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Information on EC 7.5.2.B8 - ABC-type D-glucose transporter and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97UY8

for references in articles please use BRENDA:EC7.5.2.B8
preliminary BRENDA-supplied EC number
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Saccharolobus solfataricus
UNIPROT: Q97UY8 not found.
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Saccharolobus solfataricus
Reaction Schemes
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ATP
+
H2O
+
D-glucose-[glucose-binding protein][side 1]
=
ADP
+
phosphate
+
D-glucose[side 2]
+
[glucose-binding protein][side 1]
+
+
D-glucose-[glucose-binding protein][side 1]
=
+
+
+
[glucose-binding protein][side 1]
Synonyms
glucose abc transporter, abc-atpase glcv, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ABC transporter, ATP binding protein (glucose)
-
glucose ABC transporter
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, D-glucose-importing)
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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
ATP + H2O + D-glucose/out
ADP + phosphate + D-glucose/in
show the reaction diagram
ATP + H2O + monosaccharide/out
ADP + phosphate + monosaccharide/in
show the reaction diagram
-
-
-
?
ATP + H2O + D-glucose/out
ADP + phosphate + D-glucose/in
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
ATP + H2O + monosaccharide/out
ADP + phosphate + monosaccharide/in
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
high-resolution structures of the enzyme–ADP-Mg2+ and GlcV–AMPPNP-Mg2+ complexes provide a detailed view of the residues involved in the binding of the nucleotide and the magnesium ion
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
glucose uptake is mediated by an ABC transport system
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
in absence of nucleotide-Mg2+, monomer, gel filtration
60000
dimer, this molecular mass of 60 kDa can be explained by the occurrence of a fast equilibrium between monomeric and dimeric states, gel filtration
65000
non-denaturing PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 65000, SDS-PAGE
dimer
binding of ATP and Mg2+ to monomeric GlcV results in the formation of a productive dimer
monomer
isolated enzyme behaves apparently as a monomer in the presence of ATP-Mg2+, AMPPNP-Mg2+ or ATP alone
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of GlcV could be grown by microseeding in hanging-drop vapour diffusion setups. The crystals appear overnight and grow to final dimensions of 0.1 * 0.05 * 0.45 mm in two weeks at 20°C
Crystals of the G144A mutant are grown by microseeding from wild-type GlcV crystals in hanging-drop vapour-diffusion
high-resolution crystal structures of the enzyme in different states along its catalytic cycle: distinct monomeric nucleotide-free states and monomeric complexes with ADP-Mg2+ as a product-bound state, and with AMPPNP-Mg2+ as an ATP-like bound state. The structure of the enzyme consists of a typical ABC-ATPase domain, comprising two subdomains, connected by a linker region to a C-terminal domain of unknown function
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E166A
mutants shows no significant activity, and shows dimerization in the presence of ATP-Mg2+
E166Q
mutant lost about 80% of the wild-type activity, it shows dimerization in the presence of ATP-Mg2+ or ATP alone
G144A
mutant is completely inactive and fails to dimerize, indicating an essential role of this residue in stabilizing the productive dimeric state. Although the E166A and G144A mutants each alone are inactive, they produce an active heterodimer, showing that disruption of one active site can be tolerated
S142A
mutant retains considerable activity, and is able to dimerize, thus implying that the interaction of the serine with ATP is not essential for dimerization and catalysis. Although the E166A and G144A mutants each alone are inactive, they produce an active heterodimer, showing that disruption of one active site can be tolerated
E166A
-
the wild-type enzyme has a conserved domain structure with two membrane-spanning domains that form the transport channel and two cytosolic nucleotide-binding domains that energize the transport reaction. Binding of ATP to the nucleotide-binding domain monomer results in formation of a nucleotide-binding domain dimer. Hydrolysis of the ATP drives the dissociation of the dimer. The mutant enzymed is defective in dimer dissociation
G144A |
-
the wild-type enzyme has a conserved domain structure with two membrane-spanning domains that form the transport channel and two cytosolic nucleotide-binding domains that energize the transport reaction. Binding of ATP to the nucleotide-binding domain monomer results in formation of a nucleotide-binding domain dimer. Hydrolysis of the ATP drives the dissociation of the dimer. The mutant enzyme is unable to dimerize
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overproduced in Escherichia coli as a soluble protein
wild-type nucleotide-binding domains GlcV and the E166A and G144A mutant are expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Albers, S.V.; Elferink,.MG.; Charlebois, R.L.; Sensen, C.W.; Driessen, A.J.; Konings, W.N.
Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein
J. Bacteriol.
181
4285-4291
1999
Saccharolobus solfataricus (Q97UY8)
Manually annotated by BRENDA team
Verdon, G.; Albers, S.V.; Dijkstra, B.W.; Driessen, A.J.; Thunnissen, A.M.
Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations
J. Mol. Biol.
330
343-358
2003
Saccharolobus solfataricus (Q97UY8), Saccharolobus solfataricus
Manually annotated by BRENDA team
Verdon, G.; Albers, S.V.; van Oosterwijk, N.; Dijkstra, B.W.; Driessen, A.J.; Thunnissen, A.M.
Formation of the productive ATP-Mg2+-bound dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus
J. Mol. Biol.
334
255-267
2003
Saccharolobus solfataricus (Q97UY8), Saccharolobus solfataricus
Manually annotated by BRENDA team
Verdon, G.; Albers, S.V.; Dijkstra, B.W.; Driessen, A.J.; Thunnissen, A.M.
Purification, crystallization and preliminary X-ray diffraction analysis of an archaeal ABC-ATPase
Acta Crystallogr. Sect. D
58
362-365
2002
Saccharolobus solfataricus (Q97UY8), Saccharolobus solfataricus P2 (Q97UY8)
Manually annotated by BRENDA team
Pretz, M.G.; Albers, S.V.; Schuurman-Wolters, G.; Tamp, R.; Driessen, A.J.; van der Does, C.
Thermodynamics of the ATPase cycle of GlcV, the nucleotide-binding domain of the glucose ABC transporter of Sulfolobus solfataricus
Biochemistry
45
15056-15067
2006
Saccharolobus solfataricus
Manually annotated by BRENDA team