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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PII GlnK]
substrate GlnK-UMP3, the enzyme acts on residue Tyr51 of GlnB
-
-
r
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
diphosphate + uridylyl-[protein-PII GlnK]
UTP + [protein-PII GlnK]
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
UTP + GlnB
diphosphate + uridylyl-GlnB
UTP + GlnK
diphosphate + uridylyl-GlnK
-
-
-
?
UTP + GlnZ
diphosphate + uridylyl-GlnZ
-
-
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PII GlnK]
diphosphate + uridylyl-[protein-PII GlnK]
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
additional information
?
-
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
-
-
-
r
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
-
-
-
r
diphosphate + uridylyl-[protein-PII GlnK]
UTP + [protein-PII GlnK]
substrate GlnK-UMP3, the enzyme acts on residue Tyr51 of GlnK
-
-
r
diphosphate + uridylyl-[protein-PII GlnK]
UTP + [protein-PII GlnK]
substrate GlnK-UMP3, the enzyme acts on residue Tyr51 of GlnK
-
-
r
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
-
-
-
r
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
-
-
-
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
-
-
-
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
-
-
-
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
-
-
-
r
UTP + GlnB
diphosphate + uridylyl-GlnB
-
-
-
r
UTP + GlnB
diphosphate + uridylyl-GlnB
-
-
-
-
r
UTP + GlnB
diphosphate + uridylyl-GlnB
-
-
-
?
UTP + GlnB
diphosphate + uridylyl-GlnB
-
-
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
-
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
enzyme is pivotal in sensing intracellular levels of fixed nitrogen
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
GlnK protein mutant Y51F is no substrate
-
?
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
uridylylation of GlnK protein is essential for the cell to respond to nitrogen limitation
-
?
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
regulatory protein
-
ir
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
GlnK protein mutant Y51N is no substrate
-
ir
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
very slow reverse reaction
-
ir
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
GlnK protein wild-type and mutant R47W
-
ir
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
enzyme regulates the regulatory GlnK protein
-
ir
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
PII-1 protein
-
-
r
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
PII-1 protein
-
-
r
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
the enzyme acts on residue Tyr51 of GlnK
-
-
r
UTP + [protein-PII GlnK]
diphosphate + uridylyl-[protein-PII GlnK]
the enzyme acts on residue Tyr51 of GlnK
-
-
r
UTP + [protein-PII GlnK]
diphosphate + uridylyl-[protein-PII GlnK]
the enzyme acts on residue Tyr51 of GlnK
-
-
r
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
PII-2 protein
-
-
r
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
PII-2 protein
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
enzyme is pivotal in sensing intracellular levels of fixed nitrogen
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
unlike in enterobacteria, the enzyme is not the primary nitrogen sensor, overexpression leads to derepression of nitrogen control
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
signal transduction cascade model
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
mutants Y51F and Y51S are no substrates, Y46F is a poor substrate, structure analysis of the crystallized protein PII variants
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Tyr51 is the site of uridylation
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
signal transduction cascade model
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
nitrogen-regulation of gene transcription results from the regulation of the phosphorylation state of the enhancer-binding transcription factor NRI. Phosphorylation of NRI is regulated by a bicyclic cascade system containing four regulatory proteins, one of which is EC 2.7.7.59
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
the enzyme is constitutively expressed at a low level. The functioning of the glutamine synthetase adenylylation cascade is regulated by modulation of the activities of uridylyltransferase and adenylyltransferase, rather than by changes in the expression of their genes
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
GlnD of Herbaspirillum seropedicae is overexpressed with the two PII proteins GlnK and GlnB. Results show that GlnD uridylylates GlnB and GlnK trimers producing the forms PII(UMP)1, PII(UMP)2 and PII(UMP)3. GlnB is more efficiently uridylylated than GlnK
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is required for derepression of ntr-regulated promoters such as glnAp2 and pnifL, but is not involved in the nif-specific response to changes in nitrogen status mediated by the nifL products
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the uridylylation of the PII protein is modulated by the intracellular glutamine/alpha-ketoglutarate ratio
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
enzyme is not essential for nitrogen fixation of the host plant
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
GlnD plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of PII proteins, which in turn regulate a variety of other proteins. It is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
bifunctional uridylyltransferase/uridylyl-removing enzyme, in Rhodospirillum rubrum three PII proteins have been identified GlnB, GlnK and GlnJ, respectively, in this study it is shown that all three PII proteins are uridylylated, although the efficacy is dependent on the cation present, Mn2+ or Mg2+, respectively
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
bifunctional uridylyltransferase/uridylyl-removing enzyme, in Rhodospirillum rubrum three PII proteins have been identified GlnB, GlnK and GlnJ, respectively, in this study it is shown that all three PII proteins are uridylylated, although the efficacy is dependent on the cation present, Mn2+ or Mg2+, respectively
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
additional information
?
-
-
regulation
-
-
?
additional information
?
