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Information on EC 2.7.1.177 - L-threonine kinase
for references in articles please use BRENDA:EC2.7.1.177
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.177 L-threonine kinase
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 expected taxonomic range for this enzyme is: Bacteria, Archaea
- 2.7.1.177
- enterica
-
metal-binding
-
adocbl
- cobamide
- mazei
-
cobyric
- o-phosphate
-
methanosarcina
showSynonyms
l-threonine kinase, l-thr kinase, rsblue, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bluE
L-Thr kinase
L-Thr kinase/L-Thr-P decarboxylase
L-Thr kinase/L-Thr-phosphate decarboxylase
MmCobD
PduX
RsBluE
RSP_0788
additional information
also see for L-Thr-phosphate decarboxylase, gene MM2060, EC 4.1.1.81
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-threonine = ADP + O-phospho-L-threonine
-
-
-
-
ATP + L-threonine = ADP + O-phospho-L-threonine
steady-state ordered BiBI mechanism
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PATHWAY SOURCE
PATHWAYS
MetaCyc
aminopropanol phosphate biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-threonine
ADP + O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Cereibacter sphaeroides ATCC 17023
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Cereibacter sphaeroides DSM 158
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Cereibacter sphaeroides NCIB 8253
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
-
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Substrates: -
Products: product indentified by 31P NMR spectroscopy
Products: product indentified by 31P NMR spectroscopy
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Cereibacter sphaeroides ATCC 17023
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Cereibacter sphaeroides DSM 158
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Cereibacter sphaeroides NCIB 8253
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the activity with CTP, GTP, or UTP is 6, 11, 3% of the activity with ATP, respectively
Products: -
Products: -
?
additional information
?
-
-
Substrates: the activity with CTP, GTP, or UTP is 6, 11, 3% of the activity with ATP, respectively
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 + L-threonine
ADP + O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Cereibacter sphaeroides ATCC 17023
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Cereibacter sphaeroides DSM 158
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Cereibacter sphaeroides NCIB 8253
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + L-threonine
ADP + O-phospho-L-threonine
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
activates at low concentration, but inhibits 75% at 100 mM
Fe2+
the wild-type MmCobD that is normoxically or anoxically purified and then reconstituted, or anoxically purified without reconstitution contains an average of 25 Fe atoms per monomer, with rather poor standard deviations. The C-terminus of MmCobD contains one or more [4Fe-4S] 2+ cluster(s). Although these [4Fe-4S]2+ cluster(s) are not required for activity, perturbations in the C-terminal domain result in the loss of Fe2+ and alterations in the enzyme activities associated with the N-terminus. The C-terminus is not required for the kinase or decarboxylase activities, the [4Fe-4S]2+ cluster-containing C-terminus may have a regulatory role, perhaps by gating the active site or facilitating the decarboxylation and or kinase reactions. Fe2+ is not detected in the N-terminus only (MmCobD1-385) protein sample
Mg2+
additional information
additional information
a divalent metal ion (1 mM) is required for RsBluE ATPase activity, with optimal activity observed with MnCl2
additional information
enzyme CobD contains metallocenters needed for optimal activity, MmCobD is a ferroprotein
additional information
-
enzyme CobD contains metallocenters needed for optimal activity, MmCobD is a ferroprotein
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
activates at low concentration, but inhibits 75% at 100 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 S99A, pH 7.4, temperature not specified in the publication
0.0338
ATP
mutant D103N, 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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
-
-
brenda
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
metabolism
physiological function
additional information
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
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
Cereibacter sphaeroides DSM 158
-
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
Cereibacter sphaeroides NCIB 8253
-
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
Cereibacter sphaeroides ATCC 17023
-
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
-
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
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
Cereibacter sphaeroides DSM 158
-
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
Cereibacter sphaeroides NCIB 8253
-
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
Cereibacter sphaeroides ATCC 17023
-
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
-
metabolism
involved in the biosynthesis of adenosylcobalamin
metabolism
enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales
metabolism
Cereibacter sphaeroides DSM 158
-
enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales
-
metabolism
Cereibacter sphaeroides NCIB 8253
-
enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales
-
metabolism
Cereibacter sphaeroides ATCC 17023
-
enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales
-
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
-
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)
-
Show AA Sequence and Transmembrane Helices (764 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
additional information
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
Cereibacter sphaeroides ATCC 17023
-
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
Cereibacter sphaeroides DSM 158
-
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
Cereibacter sphaeroides NCIB 8253
-
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene blueE, encded in the bluFEDCB operon, phylogenetic analysis, recombinant expression of Rhodobacter sphaeroides BluE restores AdoCbl-dependent growth of a Salmonella enterica DELTApduX strain, functional complementation of a Rhodobacter sphaeroides DELTAcobB strain, recombinant overproduction of RsBluE results in the production of substantial quantities of insoluble protein in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
brenda
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
Cereibacter sphaeroides (Q3IZR9), Cereibacter sphaeroides DSM 158 (Q3IZR9), Cereibacter sphaeroides NCIB 8253 (Q3IZR9), Cereibacter sphaeroides ATCC 17023 (Q3IZR9)
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.1.177)
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