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Synonyms
bluE, L-Thr kinase, L-Thr kinase/L-Thr-P decarboxylase, L-Thr kinase/L-Thr-phosphate decarboxylase, MmCobD, More, PduX, RsBluE, RSP_0788,
more
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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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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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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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?
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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RsBluE has L-Thr kinase activity in vitro, no or poor activity with L-serine, L-tyrosine, D-serine, D-threonine, or L-valine. RsBluE hydrolyzed ATP in the absence of L-Thr, the RsBluE ATPase activity is independent of potential amino acid substrate
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additional information
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RsBluE has L-Thr kinase activity in vitro, no or poor activity with L-serine, L-tyrosine, D-serine, D-threonine, or L-valine. RsBluE hydrolyzed ATP in the absence of L-Thr, the RsBluE ATPase activity is independent of potential amino acid substrate
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additional information
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RsBluE has L-Thr kinase activity in vitro, no or poor activity with L-serine, L-tyrosine, D-serine, D-threonine, or L-valine. RsBluE hydrolyzed ATP in the absence of L-Thr, the RsBluE ATPase activity is independent of potential amino acid substrate
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additional information
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RsBluE has L-Thr kinase activity in vitro, no or poor activity with L-serine, L-tyrosine, D-serine, D-threonine, or L-valine. RsBluE hydrolyzed ATP in the absence of L-Thr, the RsBluE ATPase activity is independent of potential amino acid substrate
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additional information
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RsBluE has L-Thr kinase activity in vitro, no or poor activity with L-serine, L-tyrosine, D-serine, D-threonine, or L-valine. RsBluE hydrolyzed ATP in the absence of L-Thr, the RsBluE ATPase activity is independent of potential amino acid substrate
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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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0.127 - 4.698
L-threonine
additional information
additional information
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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
additional information
additional information

Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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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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evolution