-
-
enzyme is required for the relief of NifL inhibition of NifA under N-limiting conditions
-
-
?
additional information
?
-
-
schematic regulation model
-
-
?
additional information
?
-
-
protein PII is predominantly a ATase regulator protein, while PII and GlnK protein both activate the phosphatase activity of NRII, GlnK protein controls the nitrogen assimilation via ATase in absence of protein PII
-
-
?
additional information
?
-
the bifunctional enzyme GlnD catalyzes the uridylylation and, in the presence of glutamine, the deuridylylation of EcGlnB PII protein
-
-
-
additional information
?
-
-
schematic regulation model
-
-
?
additional information
?
-
-
PII protein GlnK is adenylylated by GlnD in response to nitrogen limitation. In contrast to Escherichia coli, GlnK adenylylation in Mycobyceterium tuberculosis does not regulate glutamine synthetase adenylylation, nor does it mediate the transcriptomic response to nitrogen limitation
-
-
?
additional information
?
-
-
PII protein GlnK is adenylylated by GlnD in response to nitrogen limitation. In contrast to Escherichia coli, GlnK adenylylation in Mycobyceterium tuberculosis does not regulate glutamine synthetase adenylylation, nor does it mediate the transcriptomic response to nitrogen limitation
-
-
?
additional information
?
-
PII protein GlnK is adenylylated by GlnD in response to nitrogen limitation
-
-
?
additional information
?
-
PII protein GlnK is adenylylated by GlnD in response to nitrogen limitation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
UTP + GlnB
diphosphate + uridylyl-GlnB
-
-
-
r
UTP + GlnZ
diphosphate + uridylyl-GlnZ
-
-
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
additional information
?
-
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
-
-
-
r
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
-
-
-
r
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
-
-
-
r
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
-
-
-
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
-
-
-
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
-
-
-
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
-
-
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
enzyme is pivotal in sensing intracellular levels of fixed nitrogen
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
uridylylation of GlnK protein is essential for the cell to respond to nitrogen limitation
-
?
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
enzyme regulates the regulatory GlnK protein
-
ir
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
PII-1 protein
-
-
r
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
PII-1 protein
-
-
r
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
PII-2 protein
-
-
r
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
PII-2 protein
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
enzyme is pivotal in sensing intracellular levels of fixed nitrogen
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
unlike in enterobacteria, the enzyme is not the primary nitrogen sensor, overexpression leads to derepression of nitrogen control
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
signal transduction cascade model
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
signal transduction cascade model
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
nitrogen-regulation of gene transcription results from the regulation of the phosphorylation state of the enhancer-binding transcription factor NRI. Phosphorylation of NRI is regulated by a bicyclic cascade system containing four regulatory proteins, one of which is EC 2.7.7.59
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
the enzyme is constitutively expressed at a low level. The functioning of the glutamine synthetase adenylylation cascade is regulated by modulation of the activities of uridylyltransferase and adenylyltransferase, rather than by changes in the expression of their genes
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme is required for derepression of ntr-regulated promoters such as glnAp2 and pnifL, but is not involved in the nif-specific response to changes in nitrogen status mediated by the nifL products
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
the uridylylation of the PII protein is modulated by the intracellular glutamine/alpha-ketoglutarate ratio
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
enzyme is not essential for nitrogen fixation of the host plant
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
GlnD plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of PII proteins, which in turn regulate a variety of other proteins. It is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
-
-
?
additional information
?
-
-
regulation
-
-
?
additional information
?
-
-
enzyme is required for the relief of NifL inhibition of NifA under N-limiting conditions
-
-
?
additional information
?
-
-
schematic regulation model
-
-
?
additional information
?
-
-
protein PII is predominantly a ATase regulator protein, while PII and GlnK protein both activate the phosphatase activity of NRII, GlnK protein controls the nitrogen assimilation via ATase in absence of protein PII
-
-
?
additional information
?
