7.5.2.1: ABC-type maltose transporter
This is an abbreviated version!
For detailed information about ABC-type maltose transporter, go to the full flat file.
Word Map on EC 7.5.2.1
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7.5.2.1
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maltose-binding
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maltodextrins
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outward-facing
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proteoliposomes
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maltotriose
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nanodiscs
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atp-bound
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inward-facing
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atp-binding-cassette
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lager
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q-loops
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eiiaglc
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analysis
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synthesis
- 7.5.2.1
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maltose-binding
- maltodextrins
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outward-facing
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proteoliposomes
- maltotriose
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nanodiscs
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atp-bound
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inward-facing
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atp-binding-cassette
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lager
-
q-loops
- eiiaglc
- analysis
- synthesis
Reaction
Synonyms
ATP phosphohydrolase (maltose-importing), Cg2463, EC 3.6.3.19, GlvC, Mal-EFGK2, Mal11, MalE, MalE-FGK2, MalF, MalFGK2, MalFGK2-E, MalG511, MalK, MalK2, malK3, MalP, MalT, MALT2, MALT4, maltose ABC transporter, maltose ABC transporter MALFGK2-E, maltose ABC-type transporter, maltose ATP binding cassette transporter, maltose ATP-binding cassette importer, maltose ATP-binding cassette transporter, maltose importer, maltose transporter, maltose transporter ATPase, maltose transporter MalFGK2, maltose-specific enzyme IICB, maltose-transporting ATPase, maltose/maltodextrin ABC transporter, More, MuSK, proton-maltose symporter
ECTree
7.5.2.1 ABC-type maltose transporterAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 7.5.2.1 - ABC-type maltose transporter
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
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-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
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-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
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-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
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-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
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-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
P68187; P68183; P02916
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-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
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-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Saccharomyces eubayanus CBS 12357T
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-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Q9X0S9; Q9X2F5
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
Saccharomyces cerevisiae IMK289
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-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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-
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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the putative helical domain of the nucleotide binding domains is involved, through its conformational changes, in the coupling between the transmembrane domains and the ATP binding/hydrolysis at the nucleotide-binding domains
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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the peripheral membrane protein MalK associates with integral cytoplasmic membrane proteins MalF and MalG to form the maltose transport complex MalFGK. In addition malK participates in two different regulatory pathways which modulate mal gene expression and MalFGK transport activity
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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molecular dynamics simulations to study the ATP-driven association of the NBDs of the maltose ABC transporter, MalK, based on the crystal structures of its open and semiopen dimers, MgATP-dependent opening and closure, mechanism, overview
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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extracytoplasmic anchoring of the substrate binding protein, the receptor, is emerging as key determinant for the structural rearrangements in the cytoplasmically exposed ATP-binding cassette domains and in the transmembrane gates during the nucleotide cycle, molecular mechanism, overview
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-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
the MalK dimer complex component provides the energy for maltose transport by hydrolysing ATP
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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maltose transport and ATPase activity of the MalFGK2 complex
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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structure and transport mechanism, overview
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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the transmembrane protein MalF, MalF-P2, of the maltose ATP-binding cassette transporter MalFGK2-E as an important element in the recognition of substrate by the maltose-binding protein MalE. MalF-P2 is not only responsible for substrate recognition, but also directly involved in activation of substrate transport. Substrate transport model for MalFGK2-E, isothermal titration calorimetry and molecular dynamics simulation, overview
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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-
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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translocation of maltose across biological membranes
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?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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signal-transducing protein EIIAGlc interacts with the MalK subunits of the maltose ATP-binding cassette transporter
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-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
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the MalK dimer complex component provides the energy for maltose transport by hydrolysing ATP
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?
additional information
?
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interactions of MalK with the regulatory proteins MalT and enzyme IIAglc
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?
additional information
?
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concomitantly with the three conformations of the ATP-binding cassette MalK2, three functionally relevant conformations are found also in the periplasmic MalF-P2 loop, strictly dependent on cytoplasmic nucleotide-binding and periplasmic docking of liganded MalE to MalFG, overview
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-
?
additional information
?
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MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA
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?
additional information
?
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MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA
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?
additional information
?
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the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. the MalF P2 loop of the ATP-binding cassette transporter MalFGK2 interacts with maltose binding protein MalE throughout the catalytic cycle, overview
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?
additional information
?
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quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK2, of the maltose ATP-binding cassette importer MalFGK2 during the transport cycle, overview
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?
additional information
?
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the periplasmic loop P2 of subunit MalF interacts with the maltose-binding potein MalE independently of the transmembrane region of MalF and MalG in the presence and absence of substrate, overview
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-
?
additional information
?
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the maltose transporter solubilized in detergent micelles hydrolyses ATP independently of the presence of liganded MalE, ATP-induced MalK dimer closure occurs in absence of MalK. The isolated MalK2 domains are also known to exhibit a spontaneous but low ATPase activity
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-
?
additional information
?
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stabilization of the semi-open MalK2 conformation by maltose-bound maltose-binding protein is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP
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-
?
additional information
?
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stabilization of the semi-open MalK2 conformation by maltose-bound maltose-binding protein is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP
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-
?
additional information
?
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the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. the MalF P2 loop of the ATP-binding cassette transporter MalFGK2 interacts with maltose binding protein MalE throughout the catalytic cycle, overview
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-
?
additional information
?
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although MalF and MalG differ in the number of transmembrane segments of 8 and 6, respectively, and their amino acid sequences, both contain the so-called EAA-motif, i.e. L-loop or coupling helix, which is in contact with MalK. MalF and MalG form a large central cavity for transport, but maltose is only bound to MalF. The MalK subunits bind and hydrolyze ATP, thereby generating the power stroke necessary for the rearrangements of MalFG, quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK2, of the maltose ATP-binding cassette importer MalFGK2 during the transport cycle, overview
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-
?
additional information
?
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the maltose transporter solubilized in detergent micelles hydrolyses ATP independently of the presence of liganded MalE, ATP-induced MalK dimer closure occurs in absence of MalK. The isolated MalK2 domains are also known to exhibit a spontaneous but low ATPase activity
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-
?
