Information on EC 2.7.7.59 - [protein-PII] uridylyltransferase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
2.7.7.59
-
RECOMMENDED NAME
GeneOntology No.
[protein-PII] uridylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]
show the reaction diagram
The enzyme uridylates and de-uridylates the small trimeric protein PII
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
uridylylation
-, Q8RQD1
-
SYSTEMATIC NAME
IUBMB Comments
UTP:[protein-PII] uridylyltransferase
The enzyme uridylylates and de-uridylylates the small trimeric protein PII. The enzymes from Escherichia coli and Salmonella typhimurium have been wrongly identified, in some databases, as EC 2.7.7.12 (UDP-glucose---hexose-1-phosphate uridylyltransferase), from which it differs greatly in both reaction catalysed and sequence.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
GlnD
Mycobacterium smegmatis ATCC 700084
A0QV29
-
-
GlnD
-
bifunctional uridylyltransferase/uridylyl-removing enzyme
GlnD
-
the bifunctional uridylyltransferase/uridylyl-removing enzyme is coded by the glnD gene in Rhodospirillum rubrum
GlnD
Rhodospirillum rubrum S1
-
the bifunctional uridylyltransferase/uridylyl-removing enzyme is coded by the glnD gene in Rhodospirillum rubrum
-
GlnD protein
Q8RQD1
-
PII uridylyl-transferase
-
-
-
-
PII uridylyltransferase
-
-
-
-
PII uridylyltransferase (Escherichia coli gene glnD)
-
-
-
-
uridyl removing enzyme
-
-
-
-
uridyltransferase, glutamine synthetase adenylyltransferase-regulating protein
-
-
-
-
uridylyl removing enzyme
-
-
-
-
uridylyl-removing enzyme
Q8RQD1
-
uridylyltransferase
Q8RQD1
-
uridylyltransferase
-
-
uridylyltransferase enzyme
-
-
uridylyltransferase enzyme
Rhodospirillum rubrum S1
-
-
-
uridylyltransferase, glutamine synthetase adenylyltransferase-regulating protein (Escherichia coli clone 21C8 gene glnD reduced)
-
-
-
-
uridylyltransferase/uridylyl removing enzyme
-
-
-
-
uridylyltransferase/uridylyl-removing enzyme
-
-
-
-
uridylyltransferase/uridylyl-removing enzyme
-
-
UTase/UR
-
-
-
-
UTase/UR
-
-
UTP:PII protein uridylyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
151596-34-8
Escherichia coli clone 21C8 gene glnD reduced
57657-57-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
expression is upregulated upon nitrogen limitation
SwissProt
Manually annotated by BRENDA team
gene glnD within the isolated glnB gene cluster
SwissProt
Manually annotated by BRENDA team
bifunctional uridylyltransferase/uridylyl-removing enzyme
-
-
Manually annotated by BRENDA team
gene glnD
-
-
Manually annotated by BRENDA team
gene glnD
SwissProt
Manually annotated by BRENDA team
Mycobacterium smegmatis ATCC 700084
putative
UniProt
Manually annotated by BRENDA team
bv. viciae, constitutive gene glnD; from root nodules of Vicia hirsuta
SwissProt
Manually annotated by BRENDA team
bifunctional uridylyltransferase/uridylyl-removing enzyme
UniProt
Manually annotated by BRENDA team
Rhodospirillum rubrum S1
S1
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti Rm1021
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
P56884, -
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
Sinorhizobium meliloti Rm1021
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UTP + GlnB
diphosphate + uridylyl-GlnB
show the reaction diagram
-
-
-
-
r
UTP + GlnB
diphosphate + uridylyl-GlnB
show the reaction diagram
-, Q8RQD1
-
-
-
r
UTP + GlnB
diphosphate + uridylyl-GlnB
show the reaction diagram
D8IU13
-
-
-
?
UTP + GlnB
diphosphate + uridylyl-GlnB
show the reaction diagram
Q2RNG2
-
-
-
r
UTP + GlnK
diphosphate + uridylyl-GlnK
show the reaction diagram
D8IU13
-
-
-
?
UTP + GlnZ
diphosphate + uridylyl-GlnZ
show the reaction diagram
-, Q8RQD1
-
-
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
-
-
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
-, Q9X706
GlnK protein mutant Y51F is no substrate
-
?
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
-
regulatory protein, GlnK protein mutant Y51N is no substrate, very slow reverse reaction, GlnK protein wild-type and mutant R47W
-
ir
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
-
enzyme is pivotal in sensing intracellular levels of fixed nitrogen
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
-, Q9X706
uridylylation of GlnK protein is essential for the cell to respond to nitrogen limitation
-
?
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
-
enzyme regulates the regulatory GlnK protein
-
ir
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
P27249
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-, Q9X706
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-, Q9X706
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
Q9RAE4
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
mutants Y51F and Y51S are no substrates, Y46F is a poor substrate, structure analysis of the crystallized protein PII variants, Tyr51 is the site of uridylation
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the uridylylation of the PII protein is modulated by the intracellular glutamine/alpha-ketoglutarate ratio
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-, Q9X706
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]
show the reaction diagram
-
enzyme is pivotal in sensing intracellular levels of fixed nitrogen
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
signal transduction cascade model
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-, Q9X706
signal transduction cascade model
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
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]
show the reaction diagram
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
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]
show the reaction diagram
-
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]
show the reaction diagram
-
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]
show the reaction diagram
Q9RAE4
enzyme is not essential for nitrogen fixation of the host plant
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-, Q9X706
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
Q9RAE4
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
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]
show the reaction diagram
P27249
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]
show the reaction diagram
-
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]
show the reaction diagram
-
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]
show the reaction diagram
-
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]
show the reaction diagram
Rhodospirillum rubrum S1
-
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
additional information
?
-
-
regulation, enzyme is required for the relief of NifL inhibition of NifA under N-limiting conditions
-
-
-
additional information
?
-
-
schematic regulation model
-
-
-
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
?
-
A0QV29
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. 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
?
-
Mycobacterium smegmatis ATCC 700084
A0QV29
PII protein GlnK is adenylylated by GlnD in response to nitrogen limitation
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UTP + GlnB
diphosphate + uridylyl-GlnB
show the reaction diagram
-, Q8RQD1
-
-
-
r
UTP + GlnZ
diphosphate + uridylyl-GlnZ
show the reaction diagram
-, Q8RQD1
-
-
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
-
enzyme is pivotal in sensing intracellular levels of fixed nitrogen
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
-, Q9X706
uridylylation of GlnK protein is essential for the cell to respond to nitrogen limitation
-
?
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
-
enzyme regulates the regulatory GlnK protein
-
ir
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the uridylylation of the PII protein is modulated by the intracellular glutamine/alpha-ketoglutarate ratio
-
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-, Q9X706
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]
show the reaction diagram
-
enzyme is pivotal in sensing intracellular levels of fixed nitrogen
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
signal transduction cascade model
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-, Q9X706
signal transduction cascade model
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
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]
show the reaction diagram
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme is involved in the cascade control of glutamine synthetase
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
-
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
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]
show the reaction diagram
-
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]
show the reaction diagram
-
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]
show the reaction diagram
Q9RAE4
enzyme is not essential for nitrogen fixation of the host plant
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-, Q9X706
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
Q9RAE4
the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
-
-
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
-
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]
show the reaction diagram
P27249
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]
show the reaction diagram
-
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
-
-
?
additional information
?
-
-
regulation, enzyme is required for the relief of NifL inhibition of NifA under N-limiting conditions
-
-
-
additional information
?
-
-
schematic regulation model
-
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
uridylylation assay with 100 mM KCl
Mg2+
-
uridylylation assay with 25 mM Mg2+
Mg2+
-
or Mn2+, required. Enzyme shows more than 5fold higher uridylyl-removing activity in presence of Mn2+ than with Mg2+
Mn2+
-
supports activity
Mn2+
-
highest degree of uridylylation at 3 mM MnCl2
Mn2+
-
or Mn2+, required. Enzyme shows more than 5fold higher uridylyl-removing activity in presence of Mn2+ than with Mg2+
NH4+
-, Q8RQD1
uridylylation in response to the concentration of ammonium ions
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
glutamine
-
