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Information on EC 2.7.1.50 - hydroxyethylthiazole kinase and Organism(s) Pyrococcus horikoshii and UniProt Accession O58877

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Pyrococcus horikoshii
UNIPROT: O58877 not found.
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The taxonomic range for the selected organisms is: Pyrococcus horikoshii
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
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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
additional information
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the active site is located at the interface between adjacent subunits. Each active site contains a thiazole-binding site and a nucleotide-binding site, structure, overview. Asp residue as a catalytic base
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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three-quarters of the residues involved in interfacial regions are conserved, also the amino-acid residues in the nucleotide-binding, magnesium ion-binding and substrate-binding sites are conserved. The overall structure of PhThiK is similar to those of Bacillus subtilis ThiK (BsThiK) and Enterococcus faecalis V583 ThiK (EfThiK)
additional information
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the enzyme topology shows the typical ribokinase fold of an alpha/beta protein. Binding of the nucleotide and substrate to the ThiK enzyme do not influence the trimeric quaternary association
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
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residues involved in hydrogen bonds between subunits in the enzyme trimer, overview
additional information
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monomer structure, docking of ternary complexes, tertiary structure, molecular modelling, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme with a phosphate ion occupying the position of the beta-phosphate of the nucleotide, mixing of 0.001 ml of protein solution containing 1.95 mg/ml protein in 20 mM Tris-HCl containing 200 mM NaCl and 1 mM DTT, pH 8.0, with 0.001 ml of reservoir solution containing 0.1 M CHESS buffer, pH 9.3, and 0.88 M sodium citrate as the precipitant, 20°C, 1 week, 25% v/v glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 1.85 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by gel filtration, anion exchange chromatography to over 95% purity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Drebes, J.; Perbandt, M.; Wrenger, C.; Betzel, C.
Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus
Acta Crystallogr. Sect. F
67
479-481
2011
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Manually annotated by BRENDA team