinase
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THZ kinase
additional information
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the enzyme belongs to the family of ribokinase-like carbohydrate kinases
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole
show the reaction diagram
SN2-like mechanism, with gamma-phosphate acting as an alcohol-activation base. Mg2+ ion 2, residues E126 and C198 play a major catalytic role, whereas Mg2+ ion 1 and C198 are responsible for product release
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole
show the reaction diagram
catalytic mechanism of phosphoryl transfer reaction and role of active site residues, e.g. R121 and C198, calculated on the basis of data on crystal structures of ribokinase-like kinases, transition state stabilization involves an oxyanion hole and a magnesium ion
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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-methyl-5-(2-hydroxyethyl)thiazole 2-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-56-6
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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-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
show the reaction diagram
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphoethyl)thiazole
show the reaction diagram
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additional information
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ATP-dependent phosphorylation of small molecules containing hydroxymethyl groups, reaction pathway mapping, molecular mechanism optimization and quantum mechanis calculations on the basis of enzyme crystal structure, PDB code 1C3Q and 1ESQ, overview
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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-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
show the reaction diagram
the enzyme is a salvage enzyme in the thiamin biosynthetic pathway and enables the cell to use recycled 4-methyl-5-beta-hydroxyethylthiazole as an alternative to its synthesis from 1-deoxy-D-xylulose-5-phosphate, cysteine, and tyrosine
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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stabilizes the transition state and the phosphoryl goup
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
modeling of stationary points along the reaction pathway, determination of relative energies of the transition state and product
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization by vapor diffusion equilibration, crystal structure at 1.5 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C198D
increase in catalytic activity, catalytic field predictions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Campobasso, N.; Mathews, II; Begley, T.P.; Ealick, S.E.
Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution
Biochemistry
39
7868-7877
2000
Bacillus subtilis (P39593), Bacillus subtilis
Manually annotated by BRENDA team
Dyguda, E.; Szefczyk, B.; Sokalski, W.A.
The mechanism of phosphoryl transfer reaction and the role of active site residues on the basis of ribokinase-like kinases
Int. J. Mol. Sci.
5
141-153
2004
Bacillus subtilis
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Manually annotated by BRENDA team
Dyguda-Kazimierowicz, E.; Sokalski, W.A.; Leszczynski, J.
Non-empirical study of the phosphorylation reaction catalyzed by 4-methyl-5-beta-hydroxyethylthiazole kinase: relevance of the theory of intermolecular interactions
J. Mol. Model.
13
839-849
2007
Bacillus subtilis (P39593)
Manually annotated by BRENDA team