Information on EC 3.6.3.18 - oligosaccharide-transporting ATPase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.3.18
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RECOMMENDED NAME
GeneOntology No.
oligosaccharide-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + oligosaccharide/out = ADP + phosphate + oligosaccharide/in
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (disaccharide-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. A bacterial enzyme that imports lactose, melibiose and raffinose.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain AR50
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Manually annotated by BRENDA team
strain AR50
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Manually annotated by BRENDA team
strain DH5alpha
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Manually annotated by BRENDA team
strain DH5alpha
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
8-azido-ATP + H2O + ?
8-azido-ADP + phosphate + ?
show the reaction diagram
ATP + H2O + ?
ADP + phosphate + ?
show the reaction diagram
ATP + H2O + cellobiose/out
ADP + phosphate + cellobiose/in
show the reaction diagram
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two separate uptake systems for cellobiose and maltose, the ATP-binding component MsiK assists in cellobiose and maltose transport
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?
ATP + H2O + isomaltotriose/out
ADP + phosphate + isomaltotriose/in
show the reaction diagram
ATP + H2O + lactose/out
ADP + phosphate + lactose/in
show the reaction diagram
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
show the reaction diagram
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two separate uptake systems for cellobiose and maltose, the ATP-binding component MsiK assists in cellobiose and maltose transport
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?
ATP + H2O + melibiose/out
ADP + phosphate + melibiose/in
show the reaction diagram
ATP + H2O + raffinose/out
ADP + phosphate + raffinose/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 + isomaltotriose/out
ADP + phosphate + isomaltotriose/in
show the reaction diagram
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the enzyme system is responsible for the uptake of melibiose, raffinose and isomaltotriose
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?
ATP + H2O + lactose/out
ADP + phosphate + lactose/in
show the reaction diagram
ATP + H2O + melibiose/out
ADP + phosphate + melibiose/in
show the reaction diagram
-
the enzyme system is responsible for the uptake of melibiose, raffinose and isomaltotriose
-
?
ATP + H2O + raffinose/out
ADP + phosphate + raffinose/in
show the reaction diagram
-
the enzyme system is responsible for the uptake of melibiose, raffinose and isomaltotriose
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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100% activity at pH 8.0 and with 10 mM KCl
Mn2+
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125% activity at pH 8.0 and with 10 mM KCl
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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3% activity at pH 8.0 and 10 mM KCl
Co2+
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47% activity at pH 8.0 and 10 mM KCl
orthovanadate
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0.005-0.05 mM, pH 8.0, IC50: 0.016 mM
Zn2+
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1% activity at pH 8.0 and 10 mM KCl
additional information
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the activity is reversibly inhibited by high salt concentrations in the physiologically range accompanied by proportional decreased binding of 8-azido-ATP (3-5% residual activity at 200-300 mM salt)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65 - 2.33
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 0.33
ATP
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
orthovanadate
Escherichia coli
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0.005-0.05 mM, pH 8.0, IC50: 0.016 mM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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in the presence of 3 mM MgCl2 and 10 mM KCl
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27500
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HlyB NBD in the presence of 100 mM KCl and ATP, ultracentrifugation
27700
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HlyB NBD in the presence of 10 mM KCl and in the absence of ATP, ultracentrifugation
28000
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His-tagged HlyB ABC domain, gel filtration
30800
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HlyB NBD in the presence of 10 mM KCl and ATP, ultracentrifugation
35700
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HlyB NBD in the absence of KCl and ATP, ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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75% activity in the presence of 3 mM MgCl2 and 10 mM KCl
667495
7.5
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90% activity in the presence of 3 mM MgCl2 and 10 mM KCl
667495
8
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100% activity in the presence of 3 mM MgCl2 and 10 mM KCl
667495
8.5
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85% activity in the presence of 3 mM MgCl2 and 10 mM KCl
667495
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 50 mM phosphate buffer pH 8, 50 mM KCl and 10% glycerol, 15 mg/ml HlyB ABC domain, indefinite storage duration, no loss of activity
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-80C, phosphate or Tris buffer pH 8, in the absence of ATP, up to 25 mg/ml His-tagged HlyB ABC domain, indefinite storage duration, no loss of activity
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25C, 50 mM phosphate buffer pH 8, 50 mM KCl and 10% glycerol, 15 mg/ml HlyB ABC domain, 24h, 20% loss of activity
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4C, 50 mM phosphate buffer pH 8, 50 mM KCl and 10% glycerol, 15 mg/ml HlyB ABC domain, 2 days, no loss of activity
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4C, phosphate or Tris buffer pH 8, in the absence of ATP, up to 25 mg/ml His-tagged HlyB ABC domain, at least 2 days, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HlyB ABC domain, Ni2+-chelating Sepharose 16/20 fast flow column chromatography, His-tagged HlyB ABC domain, immobilized metal-affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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