Rhodobacterales lack pduX, instead they have the non-orthologous bluE gene that encodes an enzyme that, unlike PduX, is specific for L-Thr and cannot use L-Ser. Phylogenetic analysis. The RsBluE enzyme is found to be restricted to a subclass of Rhodobacterales with genetic attributes that indicate they have a strong preference for AdoCbl. That is to say, these Rhodobacter species prefer and synthesize only a cobamide (Cba) with DMB as the lower ligand base and AP-P as the nucleotide linker, Coalpha-(alpha-5,6-dimethylbenzimidazolyl-Cobeta-adenosylcobamide) (a.k.a. adenosylcobalamin, AdoCbl, coenzyme B12, CoB12). Cells with incomplete AdoCbl production have a pigmentation phenotype
evolution
the CobD protein from Methanosarcina mazei differs from other CobD homologues by the presence of a 111-amino acid cysteine-rich extended C-terminus (MmCobD386-497) annotated as a putative metal-binding domain or zinc finger protein, but it actually is a ferroprotein. This C-terminal domain is sometimes encoded as an independent protein and other times fused to other Cba biosynthetic proteins (e.g. CbiZ, CbiA, CbiH, or BtuC)
evolution
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Rhodobacterales lack pduX, instead they have the non-orthologous bluE gene that encodes an enzyme that, unlike PduX, is specific for L-Thr and cannot use L-Ser. Phylogenetic analysis. The RsBluE enzyme is found to be restricted to a subclass of Rhodobacterales with genetic attributes that indicate they have a strong preference for AdoCbl. That is to say, these Rhodobacter species prefer and synthesize only a cobamide (Cba) with DMB as the lower ligand base and AP-P as the nucleotide linker, Coalpha-(alpha-5,6-dimethylbenzimidazolyl-Cobeta-adenosylcobamide) (a.k.a. adenosylcobalamin, AdoCbl, coenzyme B12, CoB12). Cells with incomplete AdoCbl production have a pigmentation phenotype
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evolution
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Rhodobacterales lack pduX, instead they have the non-orthologous bluE gene that encodes an enzyme that, unlike PduX, is specific for L-Thr and cannot use L-Ser. Phylogenetic analysis. The RsBluE enzyme is found to be restricted to a subclass of Rhodobacterales with genetic attributes that indicate they have a strong preference for AdoCbl. That is to say, these Rhodobacter species prefer and synthesize only a cobamide (Cba) with DMB as the lower ligand base and AP-P as the nucleotide linker, Coalpha-(alpha-5,6-dimethylbenzimidazolyl-Cobeta-adenosylcobamide) (a.k.a. adenosylcobalamin, AdoCbl, coenzyme B12, CoB12). Cells with incomplete AdoCbl production have a pigmentation phenotype
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evolution
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Rhodobacterales lack pduX, instead they have the non-orthologous bluE gene that encodes an enzyme that, unlike PduX, is specific for L-Thr and cannot use L-Ser. Phylogenetic analysis. The RsBluE enzyme is found to be restricted to a subclass of Rhodobacterales with genetic attributes that indicate they have a strong preference for AdoCbl. That is to say, these Rhodobacter species prefer and synthesize only a cobamide (Cba) with DMB as the lower ligand base and AP-P as the nucleotide linker, Coalpha-(alpha-5,6-dimethylbenzimidazolyl-Cobeta-adenosylcobamide) (a.k.a. adenosylcobalamin, AdoCbl, coenzyme B12, CoB12). Cells with incomplete AdoCbl production have a pigmentation phenotype
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evolution
-
Rhodobacterales lack pduX, instead they have the non-orthologous bluE gene that encodes an enzyme that, unlike PduX, is specific for L-Thr and cannot use L-Ser. Phylogenetic analysis. The RsBluE enzyme is found to be restricted to a subclass of Rhodobacterales with genetic attributes that indicate they have a strong preference for AdoCbl. That is to say, these Rhodobacter species prefer and synthesize only a cobamide (Cba) with DMB as the lower ligand base and AP-P as the nucleotide linker, Coalpha-(alpha-5,6-dimethylbenzimidazolyl-Cobeta-adenosylcobamide) (a.k.a. adenosylcobalamin, AdoCbl, coenzyme B12, CoB12). Cells with incomplete AdoCbl production have a pigmentation phenotype
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malfunction

inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium
malfunction
there is a 2600fold decrease in catalytic efficiency (kcat/Km) when the C-terminus is removed, or a 1200fold decrease when the enzyme is purified normoxically
malfunction
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inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium
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malfunction
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inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium
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malfunction
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inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium
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malfunction
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inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium
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metabolism

involved in the biosynthesis of adenosylcobalamin
metabolism
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involved in the biosynthesis of adenosylcobalamin
metabolism
enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales
metabolism
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enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales
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metabolism
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enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales
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metabolism
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enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales
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metabolism
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enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales
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physiological function

MmCobD is a bifunctional enzyme with L-threonine (L-Thr) kinase (PduX, EC 2.7.1.177) and pyridoxal 5'-phosphate (PLP)-dependent L-threonine phosphate (L-Thr-P) decarboxylase activities needed to synthesize the (R)-1-amino-propan-2-ol O-phosphate (a.k.a. (R)-1-amino-2-propanol-O-2-phosphate, AP-P) moiety of cobalamine (Cbl)
physiological function
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MmCobD is a bifunctional enzyme with L-threonine (L-Thr) kinase (PduX, EC 2.7.1.177) and pyridoxal 5'-phosphate (PLP)-dependent L-threonine phosphate (L-Thr-P) decarboxylase activities needed to synthesize the (R)-1-amino-propan-2-ol O-phosphate (a.k.a. (R)-1-amino-2-propanol-O-2-phosphate, AP-P) moiety of cobalamine (Cbl)
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additional information

