Information on EC 3.6.3.17 - monosaccharide-transporting ATPase

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

EC NUMBER
COMMENTARY hide
3.6.3.17
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RECOMMENDED NAME
GeneOntology No.
monosaccharide-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + monosaccharide/out = ADP + phosphate + monosaccharide/in
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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transmembrane transport
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (monosaccharide-importing)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Family of bacterial enzymes importing ribose, xylose, arabinose, galactose and methylgalactoside.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ABC-ATPase of the glucose ABC transport system
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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-galactose/out
ADP + phosphate + D-galactose/in
show the reaction diagram
ATP + H2O + D-glucose/out
ADP + phosphate + D-glucose/in
show the reaction diagram
ATP + H2O + D-ribose/out
ADP + phosphate + D-ribose/in
show the reaction diagram
ATP + H2O + L-arabinose/out
ADP + phosphate + L-arabinose/in
show the reaction diagram
ATP + H2O + monosaccharide/out
ADP + phosphate + monosaccharide/in
show the reaction diagram
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
ATP + H2O + D-galactose/out
ADP + phosphate + D-galactose/in
show the reaction diagram
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uptake of galactose
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?
ATP + H2O + D-glucose/out
ADP + phosphate + D-glucose/in
show the reaction diagram
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uptake of glucose
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?
ATP + H2O + D-ribose/out
ADP + phosphate + D-ribose/in
show the reaction diagram
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periplasmic ribose binding protein RBP is essential for high-affinity D-ribose transport, but this transport system is not necessary for growth on D-ribose as sole carbon source
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?
ATP + H2O + monosaccharide/out
ADP + phosphate + monosaccharide/in
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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ChvE is the periplasmic binding protein of the ABC-type sugar transport operon
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Actinobacillus succinogenes (strain ATCC 55618 / 130Z)
Actinobacillus succinogenes (strain ATCC 55618 / 130Z)
Actinobacillus succinogenes (strain ATCC 55618 / 130Z)
Escherichia coli (strain K12)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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in absence of nucleotide-Mg2+, monomer, gel filtration
60000
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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
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non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 65000, SDS-PAGE
dimer
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binding of ATP and Mg2+ to monomeric GlcV results in the formation of a productive dimer
monomer
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isolated enzyme behaves apparently as a monomer in the presence of ATP-Mg2+, AMPPNP-Mg2+ or ATP alone
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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proteolytic modification
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the L-arabinose binding protein encoded by araF contains a signal peptide that is cleaved upon formation of the mature protein
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
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ChvE, periplasmic binding protein
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E166Q
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mutant lost about 80% of the wild-type activity, it shows dimerization in the presence of ATP-Mg2+ or ATP alone
G144A
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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
G144A |
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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
S142A
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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
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