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Information on EC 2.7.1.47 - D-ribulokinase
for references in articles please use BRENDA:EC2.7.1.47
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.47 D-ribulokinase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.7.1.47
- aerogenes
- ribitol
-
klebsiella
- d-xylulokinase
- d-arabinose
-
aerobacter
- l-fucose
- d-xylulose
- xylitol
- l-fuculose-1-phosphate
- pentitol
- d-arabitol
- pentose
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uncommon
-
superproduce
showSynonyms
d-ribulokinase, ydr109c protein, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
kinase (phosphorylating), D-ribulo-
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kinase, D-ribulo- (phosphorylating)
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Ydr109c protein
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + D-ribulose = ADP + D-ribulose 5-phosphate
random bi bi reaction mechanism
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ATP + D-ribulose = ADP + D-ribulose 5-phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
D-arabinose degradation I, D-arabinose degradation V, ribitol degradation I
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-ribulose 5-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9026-40-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + D-arabitol
?
-
Substrates: poor substrate, not L-isomer
Products: -
Products: -
?
ATP + D-ribulose
?
-
Substrates: inducible enzyme of ribitol catabolism
Products: -
Products: -
?
ATP + L-ribulose
ADP + L-ribulose 5-phosphate
Substrates: 8% activity compared to D-ribulose
Products: -
Products: -
?
ATP + ribitol
ADP + ribitol phosphate
Substrates: 21% activity compared to D-ribulose
Products: -
Products: -
?
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
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Substrates: -
Products: -
Products: -
?
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
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Substrates: specific for D-isomer
Products: -
Products: -
?
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
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Substrates: ATP cannot be replaced by ITP, GTP or ADP
Products: -
Products: -
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ATP + D-ribulose
ADP + D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
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additional information
?
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Substrates: the FGGY protein shows a clear substrate preference for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Recombinant human FGGY protein specifically converts D-ribulose to D-ribulose 5-phosphate in the presence of ATP. No or poor activity with D-xylulose, L-xylulose, D-glucose, arabitol, erythritol, L-arabinose, D-arabinose, D-ribose, glycerol, D-ribulose 5-phosphate, gluconate, 2-deoxy-D-ribose, D-lyxose, D-ribose 5-phosphate, D-mannitol, and D-ribose 1-phosphate
Products: -
Products: -
?
additional information
?
-
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Substrates: the FGGY protein shows a clear substrate preference for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Recombinant human FGGY protein specifically converts D-ribulose to D-ribulose 5-phosphate in the presence of ATP. No or poor activity with D-xylulose, L-xylulose, D-glucose, arabitol, erythritol, L-arabinose, D-arabinose, D-ribose, glycerol, D-ribulose 5-phosphate, gluconate, 2-deoxy-D-ribose, D-lyxose, D-ribose 5-phosphate, D-mannitol, and D-ribose 1-phosphate
Products: -
Products: -
?
additional information
?
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Substrates: the Ydr109c protein shows a clear specificity for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Recombinant yeast Ydr109c specifically converts D-ribulose to D-ribulose 5-phosphate in the presence of ATP. No activity with L-ribulose, ribitol, D-xylulose, L-xylulose, D-glucose, arabitol, erythritol, L-arabinose, D-arabinose, D-ribose, glycerol, D-ribulose 5-phosphate, gluconate, 2-deoxy-D-ribose, D-lyxose, D-ribose 5-phosphate, D-mannitol, and D-ribose 1-phosphate
Products: -
Products: -
?
additional information
?
-
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Substrates: the Ydr109c protein shows a clear specificity for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Recombinant yeast Ydr109c specifically converts D-ribulose to D-ribulose 5-phosphate in the presence of ATP. No activity with L-ribulose, ribitol, D-xylulose, L-xylulose, D-glucose, arabitol, erythritol, L-arabinose, D-arabinose, D-ribose, glycerol, D-ribulose 5-phosphate, gluconate, 2-deoxy-D-ribose, D-lyxose, D-ribose 5-phosphate, D-mannitol, and D-ribose 1-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: the Ydr109c protein shows a clear specificity for D-ribulose over a range of other sugars and sugar derivatives tested, including L-ribulose. Recombinant yeast Ydr109c specifically converts D-ribulose to D-ribulose 5-phosphate in the presence of ATP. No activity with L-ribulose, ribitol, D-xylulose, L-xylulose, D-glucose, arabitol, erythritol, L-arabinose, D-arabinose, D-ribose, glycerol, D-ribulose 5-phosphate, gluconate, 2-deoxy-D-ribose, D-lyxose, D-ribose 5-phosphate, D-mannitol, and D-ribose 1-phosphate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + D-ribulose
?
-
Substrates: inducible enzyme of ribitol catabolism
Products: -
Products: -
?
