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Information on EC 7.3.2.5 - ABC-type molybdate transporter
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7.3.2.5 ABC-type molybdate transporterIUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of molybdate and tungstate. Does not undergo phosphorylation during the transport process.
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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
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molybdate-[molybdate-binding protein][side 1]
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[molybdate-binding protein][side 1]
Synonyms
modabc, molybdate transporter, high-affinity molybdate transporter, modbc, molybdate transport system, molbc-a, molybdate importer, moda/wtpa, wtpabc, molybdenum transporter, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.6.3.29
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formerly
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high-affinity molybdate transporter
low affinity molybdate transporter
ModA
ModA/WtpA
ModABC
ModABC transporter
ModB
ModBC
ModC
MolBC-A
molybdate transport system
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molybdate transporter
molybdate- or tungstate-binding protein
molybdate-transporting ATPase
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molybdate/tungstate ABC transporter
MOP
tungstate/molybdate-binding protein
additional information
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the enzyme belongs to the sulfate transporter superfamily of enzyme
ModABC
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ModABC
Oleidesulfovibrio alaskensis G20
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ModABC
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ModA is a periplasmic molybdatebinding protein, ModB is a transmembrane permease, while ModC is an ATPase that energizes transport on the cytoplasmic side of the membrane
ModABC
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ModA is a periplasmic molybdatebinding protein, ModB is a transmembrane permease, while ModC is an ATPase that energizes transport on the cytoplasmic side of the membrane
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + molybdate-[molybdate-binding protein][side 1] = ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, molybdate-importing)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of molybdate and tungstate. Does not undergo phosphorylation during the transport process.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
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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 + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
ATP + H2O + tungsten/out
ADP + phosphate + tungsten/in
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?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
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?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
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?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
the enzyme is essential for arsenite oxidation
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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two ATP per imported molybdate
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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enzyme is involved in molybdate transport
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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import of molybdate
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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sulfate and phosphate are not effective ligands for ModA
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
the ATPase activity is strictly required
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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molybdate-bound MaModA employs octahedral coordination of its substrate
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Oleidesulfovibrio alaskensis
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Oleidesulfovibrio alaskensis G20
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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import of molybdate
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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enzyme is involved in molybdate transport
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
additional information
?
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MOT1 is required for efficient uptake and translocation of molybdate and for normal growth under conditions of limited molybdate supply
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?
additional information
?
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ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate
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?
additional information
?
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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?
additional information
?
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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?
additional information
?
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component afMolA binds its substrates with high affinity, the affinity toward tungstate is higher. Binding of molybdate by afModA is endothermic, while that of tungstate is exothermic. Reconstitution of the detergent-free enzyme components BCA into liposomes and analysis of interaction between proteins BC and protein A, effects of nucleotides and substrates on the interaction, modeling of the mechanism, overview
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?
additional information
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component afMolA binds its substrates with high affinity, the affinity toward tungstate is higher. Binding of molybdate by afModA is endothermic, while that of tungstate is exothermic. Reconstitution of the detergent-free enzyme components BCA into liposomes and analysis of interaction between proteins BC and protein A, effects of nucleotides and substrates on the interaction, modeling of the mechanism, overview
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?
additional information
?
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ModABC can also transport tungstate
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?
additional information
?
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ModA specifically binds molybdate and tungstate
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?
additional information
?
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mod is primarily a molybdenum transporter that can also transport tungsten, while tup is a tungsten-specific transporter
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?
additional information
?
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ModABC can also transport tungstate and sulfate, while the sulfate/thiosulfate permease, CysPTWA belonging to the sulfate/tungstate uptake transporter SulT family, of Escherichia coli can transport sulfate, chromate, molybdate, and selenate, overview. Molybdate can also be taken up by a non-specific low-efficiency anion transport system that requires high molybdate concentrations, and which also transports sulfate, selenate, and selenite
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?
additional information
?
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ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate with a Kd of ca. 20 nM. ModE functions as a homodimer and binds two molecules of molybdate with high affinity, Kd = 800 nM
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?
additional information
?
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the MolA binding protein binds molybdate and tungstate but not other oxyanions such as sulfate and phosphate, it is thus a class III molybdate binding protein
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?
additional information
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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?
additional information
?
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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?
additional information
?
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component hiMolA binds its substrates with low affinity.Reconstitution of the detergent-free enzyme components BCA into liposomes and analysis of interaction between proteins BC and protein A, effects of nucleotides and substrates on the interaction, overview
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?
additional information
?
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component hiMolA binds its substrates with low affinity.Reconstitution of the detergent-free enzyme components BCA into liposomes and analysis of interaction between proteins BC and protein A, effects of nucleotides and substrates on the interaction, overview
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?
additional information
?
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specific binding of tungstate or molybdate to the two oxyanion pockets at the shared interface of the enzyme subunits prevents ATPase activity and locks the enzyme in the inward-facing conformation, with the actives sites of the nucleotide-binding subunits separated. The allosteric effect prevents the transporter from switchuing between the inward-facing and outward-facing states, thus interfering with the access and release mechanism, overview
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?
additional information
?
