Information on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase

New: Word Map on EC 2.7.7.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.7.7.9
-
RECOMMENDED NAME
GeneOntology No.
UTP-glucose-1-phosphate uridylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
Biosynthesis of antibiotics
-
-
degradation of hexoses
-
-
Galactose metabolism
-
-
glycogen biosynthesis
-
-
Metabolic pathways
-
-
Pentose and glucuronate interconversions
-
-
stachyose degradation
-
-
Starch and sucrose metabolism
-
-
sucrose biosynthesis II
-
-
sucrose degradation II (sucrose synthase)
-
-
UDP-glucose biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
UTP:alpha-D-glucose-1-phosphate uridylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-22-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Neff
-
-
Manually annotated by BRENDA team
Acetabularia sp.
-
-
-
Manually annotated by BRENDA team
var. Landsberg erecta, gene UGP1, a sucrose-induced gene
-
-
Manually annotated by BRENDA team
isolated from sea mud
-
-
Manually annotated by BRENDA team
isolated from sea mud
-
-
Manually annotated by BRENDA team
sugar beet
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pigeon
-
-
Manually annotated by BRENDA team
in addition to UGPase, presence of dual substrate UDP-hexose pyrophosphorylase
SwissProt
Manually annotated by BRENDA team
cv. Calypiso
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Golgi apparatus and cytosolic isozyme
-
-
Manually annotated by BRENDA team
strain 26 695
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
lamb
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isoforms UGP1, UGP2
-
-
Manually annotated by BRENDA team
Saccharomyces fragilis
galactose-adopted
-
-
Manually annotated by BRENDA team
cv. Rox Orange
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
subsp. zooepidemicus. i.e. Streptococcus zooepidemicus
UniProt
Manually annotated by BRENDA team
strain KCCM 11405, recombinant protein. Enzyme is part of the validamycin A biosynthetic pathway
-
-
Manually annotated by BRENDA team
strain KCCM 11405, recombinant protein. Enzyme is part of the validamycin A biosynthetic pathway
-
-
Manually annotated by BRENDA team
strain LY03
-
-
Manually annotated by BRENDA team
strain LY03
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
wild-type and mutant RN-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
Q4UVD0
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
show the reaction diagram
-
13.7% of the activity with UTP
-
r
diphosphate + CDP-glucose
CTP + alpha-D-glucose 1-phosphate
show the reaction diagram
diphosphate + GDP-glucose
GTP + alpha-D-glucose 1-phosphate
show the reaction diagram
diphosphate + TDP-glucose
TTP + alpha-D-glucose 1-phosphate
show the reaction diagram
diphosphate + UDP-galactose
UTP + alpha-D-galactose 1-phosphate
show the reaction diagram
-
-
-
r
diphosphate + UDP-glucose
UTP + alpha-D-glucose 1-phosphate
show the reaction diagram
diphosphate + UDP-mannose
UTP + D-mannose 1-phosphate
show the reaction diagram
diphosphate + UDP-xylose
UTP + D-xylose 1-phosphate
show the reaction diagram
farnesyl triphosphate + UDP-glucose
farnesyl-tetraphosphouridine + alpha-D-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
geranyl triphosphate + UDP-glucose
geranyl-tetraphosphouridine + alpha-D-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
isopentenyl triphosphate + UDP-glucose
isopentenyl-tetraphosphouridine + alpha-D-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
methylenebisphosphonate + UDP-glucose
uridine 5'-(beta,gamma-methylenetriphosphate) + alpha-D-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
monothiodiphosphate + UDP-glucose
UTPbeta,gammaS + alpha-D-glucose 1-phosphate
show the reaction diagram
-
poor substrate, 4.8% of Vmax with diphosphate
UTPbeta,gammaS is chemically unstable and undergoes hydrolysis to UDPbetaS and phosphate, which renders the otherwise reversible reaction irreversible, t1/2 at 25C: 0.5 min
ir
TTP + alpha-D-glucose 1-phosphate
TDP-glucose + diphosphate
show the reaction diagram
UDP-glucose + adenosine 5'-tetraphosphate
D-glucose-1-phosphate + adenosyl-5'-pentaphospho-5'-uridine
show the reaction diagram
-
-
-
-
?
UDP-glucose + ATP
D-glucose-1-phosphate + adenosyl-5'-tetraphospho-5'-uridine
show the reaction diagram
-
-
-
-
?
UDP-glucose + CTP
D-glucose-1-phosphate + cytidinyl-5'-tetraphospho-5'-uridine
show the reaction diagram
-
-
-
-
?
UDP-glucose + GTP
D-glucose-1-phosphate + guanosyl-5'-tetraphospho-5'-uridine
show the reaction diagram
-
-
-
-
?
UDP-glucose + guanosine 5'-tetraphosphate
D-glucose-1-phosphate + guanosyl-5'-pentaphospho-5'-uridine
show the reaction diagram
-
-
-
-
?
UDP-glucose + tetrapolyphosphate
uridine-5'-pentaphosphate + D-glucose-1-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + tripolyphosphate
uridine-5'-tetraphosphate + D-glucose-1-phosphate
show the reaction diagram
-
-
-
-
?
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-galactose
show the reaction diagram
UTP + alpha-D-glucose 1-phosphate
diphosphate + alpha-UDP-glucose
show the reaction diagram
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
UTP + D-glucose-1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
-
?
UTP + D-glucose-1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
UTP + glucose-1-phosphate
UDP-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + alpha-UDP-glucose
show the reaction diagram
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Magnesium
Q6M6R3
crystallization data, two magnesium ions coordinate to UDP-glucose. Magnesium is involved in catalytic mechanism
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phosphoglycerate
-
no inhibition of UDP-glucose synthesis
alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate
D-fructose 2,6-bisphosphate
-
no inhibition of UDP-glucose synthesis
D-fructose 6-phosphate
-
-
D-galactosamine
-
-
D-galactose 6-phosphate
-
UDP-glucose pyrophosphorolysis
diphosphate
iodoacetamide
-
wild-type: loss of 56% activity after 30 min at 0.1 mM, mutant C123S is not affected
Mg-diphosphate
MgUTP
-
wild-type and mutants C123S, H266R, W218, R389H, R422Q, R445H
MgUTP2-
Mn2+
-
in excess of diphosphate-concentration, activates at lower concentrations
phosphate
Sucrose
-
54% inhibition at 2%
TDP-glucose
-
-
TDP-rhamnose
-
-
UDP-D-mannose
UDP-galactose
UDP-galacturonic acid
UDP-glucose
UDP-glucuronic acid
UDP-mannose
UDP-xylose
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
3-phosphoglycerate
-
slight activation
Co2+
-
no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
D-erythrose 4-phosphate
-
slight activation
D-fructose 6-phosphate
-
slight activation
dithiothreitol
-
increases wild-type activity by about 25%
DTT
-
requirement
Sucrose
-
activates; inducible by
Triton X-100
-
activation, only membrane-bound Golgi-enzyme
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
alpha-D-galactose 1-phosphate
-
pH 7.5, temperature not specified in the publication
0.01 - 1
alpha-D-glucose 1-phosphate
0.19 - 0.83
D-glucose-1-phosphate
0.027 - 60
diphosphate
0.32
farnesyl triphosphate
-
pH 8.0, 30C
0.21
geranyl triphosphate
-
pH 8.0, 30C
0.51
isopentenyl triphosphate
-
pH 8.0, 30C
1.1
methylenebisphosphonate
-
pH 8.0, 30C
0.33 - 0.56
Mg-diphosphate
0.22
Mg-UTP
-
UDP-glucose synthesis
0.58 - 1.11
Mg2+
0.56
MgUTP
-
recombinant wild-type enzyme, pH 8.0, 25C
4.5
tripolyphosphate
-
30C, pH 8.0
0.35 - 2
TTP
0.26 - 0.42
UDP-galactose
0.03 - 57
UDP-glucose
0.0075 - 0.53
UTP
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48.81 - 55.03
alpha-D-glucose 1-phosphate
0.033
farnesyl triphosphate
Saccharomyces cerevisiae
-
pH 8.0, 30C
0.038
geranyl triphosphate
Saccharomyces cerevisiae
-
pH 8.0, 30C
0.013
isopentenyl triphosphate
Saccharomyces cerevisiae
-
pH 8.0, 30C
27
methylenebisphosphonate