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mg2+
-
inhibition at a Mg/ATP ratio above 2, 11% inhibition at a ratio of 3
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10.5
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pH 6.0: about 70% of maximal activity, pH 10.5: about half-maximal activity at pH 10.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expressed as constitutive enzyme in Escherichia coli K12 construct strain NC629
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
the enzyme belongs to the broadly conserved FGGY family of carbohydrate kinases. Yeast Ydr109c and human FGGY are homologues of a proteobacterial D-ribulokinase involved in ribitol metabolism
evolution
the enzyme belongs to the broadly conserved FGGY family of carbohydrate kinases. Yeast Ydr109c and human FGGY are homologues of a proteobacterial D-ribulokinase involved in ribitol metabolism
evolution
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the enzyme belongs to the broadly conserved FGGY family of carbohydrate kinases. Yeast Ydr109c and human FGGY are homologues of a proteobacterial D-ribulokinase involved in ribitol metabolism
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malfunction
untargeted metabolomics analysis of an Saccharomyces cerevisiae deletion mutant of YDR109C reveals ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain
malfunction
in human FGGY deletion mutant HEK293 cells, ribulose can only be detected when ribitol is added to the cultivation medium. Under this condition, FGGY silencing leads to ribulose accumulation
malfunction
-
untargeted metabolomics analysis of an Saccharomyces cerevisiae deletion mutant of YDR109C reveals ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain
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physiological function
the Ydr109c protein might act as a metabolite repair enzyme, serving to re-phosphorylate free D-ribulose generated by promiscuous phosphatases from D-ribulose 5-phosphate
physiological function
the FGGY protein might act as a metabolite repair enzyme, serving to re-phosphorylate free D-ribulose generated by promiscuous phosphatases from D-ribulose 5-phosphate
physiological function
-
the Ydr109c protein might act as a metabolite repair enzyme, serving to re-phosphorylate free D-ribulose generated by promiscuous phosphatases from D-ribulose 5-phosphate
-
additional information
the enzyme contains a 5-residue D-ribulokinase signature motif (TCSLV). Structural homology modeling of yeast D-ribulokinase and definition of a D-ribulokinase signature motif, using template structures from PDB entries 3GG4 chain A and 3L0Q chain A, respectively, of Yersinia pseudotuberculosis D-ribulokinase
additional information
-
the enzyme contains a 5-residue D-ribulokinase signature motif (TCSLV). Structural homology modeling of yeast D-ribulokinase and definition of a D-ribulokinase signature motif, using template structures from PDB entries 3GG4 chain A and 3L0Q chain A, respectively, of Yersinia pseudotuberculosis D-ribulokinase
additional information
the enzyme contains a 5-residue D-ribulokinase signature motif (TCSLV). Structural homology modeling of human D-ribulokinase and definition of a D-ribulokinase signature motif, using template structures from PDB entries 3GG4 chain A and 3L0Q chain A, respectively, of Yersinia pseudotuberculosis D-ribulokinase
additional information
-
the enzyme contains a 5-residue D-ribulokinase signature motif (TCSLV). Structural homology modeling of human D-ribulokinase and definition of a D-ribulokinase signature motif, using template structures from PDB entries 3GG4 chain A and 3L0Q chain A, respectively, of Yersinia pseudotuberculosis D-ribulokinase
additional information
-
the enzyme contains a 5-residue D-ribulokinase signature motif (TCSLV). Structural homology modeling of yeast D-ribulokinase and definition of a D-ribulokinase signature motif, using template structures from PDB entries 3GG4 chain A and 3L0Q chain A, respectively, of Yersinia pseudotuberculosis D-ribulokinase
-
Show AA Sequence and Transmembrane Helices (1014 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
112000
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recombinant enzyme expressed in E. coli strain NC629, gel filtration
60000
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2 * 60000, recombinant enzyme expressed in Escherichia coli strain NC629, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
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2 * 60000, recombinant enzyme expressed in Escherichia coli strain NC629, SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
generation of human FGGY deletion mutant HEK293 cells, when ribitol is added to the cultivation medium, FGGY silencing leads to ribulose accumulation
additional information
-
generation of human FGGY deletion mutant HEK293 cells, when ribitol is added to the cultivation medium, FGGY silencing leads to ribulose accumulation
additional information
untargeted metabolomics analysis of an Saccharomyces cerevisiae deletion mutant of YDR109C reveals ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain. Effect of YDR109C deletion on metabolite level other than ribulose and ribitol, overview
additional information
-
untargeted metabolomics analysis of an Saccharomyces cerevisiae deletion mutant of YDR109C reveals ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain. Effect of YDR109C deletion on metabolite level other than ribulose and ribitol, overview
additional information
-
untargeted metabolomics analysis of an Saccharomyces cerevisiae deletion mutant of YDR109C reveals ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain. Effect of YDR109C deletion on metabolite level other than ribulose and ribitol, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the human recombinant His-tagged FGGY protein is, unlike its yeast homologue, very stable
the yeast recombinant His-tagged Ydr109c protein is, unlike its human homologue, very unstable
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged FGGY from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His-tagged Ydr109c from Escherichia coli by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli K12 strain NC629 harbouring multi-copy lambdaprbt-101 prophage which carries the rbt-operon
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gene FGGY, sequence comparisons and phylogenetic tree, recombinant expression of N-terminally His-tagged FGGY in Escherichia coli
gene YDR109C, sequence comparisons and phylogenetic tree, recombinant expression of N-terminally His-tagged Ydr109c in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fromm, H.J.
D-Ribulokinase from Aerobacter aerogenes
J. Biol. Chem.
234
3097-3101
1959
Klebsiella aerogenes
brenda
Stayton, M.M.; Fromm, H.J.
Purification, properties, and kinetics of D-ribulokinase from Aerobacter aerogenes
J. Biol. Chem.
254
3765-3771
1979
Klebsiella aerogenes
brenda
Neuberger, M.S.; Hartley, B.S.; Walker, J.E.
Purification and properties of D-ribulokinase and D-xylulokinase from Klebsiella aerogenes
Biochem. J.
193
513-524
1981
Klebsiella aerogenes
brenda
Singh, C.; Glaab, E.; Linster, C.L.
Molecular identification of D-ribulokinase in budding yeast and mammals
J. Biol. Chem.
292
1005-1028
2017
Homo sapiens (Q96C11), Homo sapiens, Saccharomyces cerevisiae (Q04585), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q04585)
brenda
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