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specific binding of tungstate or molybdate to the two oxyanion pockets at the shared interface of the enzyme subunits prevents ATPase activity and locks the enzyme in the inward-facing conformation, with the actives sites of the nucleotide-binding subunits separated. The allosteric effect prevents the transporter from switchuing between the inward-facing and outward-facing states, thus interfering with the access and release mechanism, overview
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?
additional information
?
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ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate, WtpABC transports tungstate and molybdate in Pyrococcus furiosus
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?
additional information
?
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Oleidesulfovibrio alaskensis
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component TupA binds both tungstate and molybdate ions and has no significant interaction with sulfate, phosphate or perchlorate, quantitative analysis of metal binding by isothermal titration calorimetry, overview
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?
additional information
?
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Oleidesulfovibrio alaskensis G20
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component TupA binds both tungstate and molybdate ions and has no significant interaction with sulfate, phosphate or perchlorate, quantitative analysis of metal binding by isothermal titration calorimetry, overview
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?
additional information
?
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sulfate and phosphate have no effect on Mop mobility
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?
additional information
?
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sulfate and phosphate have no effect on Mop mobility
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?
additional information
?
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WtpABC transports tungstate and molybdate in Pyrococcus furiosus, overview
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?
additional information
?
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WtpABC transports tungstate and molybdate in Pyrococcus furiosus
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?
additional information
?
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PerO transports molybdate, sulfate, tungstate, and vanadate in Rhodobacter capsulatus functioning as a general oxyanion transporter
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?
additional information
?
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PerO mediates uptake of molybdate, sulfate, tungstate, and vanadate
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?
additional information
?
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ModABC can also transport tungstate and sulfate, while the sulfate/thiosulfate permease, CysPTWA belonging to the sulfate/tungstate uptake transporter SulT family, of Escherichia coli can transport sulfate, chromate, molybdate, and selenate, overview. Molybdate can also be taken up by a non-specific low-efficiency anion transport system that requires high molybdate concentrations, and which also transports sulfate, selenate, and selenite
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?
additional information
?
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ModA specifically binds Kd of 290 nM for molybdate and 580 nM for tungstate
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?
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NATURAL SUBSTRATE
NATURAL 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 + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
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?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
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?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
the enzyme is essential for arsenite oxidation
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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enzyme is involved in molybdate transport
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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import of molybdate
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
the ATPase activity is strictly required
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Oleidesulfovibrio alaskensis
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Oleidesulfovibrio alaskensis G20
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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import of molybdate
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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enzyme is involved in molybdate transport
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?
additional information
?
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MOT1 is required for efficient uptake and translocation of molybdate and for normal growth under conditions of limited molybdate supply
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?
additional information
?
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ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate
-
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?
additional information
?
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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?
additional information
?
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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?
additional information
?
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ModABC can also transport tungstate
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?
additional information
?
-
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ModABC can also transport tungstate and sulfate, while the sulfate/thiosulfate permease, CysPTWA belonging to the sulfate/tungstate uptake transporter SulT family, of Escherichia coli can transport sulfate, chromate, molybdate, and selenate, overview. Molybdate can also be taken up by a non-specific low-efficiency anion transport system that requires high molybdate concentrations, and which also transports sulfate, selenate, and selenite
-
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?
additional information
?
-
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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?
additional information
?
-
the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
-
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?
additional information
?
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ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate, WtpABC transports tungstate and molybdate in Pyrococcus furiosus
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-
?
additional information
?
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WtpABC transports tungstate and molybdate in Pyrococcus furiosus, overview
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?
additional information
?
-
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PerO transports molybdate, sulfate, tungstate, and vanadate in Rhodobacter capsulatus functioning as a general oxyanion transporter
-
-
?
additional information
?
-
-
ModABC can also transport tungstate and sulfate, while the sulfate/thiosulfate permease, CysPTWA belonging to the sulfate/tungstate uptake transporter SulT family, of Escherichia coli can transport sulfate, chromate, molybdate, and selenate, overview. Molybdate can also be taken up by a non-specific low-efficiency anion transport system that requires high molybdate concentrations, and which also transports sulfate, selenate, and selenite
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
molybdate
specific binding of tungstate or molybdate, involving residues Ser286, Thr320, Ser323, and Lys340, to the two oxyanion pockets at the shared interface of the enzyme subunits prevents ATPase activity and locks the enzyme in the inward-facing conformation, with the actives sites of the nucleotide-binding subunits separated. The allosteric effect prevents the transporter from switchuing between the inward-facing and outward-facing states, thus interfering with the access and release mechanism, overview
Tungsten
specific binding of tungstate or molybdate, involving residues Ser286, Thr320, Ser323, and Lys340, to the two oxyanion pockets at the shared interface of the enzyme subunits prevents ATPase activity and locks the enzyme in the inward-facing conformation, with the actives sites of the nucleotide-binding subunits separated. The allosteric effect prevents the transporter from switchuing between the inward-facing and outward-facing states, thus interfering with the access and release mechanism, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ModE
-
represses molybdenum transport in presence of both molybdenum and tungsten
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additional information
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MOT1 expression in shoots is decreased to 50% of that in plants supplied with sufficient Mo
-
additional information
structural basis of trans-inhibition in a molybdate/tungstate ABC transporter, overvciew
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additional information
-
structural basis of trans-inhibition in a molybdate/tungstate ABC transporter, overvciew
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
MOT1 expression in roots is slightly but significantly reduced under Mo limitation
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections