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Information on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase and Organism(s) Sulfurisphaera tokodaii and UniProt Accession Q975F9

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This record set is specific for:
Sulfurisphaera tokodaii
UNIPROT: Q975F9 not found.
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
Synonyms
All3274, CugP, cyanobacterial UDP-Glc PPase, ExoN, GalU, Glc-1-P UTase, GlcNAc-1-P UTase, glucose 1-phosphate uridylyltransferase, glucose-1-phosphate uridylyltransferase, plastid UDP-glucose pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glc-1-P UTase
299945
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GlcNAc-1-P UTase
299945
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glucose 1-phosphate uridylyltransferase
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glucose-1-phosphate uridylyltransferase
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ST0452
ST0452 protein
299945
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STK_04520
299945
locus name
UDP glucose pyrophosphorylase
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UDP-glucose pyrophosphorylase
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UDPG phosphorylase
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UDPG pyrophosphorylase
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UDPglucose pyrophosphorylase
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-
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uridine 5'-diphosphoglucose pyrophosphorylase
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-
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uridine diphosphate-D-glucose pyrophosphorylase
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uridine diphosphoglucose pyrophosphorylase
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uridine-diphosphate glucose pyrophosphorylase
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uridylyltransferase, glucose 1-phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
UTP:alpha-D-glucose-1-phosphate uridylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-22-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
show the reaction diagram
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-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
the multifunctional enzyme also shows activity with UTP + alpha-D-glucose 1-phosphate (EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase), dTTP + N-acetylglucosamine 1-phosphate (N-acetylglucosamine 1-phosphate thymidylyltransferase), dCTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate cytidylyltransferase), dGTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate guanylyltransferase), dATP + alpha-D-glucose 1-phosphate (glucose-1-phosphate adenylyltransferase). No activity with: alpha-D-glucose 1-phosphate + dATP, alpha-D-glucose 1-phosphate + dCTP, alpha-D-glucose 1-phosphate + dGTP, UTP + alpha-D-mannose1-phosphate, UTP + alpha-D-galactose 1-phosphate, UTP + alpha-D-glucosamine 1-phosphate
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
show the reaction diagram
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-
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.23 - 3.28
alpha-D-glucose 1-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.08 - 38.15
alpha-D-glucose 1-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.63 - 15.08
alpha-D-glucose 1-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.57
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pH 7.5, 80C, substrates: UTP + alpha-D-glucose 1-phosphate
2
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pH 7.5, 80C, mutant enzyme DC05 (deletion of the C-terminal 5 residues of the ST0452 protein)
2.2
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pH 7.5, 80C, wild-type enzyme enzyme
2.6
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pH 7.5, 80C, mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein)
7.48
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pH 7.5, 80C, substrates: diphosphate + UDP-alpha-D-glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
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the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y97A
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specific Glc-1-P UTase activity of the mutant enzyme is 2.3fold lower than the specific activity of the mutant enzyme
Y97C
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specific Glc-1-P UTase activity of the mutant enzyme is 1.9fold lower than the specific activity of the mutant enzyme
Y97D
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specific Glc-1-P UTase activity of the mutant enzyme is 6.2fold lower than the specific activity of the mutant enzyme
Y97E
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mutant enzyme shows mutant enzyme shows no activity
Y97F
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specific Glc-1-P UTase activity of the mutant enzyme is 1.2fold lower than the specific activity of the mutant enzyme
Y97G
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specific Glc-1-P UTase activity of the mutant enzyme is 4.2fold lower than the specific activity of the mutant enzyme
Y97H
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specific Glc-1-P UTase activity of the mutant enzyme is 2.6fold higher than the specific activity of the mutant enzyme
Y97I
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mutant enzyme shows no activity
Y97K
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specific Glc-1-P UTase activity of the mutant enzyme is 3.7fold lower than the specific activity of the mutant enzyme
Y97L
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specific Glc-1-P UTase activity of the mutant enzyme is 2.4fold higher than the specific activity of the mutant enzyme
Y97M
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specific Glc-1-P UTase activity of the mutant enzyme is 2.8fold higher than the specific activity of the mutant enzyme
Y97N
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specific Glc-1-P UTase activity of the mutant enzyme is 4.1fold higher than the specific activity of the mutant enzyme
Y97Q
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specific Glc-1-P UTase activity of the mutant enzyme is 1.04fold higher than the specific activity of the mutant enzyme
Y97R
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mutant enzyme shows no activity
Y97S
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specific Glc-1-P UTase activity of the mutant enzyme is 1.1fold higher than the specific activity of the mutant enzyme
Y97T
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specific Glc-1-P UTase activity of the mutant enzyme is 4fold lower than the specific activity of the mutant enzyme
Y97V
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specific Glc-1-P UTase activity of the mutant enzyme is 3.34fold lower than the specific activity of the mutant enzyme
Y97W
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mutant enzyme shows no activity
additional information
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the UTP-glucose-1-phosphate uridylyltransferase activity of mutant enzyme DC005 is reduced by 10%, as compared to that of the wild-type ST0452 protein, while the activity of DC011 is increased by 18%, indicating that the enzymatic activity in the N-terminal region is not greatly affected by truncation of the C-terminal 5 or 11 residues. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability at 80C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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mutant enzyme DC005 shows the same thermostability as wild-type ST0452 protein, whereas mutant enzyme DC011 denatures and becomes insoluble form by 5-min treatment at 80 C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
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expression in Escherichia coli, wild-type and truncated enzyme form lacking the 170-residues C-terminal domain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Z.; Tsujimura, M.; Akutsu, J.; Sasaki, M.; Tajima, H.; Kawarabayasi, Y.
Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7
J. Biol. Chem.
280
9698-9705
2005
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii 7 (Q975F9)
Manually annotated by BRENDA team
Zhang, Z.; Shimizu, Y.; Kawarabayasi, Y.
Characterization of the amino acid residues mediating the unique amino-sugar-1-phosphate acetyltransferase activity of the archaeal ST0452 protein
Extremophiles
19
417-427
2015
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii 7 (Q975F9)
Manually annotated by BRENDA team
Honda, Y.; Zang, Q.; Shimizu, Y.; Dadashipour, M.; Zhang, Z.; Kawarabayasi, Y.
Increasing the thermostable sugar-1-phosphate nucleotidylyltransferase activities of the archaeal ST0452 protein through site saturation mutagenesis of the 97th amino acid position
Appl. Environ. Microbiol.
83
e02291
2017
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Manually annotated by BRENDA team
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