Saccharomyces cerevisiae
-
pH 8.0, 30C
6.8 - 10
TTP
29.3 - 93.44
UTP
additional information
additional information
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1240
alpha-D-glucose 1-phosphate
Mycobacterium tuberculosis
O05576
-
107
0.103
farnesyl triphosphate
Saccharomyces cerevisiae
-
pH 8.0, 30C
8234
0.181
geranyl triphosphate
Saccharomyces cerevisiae
-
pH 8.0, 30C
8877
0.025
isopentenyl triphosphate
Saccharomyces cerevisiae
-
pH 8.0, 30C
8876
24.55
methylenebisphosphonate
Saccharomyces cerevisiae
-
pH 8.0, 30C
5782
18.3 - 28.3
TTP
183.3 - 7870
UTP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.135
alpha-D-glucose 1-phosphate
-
pH 8.0, 30C
0.213 - 0.95
diphosphate
0.095 - 0.42
MgUTP2-
10.9 - 12.2
phosphate
4.8
UDP-D-galactose
0.21 - 0.93
UDP-D-galacturonic acid
0.005 - 0.13
UDP-D-glucose
0.15 - 0.75
UDP-D-glucuronic acid
9.6
UDP-D-mannose
0.24 - 1.6
UDP-D-xylose
0.015 - 0.12
UDP-glucose
0.104 - 0.17
UTP
additional information
additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
Delta-NB mutant protein
0.02
-
Ncut-37 mutant protein
0.11 - 0.22
-
activity in cell extracts of cells grown on different sugar sources
0.21
-
Ccut-101 mutant protein
0.27
-
Ccut-32 mutant protein
0.42
-
K260A mutant protein
1.57
-
pH 7.5, 80C, substrates: UTP + alpha-D-glucose 1-phosphate
2
-
pH 7.5, 80C, mutant enzyme DC05 (deletion of the C-terminal 5 residues of the ST0452 protein)
2.1
-
Delta 1-4 mutant protein
2.15
-
partially purified Golgi apparatus isozyme
2.2
-
pH 7.5, 80C, wild-type enzyme enzyme
2.6
-
pH 7.5, 80C, mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein)
3.1
-
Ccut-67 mutant protein
3.7
-
mutant H191N, pH 7.8, 25C
3.9
-
partially purified enzyme
4.76
-
partially purified recombinant enzyme
5.4
-
Delta 1-8 mutant protein
7.48
-
pH 7.5, 80C, substrates: diphosphate + UDP-alpha-D-glucose
7.8
-
mutant K95A, pH 7.8, 25C
8.95
-
partially purified enzyme
12.8
-
Ncut-21 mutant protein
15.2
-
purified enzyme
15.8
-
purified enzyme
16
-
purified enzyme
240
-
mutant L281D, pH 7.8, 25C
251
-
pyrophosphorolysis
340
-
UDP-glucose synthesis
385
-
UDP-glucose synthesis
449
-
UDP-glucose synthesis
495
-
purified enzyme
510
-
pyrophosphorolysis
591
-
Y192A mutant protein
715
-
pyrophosphorolysis
752
-
K183A mutant protein
764
-
K405A mutant protein
853
-
K332A mutant protein
899
-
purified enzyme
1074
-
wild-type protein
1099
-
purified enzyme
1200
-
purified enzyme
1477
-
wild-type, pH 7.8, 25C
1547
-
Ccut-8 mutant protein
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
6.5 - 8.5
-
broad optimum in both reaction directions
6.5 - 8
7 - 9.5
-
broad
7 - 10.5
-
broad
7 - 9
-
pyrophosphorolysis
7.3 - 8.6
-
broad
7.5 - 7.6
-
pyrophosphorolysis
7.5 - 9
-
-
7.5
assay at
7.5 - 9
7.6
-
assay at
7.6 - 9.2
-
broad
8
-
assay at
8 - 8.6
-
Golgi membrane and cytosolic isozyme
8 - 9
-
bovine mammary gland, human erythrocytes
8 - 9
-
UDP-glucose synthesis
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 10
-
forward reaction sharp drop in activity above pH 10.0, inactive above pH 10.0 and below pH 4.0, profile overview
5.5 - 9.5
-
reverse reaction, inactive above pH 10.0 and below pH 5.0, profile overview
7 - 9
-
about 75% of maximal activity at pH 7.0 and maximal activity at pH 9.0
7.2 - 9.8
-
about half-maximal activity at pH 7.2 and about 90% of maximal activity at pH 9.8
additional information
-
active over a wide range of pH for both forward and reverse reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
assay at
38
-
assay at