-
-
schematic regulation model
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2-oxoglutarate
2-OG, inhibits the UR activity of GlnD
3-phosphoglycerate
-
inhibits uridylyl removing activity
acetyl-CoA
-
inhibits uridylyl removing activity
ADP
-
inhibits uridylyl removing activity
AMP
-
inhibits uridylyl removing activity
ATP
-
inhibits uridylyl removing activity
Cd2+
-
inhibits uridylyl removing activity
CDP
-
inhibits uridylyl removing activity
CDP-glucose
-
inhibits uridylyl removing activity
CMP
-
inhibits uridylyl removing activity
Co2+
-
inhibits uridylyl removing activity
CoA
-
inhibits uridylyl removing activity
CTP
-
inhibits uridylyl removing activity
Cu2+
-
inhibits uridylyl removing activity
D-fructose 1,6-diphosphate
-
inhibits uridylyl removing activity
dCMP
-
inhibits uridylyl removing activity
dUMP
-
inhibits uridylyl removing activity
Endogenous inhibitor
-
of MW greater than 100000
-
GDP
-
inhibits uridylyl removing activity
GMP
-
inhibits uridylyl removing activity
GTP
-
inhibits uridylyl removing activity
IDP
-
inhibits uridylyl removing activity
IMP
-
inhibits uridylyl removing activity
ITP
-
inhibits uridylyl removing activity
NAD+
-
inhibits uridylyl removing activity
NADH
-
inhibits uridylyl removing activity
NADP+
-
inhibits uridylyl removing activity
NADPH
-
inhibits uridylyl removing activity
Ni2+
-
inhibits uridylyl removing activity
phosphoenolpyruvate
-
inhibits uridylyl removing activity
TDP
-
inhibits uridylyl removing activity
TMP
-
inhibits uridylyl removing activity
TTP
-
inhibits uridylyl removing activity
UDP
-
inhibits uridylyl removing activity
UDP-glucose
-
inhibits uridylyl removing activity
UMP
-
inhibits uridylyl removing activity
Zn2+
-
inhibits uridylyl removing activity
glutamine
-
glutamine
-
inhibition of uridylyltransferase activity
glutamine
-
shows an inhibition of 65% of GlnB uridylylation and 70% of GlnK uridylylation
glutamine
the presence of glutamine results in increased uridylyl-removing enzyme (UR) activity of GlnD, while it inhibits the uridylyl transferase (UTase) activity of GlnD
UTP
-
inhibits uridylyl removing activity
UTP
the higher the UTP concentration, the longer GlnK remains uridylylated with the wild-type enzyme, although not with GlnDDELTAACT mutant
additional information
-
no inhibition of uridylyl removing activity by Ba2+, Ca2+, and Mg2+ at 1 mM
-
additional information
-
GlnK protein-UMP is a very poor inhibitor of protein PII-UMP deuridylylation
-
additional information
-
in contrast to Escherichia coli the uridylylation reaction is not inhibited by glutamine
-
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Ataxia
Assessment of ataxia phenotype in a new mouse model of galactose-1 phosphate uridylyltransferase (GALT) deficiency.
Carcinoma, Hepatocellular
The Leloir Pathway of Galactose Metabolism - A Novel Therapeutic Target for Hepatocellular Carcinoma.
Confusion
Separation and characterization of two UTP-utilizing hexose phosphate uridylyltransferases from Entamoeba histolytica.
Cysts
A comparative study of UTP-D-glucose-1-phosphate uridylyl transferase in the cysts of Echinococcus multilocularis and the livers of infected and control Meriones unguiculatus.
Down Syndrome
[Enzymatic study of leukocytes during leukemia and trisomy 21. A common anomaly: increase in galactose-1-phosphate uridylyl transferase]
Fructose Intolerance
Consequences of recurrent phosphate trapping induced by repeated injections of 2-deoxy-D-galactose. Biochemical and morphological studies in rats.
Galactosemias
A De Novo Variant in Galactose-1-P Uridylyltransferase (GALT) Leading to Classic Galactosemia.
Galactosemias
A pilot study of neonatal GALT gene replacement using AAV9 dramatically lowers galactose metabolites in blood, liver, and brain and minimizes cataracts in GALT-null rat pups.
Galactosemias
Developmental Outcomes of School-Age Children with Duarte Galactosemia: A Pilot Study.
Galactosemias
Hand fine motor control in classic galactosemia.
Galactosemias
Impact of patient mutations on heterodimer formation and function in human galactose-1-P uridylyltransferase.
Galactosemias
Manganese-Based Superoxide Dismutase Mimics Modify Both Acute and Long-Term Outcome Severity in a Drosophila melanogaster Model of Classic Galactosemia.
Galactosemias
Modifiers of ovarian function in girls and women with classic galactosemia.
Galactosemias
Novel mRNA-Based Therapy Reduces Toxic Galactose Metabolites and Overcomes Galactose Sensitivity in a Mouse Model of Classic Galactosemia.
Galactosemias
Receptor-mediated attenuation of insulin-like growth factor-1 activity by galactose-1-phosphate in neonate skin fibroblast cultures: Galactosemia pathogenesis.
Galactosemias
Reversal of aberrant PI3K/Akt signaling by Salubrinal in a GalT-deficient mouse model.
Galactosemias
Reversion from deficiency of galactose-1-phosphate uridylytransferase (GALT) in an SV40-transformed human fibroblast line.
Galactosemias
Salubrinal enhances eIF2? phosphorylation and improves fertility in a mouse model of Classic Galactosemia.
Galactosemias
Starch gel electrophoresis for galactose-1-phosphate uridylyl-transferase applied to dried filter paper blood specimens.
Galactosemias
Structure-Based Optimization of Small Molecule Human Galactokinase Inhibitors.
Galactosemias
Transient kinetics of formation and reaction of the uridylyl-enzyme form of galactose-1-P uridylyltransferase and its Q168R-variant: insight into the molecular basis of galactosemia.
