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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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Sulfurisphaera tokodaii
UNIPROT: Q975F9 not found.
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The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-glucose pyrophosphorylase, ugpase, udpg-pyrophosphorylase, udpgp, udp-glc pyrophosphorylase, udpglucose pyrophosphorylase, glucose-1-phosphate uridylyltransferase, udpg pyrophosphorylase, utp-glucose-1-phosphate uridylyltransferase, uridine diphosphoglucose pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ST0452
STK_04520
locus name
sugar-1-phosphate nucleotidylyltransferase
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glucose 1-phosphate uridylyltransferase
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glucose-1-phosphate uridylyltransferase
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UDP glucose pyrophosphorylase
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-
-
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UDP-glucose pyrophosphorylase
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-
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UDPG phosphorylase
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-
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UDPG pyrophosphorylase
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-
-
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UDPglucose pyrophosphorylase
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-
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uridine 5'-diphosphoglucose pyrophosphorylase
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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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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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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
UDP + alpha-D-glucose 1-phosphate
phosphate + UDP-glucose
show the reaction diagram
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
show the reaction diagram
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
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
UDP + alpha-D-glucose 1-phosphate
phosphate + UDP-glucose
show the reaction diagram
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
show the reaction diagram
-
-
-
?
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
0.66
mutant enzyme Y97D, pH 7.5, 80°C
0.98
mutant enzyme Y97G, pH 7.5, 80°C
1.03
mutant enzyme Y97T, pH 7.5, 80°C
1.09
mutant enzyme Y97K, pH 7.5, 80°C
1.22
mutant enzyme Y97V, pH 7.5, 80°C
1.57
pH 7.5, 80°C, substrates: UTP + alpha-D-glucose 1-phosphate
1.74
mutant enzyme Y97A, pH 7.5, 80°C
10.41
mutant enzyme Y97H, pH 7.5, 80°C
11.45
mutant enzyme Y97M, pH 7.5, 80°C
16.92
mutant enzyme Y97N, pH 7.5, 80°C
2
pH 7.5, 80°C, mutant enzyme DC05 (deletion of the C-terminal 5 residues of the ST0452 protein)
2.18
mutant enzyme Y97C, pH 7.5, 80°C
2.2
pH 7.5, 80°C, wild-type enzyme enzyme
2.6
pH 7.5, 80°C, mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein)
3.35
mutant enzyme Y97F, pH 7.5, 80°C
4.08
wild-type enzyme, pH 7.5, 80°C
4.26
mutant enzyme Y97Q, pH 7.5, 80°C
4.51
mutant enzyme Y97S, pH 7.5, 80°C
7.48
pH 7.5, 80°C, substrates: diphosphate + UDP-alpha-D-glucose
9.97
mutant enzyme Y97L, pH 7.5, 80°C
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
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
additional information
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 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. 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 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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
His SpinTrap Talon column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells
expressed in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
expression in Escherichia coli
expression in Escherichia coli, wild-type and truncated enzyme form lacking the 170-residues C-terminal domain
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, Sulfurisphaera tokodaii DSM 16993 (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
e02291-16
2017
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Manually annotated by BRENDA team