shows an inhibition of 65% of GlnB uridylylation and 70% of GlnK uridylylation
glutamine
-, Q8RQD1
-
glutamine
-
inhibition of uridylyltransferase activity
GMP
-
inhibits uridylyl removing activity
GTP
-
inhibits uridylyl removing activity
IDP
-
inhibits uridylyl removing activity
IMP
-
inhibits uridylyl removing activity
iodoacetamide
-
-
iodoacetate
-
-
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
PCMB
-
inactivation
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
UTP
-
inhibits uridylyl removing activity
Zn2+
-
inhibits uridylyl removing activity
ITP
-
inhibits uridylyl removing activity
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
at low concentration, required for PII uridylylation
2-oxoglutarate
-
required compound, uridylylation assay with 5 mM 2-oxoglutarate
2-oxoglutarate
-, Q8RQD1
-
2-oxoglutarate
D8IU13
maximum uridylylation rates for both PII proteins GlnB and GlnK are observed in the presence of about 2 mM 2-oxoglutarate and 200500 microM ATP. Uridylylation of both GlnB and GlnK responds to 2-oxoglutarate levels, but only GlnB responds effectively to variation on ADP/ATP ratio
ADP
D8IU13
or ATP, absolutely required for in vitro uridylylation of PII proteins GlnB and GlnK. Maximum uridylylation rates for both proteins are observed in the presence of about 2 mM 2-oxoglutarate and 200-500 microM ATP. Uridylylation of both GlnB and GlnK responds to 2-oxoglutarate levels, but only GlnB responds effectively to variation on ADP/ATP ratio
AMP
D8IU13
may partially replace ATP or ADP
ATP
-
required for uridylylation
ATP
-
required compound, uridylylation assay with 0.2 mM ATP
ATP
D8IU13
or ADP, absolutely required for in vitro uridylylation of PII proteins GlnB and GlnK. Maximum uridylylation rates for both proteins are observed in the presence of about 2 mM 2-oxoglutarate and 200-500 microM ATP. Uridylylation of both GlnB and GlnK responds to 2-oxoglutarate levels, but only GlnB responds effectively to variation on ADP/ATP ratio
glutamine
-
5 mM, no effect at pH 8.6; pH 7.6, enhances uridylyl removing activity at 0.5 mM
L-glutamine
-
stimulates the deuridylylation reaction but in contrast to Escherichia coli glutamine has no effect on the uridylylation reaction
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
steady state model for quantification of sensitivity of glutamine synthetase cascade regulation system system, kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
7.5
-
-, Q8RQD1
in vitro uridylylation
7.6
-
-
uridylyltransferase activity
7.6
-
-
assay at
8.6
-
-
uridylyl-removing activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-, Q8RQD1
in vitro uridylylation
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q9RAE4
enzyme expression
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
94000
-
-
monomeric enzyme form, HPLC gel filtration
105000
-
-
deduced from the gene sequence
140000
-
-
gel filtration
186000
-
-
dimeric enzyme form, HPLC gel filtration
550000
-
-
hexameric form, HPLC gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 94000, the enzyme is detected as monomeric, dimeric and hexameric form, HPLC after equilibration with SDS
hexamer
-
6 * 94000, the enzyme is detected as monomeric, dimeric and hexameric form, HPLC after equilibration with SDS
monomer
-
1 * 94000, the enzyme is detected as monomeric, dimeric and hexameric form, HPLC after equilibration with SDS
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing and thawing of the purified enzyme results in 35-50% loss of activity
-
purification drastically reduces enzyme stability
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, several months without loss of activity
-
4C, purified enzyme, in presence of ATP and 0.2 M KCl, 10 h, loss of 15-20% activity compared to storage conditions at -5C
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
on a Hi-trap-chelating-Ni2+ column
-, Q8RQD1
1720fold to homogeneity from recombinant overexpressing strain
-
GlnD is less soluble than the purified PII proteins GlnB or GlnK, to improve solubility of GlnD a special buffer is utilised (50 mM Tris-HCl, pH 7.0, 200 mM NaCl, 1 mM DTT) which produces 50% solubilization; protein is purified by anionic exchange chromatography (DEAE-Sepharose column) and gel chromatography (Agarose-Heparin column)
-
GlnD is expressed as a GST-fusion protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
into the vector pET28a for expression in Escherichia coli cells
-, Q8RQD1
expression of glnD in a deficient mutant strain restores the constitutive enzyme, complementation; gene glnD, construction of chromosomal deletion mutant
-, Q9X706
gene glnD, DNA sequence determination and analysis
-, Q9X706
expression in Escherichia coli
-
gene glnD, DNA and amino acid sequence determination and analysis, chromosome mapping, overexpression and functional complementation in Escherichia coli strain DH5
P27249
gene glnD, overexpression from plasmid in an Escherichia coli strain
-
expression in Echerichia coli RB9065lambdaDE3
-
DNA sequence determination and analysis, overexpression in Escherichia coli strain JM109
-
DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli, recombination of mutant gene into genomic glnD region via double crossover, mutnat VF39-BB3 and VF39-BB1
Q9RAE4
cloned in Escherichia coli strain RB 9040
-
expression in Escherichia coli
Q2RNG2
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
-, Q9X706
deletion mutants of glnD are unstable
additional information
-, Q9X706
a GlnKY51F protein mutant strain shows no enzyme expression, irrespective of the nitrogen status; 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
H514Q/D515N
-
large decrease in activity
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
-
construction of several chromosomal glnD mutants, phenotype studies
additional information
Q9RAE4
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
Q2RNG2
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