Galactosemias
[Galactosemia caused by galactosephosphate uridylyltransferase]
Genetic Diseases, Inborn
A De Novo Variant in Galactose-1-P Uridylyltransferase (GALT) Leading to Classic Galactosemia.
Genetic Diseases, Inborn
Consequences of recurrent phosphate trapping induced by repeated injections of 2-deoxy-D-galactose. Biochemical and morphological studies in rats.
Genetic Diseases, Inborn
Modifiers of ovarian function in girls and women with classic galactosemia.
glucose-6-phosphatase deficiency
Consequences of recurrent phosphate trapping induced by repeated injections of 2-deoxy-D-galactose. Biochemical and morphological studies in rats.
Glycogen Storage Disease Type I
Consequences of recurrent phosphate trapping induced by repeated injections of 2-deoxy-D-galactose. Biochemical and morphological studies in rats.
Infertility
Galactose-1 phosphate uridylyltransferase (GalT) gene: A novel positive regulator of the PI3K/Akt signaling pathway in mouse fibroblasts.
Infertility
Subfertility and growth restriction in a new galactose-1 phosphate uridylyltransferase (GALT) - deficient mouse model.
Leukemia
[Enzymatic study of leukocytes during leukemia and trisomy 21. A common anomaly: increase in galactose-1-phosphate uridylyl transferase]
Metabolism, Inborn Errors
Starch gel electrophoresis for galactose-1-phosphate uridylyl-transferase applied to dried filter paper blood specimens.
Starvation
The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP.
Tuberculosis
Expression, purification and preliminary crystallographic analysis of N-acetylglucosamine-1-phosphate uridylyltransferase from Mycobacterium tuberculosis.
[protein-pii] uridylyltransferase deficiency
Consequences of recurrent phosphate trapping induced by repeated injections of 2-deoxy-D-galactose. Biochemical and morphological studies in rats.
[protein-pii] uridylyltransferase deficiency
[Galactose 1-phosphate level in children with various types of hexosephosphate uridylyltransferase deficiency]
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additional information
crystal structure determination and analysis at 1.9 A resolution of the purified Escherichia coli GlnB (EcGlnB) PII protein in fully uridylylated form (EcGlnB-UMP3), structure-function analysis, overview. The T-loop is not visible. Unlike crystalline non-uridylylated EcGlnB, in which T-loops are fixed, uridylylation renders the T-loop highly mobile because of loss of contacts mediated by Tyr51, with concomitant abolition of T-loop anchoring via Arg38 on the ATP site. Analysis of mechanisms of PII selectivity for ATP and of PII-UMP3 signalling, proposing a model for the architecture of the complex of EcGlnBUMP3 with the uridylylation-sensitive PII target ATase (which adenylylates/deadenylylates glutamine synthetase [GS]) and with GS. Good X-ray diffracting crystals of trigonal shape and good size are obtained with fully uridylylated EcGlnB only when ATP, MgCl2 and 2-oxolutarate are present
malfunction
the higher the UTP concentration, the longer GlnK remains uridylylated with the wild-type enzyme, while there is enough UTP, GlnDDELTAACT catalyzes the uridylylation/deuridylylation futile cycle, confirming the regulatory role of the ACT domain
malfunction
-
the higher the UTP concentration, the longer GlnK remains uridylylated with the wild-type enzyme, while there is enough UTP, GlnDDELTAACT catalyzes the uridylylation/deuridylylation futile cycle, confirming the regulatory role of the ACT domain
-
metabolism
Azospirillum brasilense is a diazotrophic microorganism capable of associating with roots of important grasses and cereals, promoting plant growth and increasing crop yields. Nitrogen levels and the Ntr regulatory system control the nitrogen metabolism in Azospirillum brasilense. This system comprises the nitrogen regulatory proteins GlnD, which is capable of adding uridylyl groups to the PII proteins, GlnB (PII-1) and GlnZ (PII-2), under limiting nitrogen levels. Under such conditions, the histidine kinase NtrB (nitrogen regulatory protein B) cannot interact with GlnB and phosphorylate NtrC (nitrogen regulatory protein C). The phosphorylated form of NtrC acts as a transcriptional activator of genes involved in the metabolism of alternative nitrogen sources. Analysis of proteomic profile and proteins regulated by nitrogen availability in Azospirillum brasilense ntrC, identification of proteins likely to belong to the NtrC regulon, overview
metabolism
the PII proteins play an important role in this system by modulating the cellular metabolism through physical interaction with protein partners. Herbaspirillum seropedicae, a nitrogen-fixing bacterium, has two PII proteins paralogues, GlnB and GlnK. The interaction of Herbaspirillum seropedicae PII proteins with its targets is regulated by allosteric ligands and by reversible post-translational uridylylation. The interaction between PII proteins and its targets is regulated at two distinct levels: the allosteric binding of molecular effectors and the post-translational modification status. By controlling the post-translational state of PII proteins, the GlnD enzyme acts as a primary sensor of nitrogen in the cell. Regulatory role of the ACT domain
metabolism
to adapt to environments with variable nitrogen sources and richness, the widely distributed homotrimeric PII signalling proteins bind their allosteric effectors ADP/ATP/2-oxoglutarate, and experience nitrogen-sensitive uridylylation of their flexible T-loops at Tyr51 by enzyme GlnD, regulating their interactions with effector proteins
