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EC Tree
IUBMB Comments The enzyme is involved in the de novo synthesis of adenosylcobalamin. It is specific for ATP and free L-threonine. In the bacterium Salmonella enterica the activity with CTP, GTP, or UTP is 6, 11, and 3% of the activity with ATP.
The enzyme appears in viruses and cellular organisms
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ATP + L-threonine = ADP + O-phospho-L-threonine
ATP + L-threonine = ADP + O-phospho-L-threonine
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ATP + L-threonine = ADP + O-phospho-L-threonine
steady-state ordered BiBI mechanism
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ATP:L-threonine O3-phosphotransferase
The enzyme is involved in the de novo synthesis of adenosylcobalamin. It is specific for ATP and free L-threonine. In the bacterium Salmonella enterica the activity with CTP, GTP, or UTP is 6, 11, and 3% of the activity with ATP.
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ATP + L-threonine
ADP + O-phospho-L-threonine
additional information
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ATP + L-threonine
ADP + O-phospho-L-threonine
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ATP + L-threonine
ADP + O-phospho-L-threonine
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ATP + L-threonine
ADP + O-phospho-L-threonine
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product indentified by 31P NMR spectroscopy
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additional information
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the activity with CTP, GTP, or UTP is 6, 11, 3% of the activity with ATP, respectively
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additional information
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the activity with CTP, GTP, or UTP is 6, 11, 3% of the activity with ATP, respectively
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ATP + L-threonine
ADP + O-phospho-L-threonine
ATP + L-threonine
ADP + O-phospho-L-threonine
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ATP + L-threonine
ADP + O-phospho-L-threonine
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0.127 - 4.698
L-threonine
0.0547
ATP
Michaelis-Menten kinetics, pH 7.4, temperature not specified in the publication
0.0547
ATP
wild-type, pH 7.4, temperature not specified in the publication
0.068
ATP
mutant D135N, pH 7.4, temperature not specified in the publication
0.069
ATP
calculated from double-reciprocal plots, pH 7.4, temperature not specified in the publication
0.074
ATP
mutant S255A, pH 7.4, temperature not specified in the publication
0.076
ATP
mutant S253A, pH 7.4, temperature not specified in the publication
0.087
ATP
mutant T134A, pH 7.4, temperature not specified in the publication
0.098
ATP
mutant T101A, pH 7.4, temperature not specified in the publication
0.117
ATP
mutant E24Q, pH 7.4, temperature not specified in the publication
0.141
ATP
mutant D103N, pH 7.4, temperature not specified in the publication
0.163
ATP
mutant D103A, pH 7.4, temperature not specified in the publication
1.264
ATP
mutant E132Q, pH 7.4, temperature not specified in the publication
1.374
ATP
mutant S99A, pH 7.4, temperature not specified in the publication
1.979
ATP
mutant E132A, pH 7.4, temperature not specified in the publication
0.127
L-threonine
calculated from double-reciprocal plots, pH 7.4, temperature not specified in the publication
0.142
L-threonine
mutant T134A, pH 7.4, temperature not specified in the publication
0.144
L-threonine
mutant E132Q, pH 7.4, temperature not specified in the publication
0.146
L-threonine
Michaelis-Menten kinetics, pH 7.4, temperature not specified in the publication
0.146
L-threonine
wild-type, pH 7.4, temperature not specified in the publication
0.176
L-threonine
mutant S99A, pH 7.4, temperature not specified in the publication
0.184
L-threonine
mutant D103N, pH 7.4, temperature not specified in the publication
0.198
L-threonine
mutant E132A, pH 7.4, temperature not specified in the publication
0.22
L-threonine
mutant T101A, pH 7.4, temperature not specified in the publication
0.258
L-threonine
mutant D103A, pH 7.4, temperature not specified in the publication
0.273
L-threonine
mutant D135N, pH 7.4, temperature not specified in the publication
0.464
L-threonine
mutant E24Q, pH 7.4, temperature not specified in the publication
3.708
L-threonine
mutant S255A, pH 7.4, temperature not specified in the publication
4.698
L-threonine
mutant S253A, pH 7.4, temperature not specified in the publication
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0.016 - 0.0427
L-threonine
0.0173
ATP
mutant D135N, pH 7.4, temperature not specified in the publication
0.0187
ATP
mutant E24Q, pH 7.4, temperature not specified in the publication
0.0205
ATP
mutant E132A, pH 7.4, temperature not specified in the publication
0.0227
ATP
mutant S255A, pH 7.4, temperature not specified in the publication
0.026
ATP
mutant S253A, pH 7.4, temperature not specified in the publication
0.0272
ATP
mutant E132Q, pH 7.4, temperature not specified in the publication
0.0313
ATP
mutant D103A, pH 7.4, temperature not specified in the publication
0.0338
ATP
mutant D103N, pH 7.4, temperature not specified in the publication
0.0338
ATP
mutant S99A, pH 7.4, temperature not specified in the publication
0.0342
ATP
mutant T134A, pH 7.4, temperature not specified in the publication
0.0355
ATP
mutant T101A, pH 7.4, temperature not specified in the publication
0.408
ATP
wild-type, pH 7.4, temperature not specified in the publication
0.016
L-threonine
mutant D135N, pH 7.4, temperature not specified in the publication
0.0188
L-threonine
mutant E24Q, pH 7.4, temperature not specified in the publication
0.0193
L-threonine
mutant E132A, pH 7.4, temperature not specified in the publication
0.0238
L-threonine
mutant S255A, pH 7.4, temperature not specified in the publication
0.0258
L-threonine
mutant E132Q, pH 7.4, temperature not specified in the publication
0.0287
L-threonine
mutant S253A, pH 7.4, temperature not specified in the publication
0.0322
L-threonine
mutant D103A, pH 7.4, temperature not specified in the publication
0.0325
L-threonine
mutant S99A, pH 7.4, temperature not specified in the publication
0.0353
L-threonine
mutant T134A, pH 7.4, temperature not specified in the publication
0.0358
L-threonine
mutant D103N, pH 7.4, temperature not specified in the publication
0.037
L-threonine
mutant T101A, pH 7.4, temperature not specified in the publication
0.0427
L-threonine
wild-type, pH 7.4, temperature not specified in the publication
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0.000061 - 0.00292
L-threonine
0.000104
ATP
mutant E132A, pH 7.4, temperature not specified in the publication
0.00022
ATP
mutant E132Q, pH 7.4, temperature not specified in the publication
0.000247
ATP
mutant S99A, pH 7.4, temperature not specified in the publication
0.00159
ATP
mutant E24Q, pH 7.4, temperature not specified in the publication
0.00193
ATP
mutant D103A, pH 7.4, temperature not specified in the publication
0.0024
ATP
mutant D103N, pH 7.4, temperature not specified in the publication
0.00257
ATP
mutant D135N, pH 7.4, temperature not specified in the publication
0.00308
ATP
mutant S255A, pH 7.4, temperature not specified in the publication
0.00342
ATP
mutant S253A, pH 7.4, temperature not specified in the publication
0.00363
ATP
mutant T101A, pH 7.4, temperature not specified in the publication
0.00393
ATP
mutant T134A, pH 7.4, temperature not specified in the publication
0.00755
ATP
wild-type, pH 7.4, temperature not specified in the publication
0.000061
L-threonine
mutant S253A, pH 7.4, temperature not specified in the publication
0.0000643
L-threonine
mutant S255A, pH 7.4, temperature not specified in the publication
0.000407
L-threonine
mutant E24Q, pH 7.4, temperature not specified in the publication
0.000587
L-threonine
mutant D135N, pH 7.4, temperature not specified in the publication
0.00098
L-threonine
mutant E132A, pH 7.4, temperature not specified in the publication
0.00125
L-threonine
mutant D103A, pH 7.4, temperature not specified in the publication
0.00168
L-threonine
mutant T101A, pH 7.4, temperature not specified in the publication
0.0018
L-threonine
mutant E132Q, pH 7.4, temperature not specified in the publication
0.00185
L-threonine
mutant S99A, pH 7.4, temperature not specified in the publication
0.00195
L-threonine
mutant D103N, pH 7.4, temperature not specified in the publication
0.00248
L-threonine
mutant T134A, pH 7.4, temperature not specified in the publication
0.00292
L-threonine
wild-type, pH 7.4, temperature not specified in the publication
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no activity in Streptomyces coelicolor
the protein CouR3, encoded by gene couR3, exhibits an ATPase activity similar to its close orthologue, the threonine kinase PduX, but it does not show a threonine kinase activity
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brenda
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UniProt
brenda
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metabolism
involved in the biosynthesis of adenosylcobalamin
metabolism
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involved in the biosynthesis of adenosylcobalamin
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32787
x * 32787, calculated from sequence, x * 35000, SDS-PAGE
35000
x * 35000, SDS-PAGE
35000
x * 32787, calculated from sequence, x * 35000, SDS-PAGE
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x * 35000, SDS-PAGE
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x * 32787, calculated from sequence, x * 35000, SDS-PAGE
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D103N
similar growth rate compared to wild-type
D135A
no activity, decrease in helical structure
D135N
similar growth rate compared to wild-type
E132A
similar growth rate compared to wild-type
E132Q
similar growth rate compared to wild-type
E24A
no activity, decrease in helical structure
E24Q
similar growth rate compared to wild-type
S253A
low growth rate, reduced affinity for L-threonine
S255A
low growth rate, reduced affinity for L-threonine
S99A
similar growth rate compared to wild-type
T101A
similar growth rate compared to wild-type
T134A
similar growth rate compared to wild-type
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nickel-nitrilotriacetate column
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Fan, C.; Bobik, T.A.
The PduX enzyme of Salmonella enterica is an L-threonine kinase used for coenzyme B12 synthesis
J. Biol. Chem.
283
11322-11329
2008
Salmonella enterica (Q9XDM4), Salmonella enterica
brenda
Fan, C.; Fromm, H.J.; Bobik, T.A.
Kinetic and functional analysis of L-threonine kinase, the PduX enzyme of Salmonella enterica
J. Biol. Chem.
284
20240-20248
2009
Salmonella enterica (Q9XDM4), Salmonella enterica
brenda
Novotna, J.; Gust, B.; Kulik, A.; Spizek, J.; Heide, L.
Five gene products are required for assembly of the central pyrrole moiety of coumermycin A1
J. Ind. Microbiol. Biotechnol.
40
915-925
2013
no activity in Streptomyces coelicolor
brenda
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2.7.1.177 L-threonine kinase
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