MmCobD displays redox-sensitivity
additional information
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MmCobD displays redox-sensitivity
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C434A
site-directed mutagenesis, the MmCobDC434A variant has an ATPase activity that is comparable to wild-type despite having a growth phenotype similar to the DELTApduX vector control
C458A
site-directed mutagenesis, the MmCobDC458A variant has an ATPase activity that is comparable to wild-type despite having a growth phenotype similar to the DELTApduX vector control. The mutant variant has the lowest Fe to protein ratio
K234A
site-directed mutagenesis, the mutat variant lacks the ability to bind PLP effectively, resulting in 19 Fe per monomer, which is reduced compared to wild-type
C458A
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site-directed mutagenesis, the MmCobDC458A variant has an ATPase activity that is comparable to wild-type despite having a growth phenotype similar to the DELTApduX vector control. The mutant variant has the lowest Fe to protein ratio
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K234A
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site-directed mutagenesis, the mutat variant lacks the ability to bind PLP effectively, resulting in 19 Fe per monomer, which is reduced compared to wild-type
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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
additional information

recombinant expression of Rhodobacter sphaeroides BluE restores AdoCbl-dependent growth of a Salmonella enterica DELTApduX strain. Cultures of strains producing RsBluE or SePduX display a much shorter lag time (12 and 16 h, respectively) than cultures of the wild-type strain carrying the empty cloning vector, or the strain producing RcBluE (26 h). Inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium
additional information
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recombinant expression of Rhodobacter sphaeroides BluE restores AdoCbl-dependent growth of a Salmonella enterica DELTApduX strain. Cultures of strains producing RsBluE or SePduX display a much shorter lag time (12 and 16 h, respectively) than cultures of the wild-type strain carrying the empty cloning vector, or the strain producing RcBluE (26 h). Inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium
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additional information
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recombinant expression of Rhodobacter sphaeroides BluE restores AdoCbl-dependent growth of a Salmonella enterica DELTApduX strain. Cultures of strains producing RsBluE or SePduX display a much shorter lag time (12 and 16 h, respectively) than cultures of the wild-type strain carrying the empty cloning vector, or the strain producing RcBluE (26 h). Inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium
-
additional information
-
recombinant expression of Rhodobacter sphaeroides BluE restores AdoCbl-dependent growth of a Salmonella enterica DELTApduX strain. Cultures of strains producing RsBluE or SePduX display a much shorter lag time (12 and 16 h, respectively) than cultures of the wild-type strain carrying the empty cloning vector, or the strain producing RcBluE (26 h). Inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium
-
additional information
-
recombinant expression of Rhodobacter sphaeroides BluE restores AdoCbl-dependent growth of a Salmonella enterica DELTApduX strain. Cultures of strains producing RsBluE or SePduX display a much shorter lag time (12 and 16 h, respectively) than cultures of the wild-type strain carrying the empty cloning vector, or the strain producing RcBluE (26 h). Inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium
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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
Tavares, N.K.; Stracey, N.; Brunold, T.C.; Escalante-Semerena, J.C.
The L-Thr kinase/l-Thr-phosphate decarboxylase (CobD) enzyme from Methanosarcina mazei Goe1 contains metallocenters needed for optimal activity
Biochemistry
58
3260-3279
2019
Methanosarcina mazei (Q8PVB2), Methanosarcina mazei, Methanosarcina mazei Goe1 (Q8PVB2)
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Tavares, N.K.; VanDrisse, C.M.; Escalante-Semerena, J.C.
Rhodobacterales use a unique L-threonine kinase for the assembly of the nucleotide loop of coenzyme B12
Mol. Microbiol.
110
239-261
2018
Luteovulum sphaeroides (Q3IZR9), Luteovulum sphaeroides 2.4.1 (Q3IZR9), Luteovulum sphaeroides NCIB 8253 (Q3IZR9), Luteovulum sphaeroides ATCC 17023 (Q3IZR9), Luteovulum sphaeroides DSM 158 (Q3IZR9)
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