metabolism
-
Azospirillum brasilense is a diazotrophic microorganism capable of associating with roots of important grasses and cereals, promoting plant growth and increasing crop yields. Nitrogen levels and the Ntr regulatory system control the nitrogen metabolism in Azospirillum brasilense. This system comprises the nitrogen regulatory proteins GlnD, which is capable of adding uridylyl groups to the PII proteins, GlnB (PII-1) and GlnZ (PII-2), under limiting nitrogen levels. Under such conditions, the histidine kinase NtrB (nitrogen regulatory protein B) cannot interact with GlnB and phosphorylate NtrC (nitrogen regulatory protein C). The phosphorylated form of NtrC acts as a transcriptional activator of genes involved in the metabolism of alternative nitrogen sources. Analysis of proteomic profile and proteins regulated by nitrogen availability in Azospirillum brasilense ntrC, identification of proteins likely to belong to the NtrC regulon, overview
-
metabolism
-
the PII proteins play an important role in this system by modulating the cellular metabolism through physical interaction with protein partners. Herbaspirillum seropedicae, a nitrogen-fixing bacterium, has two PII proteins paralogues, GlnB and GlnK. The interaction of Herbaspirillum seropedicae PII proteins with its targets is regulated by allosteric ligands and by reversible post-translational uridylylation. The interaction between PII proteins and its targets is regulated at two distinct levels: the allosteric binding of molecular effectors and the post-translational modification status. By controlling the post-translational state of PII proteins, the GlnD enzyme acts as a primary sensor of nitrogen in the cell. Regulatory role of the ACT domain
-
physiological function
the uridylyltransferase/uridylyl-cleavage enzyme GlnD has a role in free-living growth and in symbiotic nitrogen exchange that does not depend on its substrates, the PII proteins. An in-frame deletion mutationglnDsm2 mutation has severe defects in regulating free-living and symbiotic nitrogen metabolismcompared to the glnBglnK double-deletion strain lacking the substrates of GlnD. Data indicate that the GlnD uridylyltransferase is required for proper regulation of nitrogen exchange in symbiosis with the host plant but that the PII substrate proteins are not involved in this regulation or that the glnD-sm2 mutation disrupts some additional activity of GlnD
physiological function
control for PII interaction with target proteins involves the covalent modification of the T-loop, such as uridylylation, phosphorylation or adenylylation. The uridylylation of PII proteins occurs in a conserved residue of tyrosine (Tyr51) in the T-loop. Uridylylation of Tyr51 renders a T-loop more mobile in comparison with the unmodified protein. The PII uridylylation is catalyzed by the GlnD enzyme, which also catalyzes the removal of the uridylyl group from PII. The choice between uridylyl transferase (UTase) and the uridylyl-removing activities (UR) of GlnD is essential to the function of the Ntr system and is supposedly dependent on the in vivo fluctuation of key metabolites. The deuridylylation activity of Herbaspirillum seropedicae GlnD protein is regulated by the glutamine:2-oxoglutarate ratio. GlnD can sense the glutamine:2-oxoglutarate ratio. The ACT domains of GlnD are the protein sensor of environment clues of nitrogen availability. Regulatory role of the ACT domain
physiological function
-
control for PII interaction with target proteins involves the covalent modification of the T-loop, such as uridylylation, phosphorylation or adenylylation. The uridylylation of PII proteins occurs in a conserved residue of tyrosine (Tyr51) in the T-loop. Uridylylation of Tyr51 renders a T-loop more mobile in comparison with the unmodified protein. The PII uridylylation is catalyzed by the GlnD enzyme, which also catalyzes the removal of the uridylyl group from PII. The choice between uridylyl transferase (UTase) and the uridylyl-removing activities (UR) of GlnD is essential to the function of the Ntr system and is supposedly dependent on the in vivo fluctuation of key metabolites. The deuridylylation activity of Herbaspirillum seropedicae GlnD protein is regulated by the glutamine:2-oxoglutarate ratio. GlnD can sense the glutamine:2-oxoglutarate ratio. The ACT domains of GlnD are the protein sensor of environment clues of nitrogen availability. Regulatory role of the ACT domain
-
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D107A
-
large decrease in activity
D107V
-
large decrease in activity
D107Y
-
large decrease in activity
G93L
-
large decrease in activity
G93V
-
large decrease in activity
G94L
-
large decrease in activity
G94V
-
large decrease in activity
H514A/D515A
-
large decrease in activity
H514Q/D515N
-
large decrease in activity
additional information
-
null glnD mutations are introduced into the genome, but can not be stably maintained unless a second mutation is present which results in deregulated glutamine synthetase, for example: spontaneous mutation MV71, probably in gene glnE, adenylyltransferase, and introduced mutation Y407F in gene glnA, glutamine synthetase, can stabilize the glnD null mutation
additional information
deletion mutants of glnD are unstable
additional information
-
deletion mutants of glnD are unstable
additional information
deletion mutant is impaired in its response to nitrogen shortage, mutant shows reduced growth rate in presence of limiting amounts of ammonium or urea, deletion also impairs the transcription of genes amtB and glnK within the same operon
additional information
-
deletion mutant is impaired in its response to nitrogen shortage, mutant shows reduced growth rate in presence of limiting amounts of ammonium or urea, deletion also impairs the transcription of genes amtB and glnK within the same operon
additional information
a GlnKY51F protein mutant strain shows no enzyme expression, irrespective of the nitrogen status
additional information
-
a GlnKY51F protein mutant strain shows no enzyme expression, irrespective of the nitrogen status
additional information
-
the presence of a His tag does not alter PII substrate inhibition of the uridylyltransferase activity and has little effect on the level of the uridylyltransferase activity but results in a slight defect in uridylyl removing activity. At high PII substrate concentrations, glutamine inhibition of the uridylyltransferase activity is incomplete in the enzyme carrying a His tag. In the wild-type enzyme PII brings about substrate inhibition of the uridylyltransferase activity by binding to the central HD domain of the enzyme, and that addition of an N-terminal His tag results in an altered enzyme with subtle changes in the interactions between domains such that binding of PII to the HD domain interferes with glutamine regulation of the uridylyltransferase domain
additional information
-
the uridylyl-removing activity is a property specifically of the central HD domain, substitutions in this domain eliminated uridylyl-removing activity, and a truncated protein lacking the N-terminal domain display uridylyl-removing activity. The deletion of C-terminal ACT domains has little effect on uridylyl-removing activity itself but eliminates the ability of glutamine to stimulate that activity. The deletion of C-terminal ACT domains also dramatically decreases uridylyltransferase activity under all conditions tested
additional information
recombinant production and purification of the uridylylating enzyme GlnD and its use for full uridylylation of large amounts of recombinantly produced pure EcGlnB
additional information
generation of enzyme mutant GlnDDELTAACT. The amplified sequence corresponds to the 1 to 1779 nucleotide according to the Herbaspirillum seropedicae SmRI glnD sequence. This sequence encodes the Herbaspirillum seropedicae GlnD, lacking the last 258 amino acid residues, which corresponds to the two ACT domains. The wild-type GlnD seems more sensible to nucleotides and Mn2+ than the truncated enzyme
additional information
-
generation of enzyme mutant GlnDDELTAACT. The amplified sequence corresponds to the 1 to 1779 nucleotide according to the Herbaspirillum seropedicae SmRI glnD sequence. This sequence encodes the Herbaspirillum seropedicae GlnD, lacking the last 258 amino acid residues, which corresponds to the two ACT domains. The wild-type GlnD seems more sensible to nucleotides and Mn2+ than the truncated enzyme
additional information
-
generation of enzyme mutant GlnDDELTAACT. The amplified sequence corresponds to the 1 to 1779 nucleotide according to the Herbaspirillum seropedicae SmRI glnD sequence. This sequence encodes the Herbaspirillum seropedicae GlnD, lacking the last 258 amino acid residues, which corresponds to the two ACT domains. The wild-type GlnD seems more sensible to nucleotides and Mn2+ than the truncated enzyme
-
additional information
-
construction of several chromosomal glnD mutants, phenotype studies
additional information
mutant construction by transposon Tn5 insertion and by subcloning + double crossover for recombination, phenotype characterization. Mutants are unable to utilize nitrate, essential function of glnD since most mutations close to the 5'-end are lethal
additional information
-
mutation and complementation studies show that the uridylyltransferase activity of the bifunctional uridylyltransferase/uridylyl-removing enzyme GlnD is localized to the N-terminal region
additional information
the uridylyl-removing activity is a property specifically of the central HD domain, substitutions in this domain eliminated uridylyl-removing activity, and a truncated protein lacking the N-terminal domain display uridylyl-removing activity. The deletion of C-terminal ACT domains has little effect on uridylyl-removing activity itself but eliminates the ability of glutamine to stimulate that activity. The deletion of C-terminal ACT domains also dramatically decreases uridylyltransferase activity under all conditions tested
additional information
-
the uridylyl-removing activity is a property specifically of the central HD domain, substitutions in this domain eliminated uridylyl-removing activity, and a truncated protein lacking the N-terminal domain display uridylyl-removing activity. The deletion of C-terminal ACT domains has little effect on uridylyl-removing activity itself but eliminates the ability of glutamine to stimulate that activity. The deletion of C-terminal ACT domains also dramatically decreases uridylyltransferase activity under all conditions tested
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Atkinson, M.R.; Kamberov, E.S.; Weiss, R.L.; Ninfa, A.J.
Reversible uridylylation of the Escherichia coli PII signal transduction protein regulates its ability to stimulate the dephosphorylation of the transcription factor nitrogen regulator I (NRI or NtrC)
J. Biol. Chem.
269
28288-28293
1994
Escherichia coli
brenda
Mura, U.; Ceccherelli, M.; Gini, S.
Growth conditions and inactivation of the uridylation cycle of the glutamine synthetase regulatory system in permeabilized cells of E. coli
Boll. Soc. Ital. Biol. Sper.
58
1152-1157
1982
Escherichia coli
brenda
Garcia, E.; Rhee, S.G.
Cascade control of Escherichia coli glutamine synthetase
J. Biol. Chem.
258
2246-2253
1983
Escherichia coli
brenda
Jaggi, R.; Ybarlucea, W.; Cheah, E.; Carr, P.D.; Edwards, K.J.; Ollis, D.L.; Vasudevan, S.G.
The role of the T-loop of the signal transducing protein PII from Escherichia coli
FEBS Lett.
391
223-228
1996
Escherichia coli
brenda
Rhee, S.G.; Huang, C.Y.; Chock, P.B.; Stadtman, E.R.
New methods for the colorimetric assay of PIII regulatory protein, uridylyltransferase, and uridylyl-removing enzyme in glutamine synthetase cascade
Anal. Biochem.
90
752-766
1978
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Edwards, R.; Merrick, M.
The role of uridylyltransferase in the control of Klebsiella pneumoniae nif gene regulation
Mol. Gen. Genet.
247
189-198
1995
Klebsiella pneumoniae
brenda
Johansson, M.; Nordlund, S.
Uridylylation of the PII protein in the photosynthetic bacterium Phodospirillum rubrum
J. Bacteriol.
179
4190-4194
1997
Rhodospirillum rubrum
brenda
Jiang, P.; Peliska, J.A.; Ninfa, A.J.
Reconstitution of the signal-transduction bicyclic cascade responsible for the regulation of ntr gene transcription in Escherichia coli
Biochemistry
37
12795-12801
1998
Escherichia coli
brenda
Francis, S.H.; Engleman, E.G.
Cascade control of E. coli glutamine synthetase. I. Studies on the uridylyl transferase and uridylyl removing enzyme(s) from E. coli
Arch. Biochem. Biophys.
191
590-601
1978
Escherichia coli
brenda
Engleman, E.G.; Francis, S.H.
Cascade control of E. coli glutamine synthetase. II. Metabolite regulation of the enzymes in the cascade
Arch. Biochem. Biophys.
191
602-612
1978
Escherichia coli
brenda
van Heeswijk, W.C.; Rabenberg, M.; Westerhoff, H.V.; Kahn, D.
The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli
Mol. Microbiol.
9
443-457
1993
Escherichia coli (P27249)
brenda
Colonna-Romano, S.; Patriarca, E.J.; Amar, M.; Bernard, P.; Manco, G.; Lamberti, A.; Iaccarino, M.; Defez, R.
Uridylylation of the PII protein in Rhizobium leguminosarum
FEBS Lett.
330
95-98
1993
Rhizobium leguminosarum
brenda
Atkinson, M.R.; Ninfa, A.J.
Characterization of the GlnK protein of Escherichia coli
Mol. Microbiol.
32
301-313
1999
Escherichia coli
brenda
Jakoby, M.; Kramer, R.; Burkovski, A.
Nitrogen regulation in Corynebacterium glutamicum: isolation of genes involved and biochemical characterization of corresponding proteins
FEMS Microbiol. Lett.
173
303-310
1999
Corynebacterium glutamicum (Q9X706), Corynebacterium glutamicum
brenda
Schlter, A.; Nohlen, M.; Kramer, M.; Defez, R.; Priefer, U.B.
The Rhizobium leguminosarum bv. viciae glnD gene, encoding a uridylyltransferase/uridylyl-removing enzyme, is expressed in the root nodule but is not essential for nitrogen fixation
Microbiology
146
2987-2996
2000
Rhizobium leguminosarum (Q9RAE4)
-
brenda
Nolden, L.; Ngouoto-Nkili, C.E.; Bendt, A.K.; Kramer, R.; Burkovski, A.
Sensing nitrogen limitation in Corynebacterium glutamicum: the role of glnK and glnD
Mol. Microbiol.
42
1281-1295
2001
Corynebacterium glutamicum (Q9X706), Corynebacterium glutamicum
brenda
Mutalik, V.K.; Shah, P.; Venkatesh, K.V.
Allosteric interactions and bifunctionality make the response of glutamine synthetase cascade system of Escherichia coli robust and ultrasensitive
J. Biol. Chem.
278
26327-26332
2003
Escherichia coli
brenda
Colnaghi, R.; Rudnick, P.; He, L.; Green, A.; Yan, D.; Larson, E.; Kennedy, C.
Lethality of glnD null mutations in Azotobacter vinelandii is suppressible by prevention of glutamine synthetase adenylylation
Microbiology
147
1267-1276
2001
Azotobacter vinelandii
brenda
Zhang, Y.; Pohlmann, E.L.; Roberts, G.P.
GlnD is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity in the photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum
J. Bacteriol.
187
1254-1265
2005
Rhodospirillum rubrum
brenda
Jonsson, A.; Nordlund, S.
In vitro studies of the uridylylation of the three PII protein paralogs from Rhodospirillum rubrum: the transferase activity of R. rubrum GlnD is regulated by alpha-ketoglutarate and divalent cations but not by glutamine
J. Bacteriol.
189
3471-3478
2007
Rhodospirillum rubrum, Rhodospirillum rubrum S1
brenda
Bonatto, A.C.; Couto, G.H.; Souza, E.M.; Araujo, L.M.; Pedrosa, F.O.; Noindorf, L.; Benelli, E.M.
Purification and characterization of the bifunctional uridylyltransferase and the signal transducing proteins GlnB and GlnK from Herbaspirillum seropedicae
Protein Expr. Purif.
55
293-299
2007
Herbaspirillum seropedicae
brenda
Araujo, L.M.; Huergo, L.F.; Invitti, A.L.; Gimenes, C.I.; Bonatto, A.C.; Monteiro, R.A.; Souza, E.M.; Pedrosa, F.O.; Chubatsu, L.S.
Different responses of the GlnB and GlnZ proteins upon in vitro uridylylation by the Azospirillum brasilense GlnD protein
Braz. J. Med. Biol. Res.
41
289-294
2008
Azospirillum brasilense (Q8RQD1), Azospirillum brasilense
brenda
Bonatto, A.C.; Souza, E.M.; Oliveira, M.A.; Monteiro, R.A.; Chubatsu, L.S.; Huergo, L.F.; Pedrosa, F.O.
Uridylylation of Herbaspirillum seropedicae GlnB and GlnK proteins is differentially affected by ATP, ADP and 2-oxoglutarate in vitro
Arch. Microbiol.
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643-652
2012
Herbaspirillum seropedicae (D8IU13)
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Jiang, P.; Zhang, Y.; Atkinson, M.R.; Ninfa, A.J.
The robustness of the Escherichia coli signal-transducing UTase/UR-PII covalent modification cycle to variation in the PII concentration requires very strong inhibition of the UTase activity of UTase/UR by glutamine
Biochemistry
51
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2012
Escherichia coli
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Zhang, Y.; Pohlmann, E.L.; Serate, J.; Conrad, M.C.; Roberts, G.P.
Mutagenesis and functional characterization of the four domains of GlnD, a bifunctional nitrogen sensor protein
J. Bacteriol.
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2010
Escherichia coli, Rhodospirillum rubrum (Q2RNG2), Rhodospirillum rubrum
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Yurgel, S.N.; Rice, J.; Kahn, M.L.
Nitrogen metabolism in Sinorhizobium meliloti-alfalfa symbiosis: dissecting the role of GlnD and PII proteins
Mol. Plant Microbe Interact.
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2012
Sinorhizobium meliloti (P56884), Sinorhizobium meliloti
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Williams, K.J.; Bennett, M.H.; Barton, G.R.; Jenkins, V.A.; Robertson, B.D.
Adenylylation of mycobacterial Glnk (PII) protein is induced by nitrogen limitation
Tuberculosis
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2013
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Mycolicibacterium smegmatis (A0QV29), Mycolicibacterium smegmatis ATCC 700084 (A0QV29)
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Emori, M.T.; Tomazini, L.F.; Souza, E.M.; Pedrosa, F.O.; Chubatsu, L.S.; Oliveira, M.A.S.
The deuridylylation activity of Herbaspirillum seropedicae GlnD protein is regulated by the glutamine 2-oxoglutarate ratio
Biochim. Biophys. Acta
1866
1216-1223
2018
Herbaspirillum seropedicae (D8IU13), Herbaspirillum seropedicae, Herbaspirillum seropedicae SmR1 (D8IU13)
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Palanca, C.; Rubio, V.
Effects of T-loop modification on the PII-signalling protein structure of uridylylated Escherichia coli GlnB bound to ATP
Environ. Microbiol. Rep.
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290-299
2017
Escherichia coli (P27249)
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Kukolj, C.; Pedrosa, F.O.; de Souza, G.A.; Sumner, L.W.; Lei, Z.; Sumner, B.; do Amaral, F.P.; Juexin, W.; Trupti, J.; Huergo, L.F.; Monteiro, R.A.; Valdameri, G.; Stacey, G.; de Souza, E.M.
Proteomic and metabolomic analysis of Azospirillum brasilense ntrC mutant under high and low nitrogen conditions
J. Proteome Res.
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2020
Azospirillum brasilense (Q8RQD1), Azospirillum brasilense FP2 (Q8RQD1)
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